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2h89_IF10317.pdb
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2h89_IF10317.pdb
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HEADER Entry: 2h89 InterfaceID: 1 3/7/2022
Remark 300 Interface Chain A For Asymmetric Chain A Author Chain A Entity 1 Symmetry Operator 1_555 Full Symmetry Operator X,Y,Z
Remark 300 Interface Chain B For Asymmetric Chain B Author Chain B Entity 2 Symmetry Operator 1_555 Full Symmetry Operator X,Y,Z
Remark 300 Ligand Info
Remark 300 Interface Chain A For Asymmetric Chain DB Author Chain A Entity 15 Symmetry Operator 1_555
Remark 300 Name water Sequence - PDB Sequence Number 1018-1309 Author Sequence Number 1018-1309
Remark 300 Interface Chain A For Asymmetric Chain E Author Chain A Entity 5 Symmetry Operator 1_555
Remark 300 Name POTASSIUM ION Sequence K PDB Sequence Number 622 Author Sequence Number 622
Remark 300 Interface Chain A For Asymmetric Chain F Author Chain A Entity 6 Symmetry Operator 1_555
Remark 300 Name FLAVIN-ADENINE DINUCLEOTIDE Sequence FAD PDB Sequence Number 1001 Author Sequence Number 1001
Remark 300 Interface Chain A For Asymmetric Chain G Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name MALONATE ION Sequence MLI PDB Sequence Number 1002 Author Sequence Number 1002
Remark 300 Interface Chain A For Asymmetric Chain H Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1003 Author Sequence Number 1003
Remark 300 Interface Chain A For Asymmetric Chain I Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1004 Author Sequence Number 1004
Remark 300 Interface Chain A For Asymmetric Chain J Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1005 Author Sequence Number 1005
Remark 300 Interface Chain A For Asymmetric Chain K Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1006 Author Sequence Number 1006
Remark 300 Interface Chain A For Asymmetric Chain L Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1007 Author Sequence Number 1007
Remark 300 Interface Chain A For Asymmetric Chain M Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1008 Author Sequence Number 1008
Remark 300 Interface Chain A For Asymmetric Chain N Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1009 Author Sequence Number 1009
Remark 300 Interface Chain A For Asymmetric Chain O Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1010 Author Sequence Number 1010
Remark 300 Interface Chain A For Asymmetric Chain P Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1011 Author Sequence Number 1011
Remark 300 Interface Chain A For Asymmetric Chain Q Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1012 Author Sequence Number 1012
Remark 300 Interface Chain A For Asymmetric Chain R Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1013 Author Sequence Number 1013
Remark 300 Interface Chain A For Asymmetric Chain S Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1014 Author Sequence Number 1014
Remark 300 Interface Chain A For Asymmetric Chain T Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1015 Author Sequence Number 1015
Remark 300 Interface Chain A For Asymmetric Chain U Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1016 Author Sequence Number 1016
Remark 300 Interface Chain A For Asymmetric Chain V Author Chain A Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1017 Author Sequence Number 1017
Remark 300 Interface Chain B For Asymmetric Chain AA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1005 Author Sequence Number 1005
Remark 300 Interface Chain B For Asymmetric Chain BA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1006 Author Sequence Number 1006
Remark 300 Interface Chain B For Asymmetric Chain CA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1007 Author Sequence Number 1007
Remark 300 Interface Chain B For Asymmetric Chain DA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1008 Author Sequence Number 1008
Remark 300 Interface Chain B For Asymmetric Chain EA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1009 Author Sequence Number 1009
Remark 300 Interface Chain B For Asymmetric Chain EB Author Chain B Entity 15 Symmetry Operator 1_555
Remark 300 Name water Sequence - PDB Sequence Number 1015-1180 Author Sequence Number 1015-1180
Remark 300 Interface Chain B For Asymmetric Chain FA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1010 Author Sequence Number 1010
Remark 300 Interface Chain B For Asymmetric Chain GA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1011 Author Sequence Number 1011
Remark 300 Interface Chain B For Asymmetric Chain HA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1012 Author Sequence Number 1012
Remark 300 Interface Chain B For Asymmetric Chain IA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1013 Author Sequence Number 1013
Remark 300 Interface Chain B For Asymmetric Chain JA Author Chain B Entity 8 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1014 Author Sequence Number 1014
Remark 300 Interface Chain B For Asymmetric Chain W Author Chain B Entity 5 Symmetry Operator 1_555
Remark 300 Name POTASSIUM ION Sequence K PDB Sequence Number 253 Author Sequence Number 253
Remark 300 Interface Chain B For Asymmetric Chain X Author Chain B Entity 9 Symmetry Operator 1_555
Remark 300 Name FE2/S2 (INORGANIC) CLUSTER Sequence FES PDB Sequence Number 1002 Author Sequence Number 1002
Remark 300 Interface Chain B For Asymmetric Chain Y Author Chain B Entity 10 Symmetry Operator 1_555
Remark 300 Name IRON/SULFUR CLUSTER Sequence SF4 PDB Sequence Number 1003 Author Sequence Number 1003
Remark 300 Interface Chain B For Asymmetric Chain Z Author Chain B Entity 11 Symmetry Operator 1_555
Remark 300 Name FE3-S4 CLUSTER Sequence F3S PDB Sequence Number 1004 Author Sequence Number 1004
Remark 350 Interface surface area: 2506.1
SEQRES 1 A 621 SER THR LYS VAL SER ASP SER ILE SER THR GLN TYR PRO
SEQRES 2 A 621 VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY ALA
SEQRES 3 A 621 GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER GLU
SEQRES 4 A 621 ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE PRO
SEQRES 5 A 621 THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE ASN
SEQRES 6 A 621 ALA ALA LEU GLY ASN MET GLU ASP ASP ASN TRP ARG TRP
SEQRES 7 A 621 HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU GLY
SEQRES 8 A 621 ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA PRO
SEQRES 9 A 621 ALA ALA VAL ILE GLU LEU GLU ASN TYR GLY MET PRO PHE
SEQRES 10 A 621 SER ARG THR GLU GLU GLY LYS ILE TYR GLN ARG ALA PHE
SEQRES 11 A 621 GLY GLY GLN SER LEU GLN PHE GLY LYS GLY GLY GLN ALA
SEQRES 12 A 621 HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS SER
SEQRES 13 A 621 LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR ASP
SEQRES 14 A 621 THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU LEU
SEQRES 15 A 621 MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU CYS
SEQRES 16 A 621 ILE GLU ASP GLY THR ILE HIS ARG PHE ARG ALA LYS ASN
SEQRES 17 A 621 THR VAL ILE ALA THR GLY GLY TYR GLY ARG THR TYR PHE
SEQRES 18 A 621 SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY THR
SEQRES 19 A 621 ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP LEU
SEQRES 20 A 621 GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY ALA
SEQRES 21 A 621 GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY GLY
SEQRES 22 A 621 ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU ARG
SEQRES 23 A 621 TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP VAL
SEQRES 24 A 621 VAL SER ARG SER MET THR ILE GLU ILE ARG GLU GLY ARG
SEQRES 25 A 621 GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN LEU
SEQRES 26 A 621 HIS HIS LEU PRO PRO GLN GLN LEU ALA THR ARG LEU PRO
SEQRES 27 A 621 GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL ASP
SEQRES 28 A 621 VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL HIS
SEQRES 29 A 621 TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY GLN
SEQRES 30 A 621 VAL ILE THR HIS VAL ASN GLY GLU ASP LYS VAL VAL PRO
SEQRES 31 A 621 GLY LEU TYR ALA CYS GLY GLU ALA ALA SER ALA SER VAL
SEQRES 32 A 621 HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU ASP
SEQRES 33 A 621 LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU THR ILE ALA
SEQRES 34 A 621 GLU THR CYS LYS PRO GLY GLU PRO VAL PRO SER ILE LYS
SEQRES 35 A 621 PRO ASN ALA GLY GLU GLU SER VAL ALA ASN LEU ASP LYS
SEQRES 36 A 621 LEU ARG PHE ALA ASP GLY THR ILE ARG THR SER GLU ALA
SEQRES 37 A 621 ARG LEU ASN MET GLN LYS THR MET GLN SER HIS ALA ALA
SEQRES 38 A 621 VAL PHE ARG THR GLY SER ILE LEU GLN GLU GLY CYS GLU
SEQRES 39 A 621 LYS LEU SER GLN ILE TYR ARG ASP LEU ALA HIS LEU LYS
SEQRES 40 A 621 THR PHE ASP ARG GLY ILE VAL TRP ASN THR ASP LEU VAL
SEQRES 41 A 621 GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA LEU
SEQRES 42 A 621 GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER ARG
SEQRES 43 A 621 GLY ALA HIS ALA ARG GLU ASP TYR LYS LEU ARG ILE ASP
SEQRES 44 A 621 GLU PHE ASP TYR SER LYS PRO LEU GLN GLY GLN GLN LYS
SEQRES 45 A 621 ARG PRO PHE GLU GLU HIS TRP ARG LYS HIS THR LEU SER
SEQRES 46 A 621 TYR VAL ASP VAL LYS SER GLY LYS VAL THR LEU LYS TYR
SEQRES 47 A 621 ARG PRO VAL ILE ASP ARG THR LEU ASN GLU GLU ASP CYS
SEQRES 48 A 621 SER SER VAL PRO PRO ALA ILE ARG SER TYR
SEQRES 1 B 252 ALA GLN THR ALA ALA ALA ALA THR SER ARG ILE LYS LYS
SEQRES 2 B 252 PHE SER ILE TYR ARG TRP ASP PRO ASP LYS PRO GLY ASP
SEQRES 3 B 252 LYS PRO ARG MET GLN THR TYR GLU VAL ASP LEU ASN LYS
SEQRES 4 B 252 CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS
SEQRES 5 B 252 ASN GLU LEU ASP SER THR LEU THR PHE ARG ARG SER CYS
SEQRES 6 B 252 ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ALA
SEQRES 7 B 252 GLY GLY ASN THR LEU ALA CYS THR LYS LYS ILE ASP PRO
SEQRES 8 B 252 ASP LEU SER LYS THR THR LYS ILE TYR PRO LEU PRO HIS
SEQRES 9 B 252 MET TYR VAL VAL LYS ASP LEU VAL PRO ASP LEU SER ASN
SEQRES 10 B 252 PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS
SEQRES 11 B 252 LYS LYS ASP GLU SER LYS GLN GLY LYS GLU GLN TYR LEU
SEQRES 12 B 252 GLN SER ILE GLU ASP ARG GLN LYS LEU ASP GLY LEU TYR
SEQRES 13 B 252 GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO
SEQRES 14 B 252 SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA
SEQRES 15 B 252 VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG
SEQRES 16 B 252 ASP ASP TYR THR GLU GLU ARG LEU ALA GLN LEU GLN ASP
SEQRES 17 B 252 PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS
SEQRES 18 B 252 THR ARG THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA
SEQRES 19 B 252 ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU
SEQRES 20 B 252 LYS ALA ALA ALA ALA
ATOM 1 CA SER A 9 55.502 36.851 118.388 1.00 97.20 C
ATOM 2 N THR A 10 53.092 39.261 118.985 1.00122.39 N
ATOM 3 CA THR A 10 51.786 38.743 118.594 1.00122.28 C
ATOM 4 C THR A 10 51.660 38.675 117.071 1.00120.92 C
ATOM 5 O THR A 10 51.550 39.698 116.390 1.00121.35 O
ATOM 6 CB THR A 10 50.638 39.618 119.175 1.00123.56 C
ATOM 7 OG1 THR A 10 49.373 39.045 118.822 1.00124.25 O
ATOM 8 CG2 THR A 10 50.713 41.047 118.640 1.00124.24 C
ATOM 9 N GLN A 11 51.683 37.457 116.541 1.00118.91 N
ATOM 10 CA GLN A 11 51.576 37.242 115.102 1.00115.67 C
ATOM 11 C GLN A 11 50.112 36.975 114.749 1.00112.34 C
ATOM 12 O GLN A 11 49.748 36.821 113.577 1.00111.55 O
ATOM 13 CB GLN A 11 52.474 36.070 114.701 1.00117.51 C
ATOM 14 CG GLN A 11 53.844 36.150 115.374 1.00119.88 C
ATOM 15 CD GLN A 11 54.810 35.074 114.928 1.00121.06 C
ATOM 16 OE1 GLN A 11 55.883 34.920 115.511 1.00122.47 O
ATOM 17 NE2 GLN A 11 54.444 34.330 113.888 1.00121.69 N
ATOM 18 N TYR A 12 49.284 36.925 115.790 1.00106.49 N
ATOM 19 CA TYR A 12 47.852 36.719 115.656 1.00 99.63 C
ATOM 20 C TYR A 12 47.158 37.890 116.336 1.00 99.82 C
ATOM 21 O TYR A 12 47.614 38.374 117.370 1.00 98.80 O
ATOM 22 CB TYR A 12 47.412 35.433 116.346 1.00 92.31 C
ATOM 23 CG TYR A 12 47.933 34.176 115.717 1.00 84.77 C
ATOM 24 CD1 TYR A 12 49.256 33.792 115.876 1.00 82.16 C
ATOM 25 CD2 TYR A 12 47.098 33.361 114.967 1.00 81.64 C
ATOM 26 CE1 TYR A 12 49.734 32.625 115.303 1.00 80.30 C
ATOM 27 CE2 TYR A 12 47.565 32.193 114.391 1.00 79.37 C
ATOM 28 CZ TYR A 12 48.879 31.830 114.561 1.00 78.98 C
ATOM 29 OH TYR A 12 49.339 30.666 113.994 1.00 80.94 O
ATOM 30 N PRO A 13 46.053 38.372 115.753 1.00100.09 N
ATOM 31 CA PRO A 13 45.304 39.493 116.330 1.00 98.73 C
ATOM 32 C PRO A 13 44.347 38.997 117.420 1.00 96.79 C
ATOM 33 O PRO A 13 43.679 37.967 117.258 1.00 94.76 O
ATOM 34 CB PRO A 13 44.572 40.067 115.121 1.00100.34 C
ATOM 35 CG PRO A 13 44.264 38.830 114.326 1.00101.71 C
ATOM 36 CD PRO A 13 45.561 38.045 114.401 1.00100.63 C
ATOM 37 N VAL A 14 44.282 39.731 118.527 1.00 94.73 N
ATOM 38 CA VAL A 14 43.420 39.347 119.642 1.00 92.51 C
ATOM 39 C VAL A 14 42.301 40.349 119.937 1.00 90.85 C
ATOM 40 O VAL A 14 42.554 41.543 120.091 1.00 90.92 O
ATOM 41 CB VAL A 14 44.245 39.158 120.932 1.00 91.50 C
ATOM 42 CG1 VAL A 14 43.413 38.445 121.979 1.00 91.85 C
ATOM 43 CG2 VAL A 14 45.508 38.378 120.630 1.00 92.31 C
ATOM 44 N VAL A 15 41.067 39.852 120.014 1.00 88.68 N
ATOM 45 CA VAL A 15 39.911 40.690 120.308 1.00 84.64 C
ATOM 46 C VAL A 15 39.325 40.243 121.639 1.00 84.42 C
ATOM 47 O VAL A 15 38.968 39.075 121.804 1.00 84.44 O
ATOM 48 CB VAL A 15 38.824 40.558 119.226 1.00 84.69 C
ATOM 49 CG1 VAL A 15 37.615 41.398 119.604 1.00 82.80 C
ATOM 50 CG2 VAL A 15 39.372 40.990 117.878 1.00 81.27 C
ATOM 51 N ASP A 16 39.241 41.176 122.585 1.00 82.91 N
ATOM 52 CA ASP A 16 38.707 40.889 123.914 1.00 82.15 C
ATOM 53 C ASP A 16 37.227 41.233 123.998 1.00 79.69 C
ATOM 54 O ASP A 16 36.818 42.331 123.619 1.00 78.95 O
ATOM 55 CB ASP A 16 39.471 41.684 124.987 1.00 86.20 C
ATOM 56 CG ASP A 16 40.885 41.160 125.222 1.00 89.58 C
ATOM 57 OD1 ASP A 16 41.032 39.972 125.587 1.00 88.89 O
ATOM 58 OD2 ASP A 16 41.850 41.938 125.048 1.00 92.48 O
ATOM 59 N HIS A 17 36.434 40.291 124.508 1.00 77.51 N
ATOM 60 CA HIS A 17 34.985 40.475 124.655 1.00 73.50 C
ATOM 61 C HIS A 17 34.608 40.542 126.129 1.00 73.76 C
ATOM 62 O HIS A 17 35.180 39.826 126.948 1.00 76.10 O
ATOM 63 CB HIS A 17 34.239 39.318 123.994 1.00 67.50 C
ATOM 64 CG HIS A 17 34.507 39.186 122.529 1.00 62.43 C
ATOM 65 ND1 HIS A 17 33.938 40.019 121.591 1.00 62.55 N
ATOM 66 CD2 HIS A 17 35.291 38.324 121.840 1.00 65.28 C
ATOM 67 CE1 HIS A 17 34.359 39.673 120.387 1.00 64.55 C
ATOM 68 NE2 HIS A 17 35.181 38.647 120.510 1.00 64.63 N
ATOM 69 N GLU A 18 33.646 41.396 126.464 1.00 72.76 N
ATOM 70 CA GLU A 18 33.215 41.549 127.845 1.00 73.03 C
ATOM 71 C GLU A 18 31.757 41.161 128.029 1.00 72.51 C
ATOM 72 O GLU A 18 30.870 41.831 127.512 1.00 74.36 O
ATOM 73 CB GLU A 18 33.406 42.997 128.298 1.00 76.72 C
ATOM 74 CG GLU A 18 34.855 43.419 128.503 1.00 84.64 C
ATOM 75 CD GLU A 18 34.990 44.875 128.951 1.00 90.86 C
ATOM 76 OE1 GLU A 18 34.319 45.262 129.936 1.00 91.67 O
ATOM 77 OE2 GLU A 18 35.773 45.628 128.322 1.00 93.79 O
ATOM 78 N PHE A 19 31.509 40.083 128.768 1.00 70.34 N
ATOM 79 CA PHE A 19 30.141 39.627 129.027 1.00 66.81 C
ATOM 80 C PHE A 19 29.921 39.302 130.495 1.00 66.72 C
ATOM 81 O PHE A 19 30.879 39.066 131.244 1.00 67.88 O
ATOM 82 CB PHE A 19 29.806 38.364 128.220 1.00 60.57 C
ATOM 83 CG PHE A 19 29.725 38.585 126.745 1.00 57.97 C
ATOM 84 CD1 PHE A 19 30.876 38.635 125.969 1.00 56.34 C
ATOM 85 CD2 PHE A 19 28.486 38.748 126.123 1.00 59.50 C
ATOM 86 CE1 PHE A 19 30.800 38.841 124.591 1.00 52.18 C
ATOM 87 CE2 PHE A 19 28.395 38.956 124.753 1.00 54.37 C
ATOM 88 CZ PHE A 19 29.562 39.001 123.984 1.00 56.93 C
ATOM 89 N ASP A 20 28.652 39.296 130.902 1.00 66.10 N
ATOM 90 CA ASP A 20 28.302 38.943 132.270 1.00 62.01 C
ATOM 91 C ASP A 20 28.687 37.486 132.442 1.00 60.85 C
ATOM 92 O ASP A 20 29.321 37.127 133.438 1.00 60.24 O
ATOM 93 CB ASP A 20 26.802 39.112 132.526 1.00 62.10 C
ATOM 94 CG ASP A 20 26.410 40.561 132.724 1.00 63.71 C
ATOM 95 OD1 ASP A 20 27.336 41.381 132.936 1.00 61.12 O
ATOM 96 OD2 ASP A 20 25.190 40.877 132.678 1.00 58.68 O
ATOM 97 N ALA A 21 28.308 36.658 131.461 1.00 59.56 N
ATOM 98 CA ALA A 21 28.617 35.220 131.467 1.00 57.18 C
ATOM 99 C ALA A 21 28.895 34.660 130.064 1.00 54.12 C
ATOM 100 O ALA A 21 28.431 35.198 129.061 1.00 51.40 O
ATOM 101 CB ALA A 21 27.474 34.433 132.126 1.00 58.18 C
ATOM 102 N VAL A 22 29.658 33.569 130.015 1.00 53.71 N
ATOM 103 CA VAL A 22 30.019 32.905 128.760 1.00 50.43 C
ATOM 104 C VAL A 22 29.604 31.445 128.743 1.00 47.05 C
ATOM 105 O VAL A 22 29.915 30.714 129.671 1.00 48.42 O
ATOM 106 CB VAL A 22 31.536 32.927 128.524 1.00 48.37 C
ATOM 107 CG1 VAL A 22 31.865 32.212 127.217 1.00 44.32 C
ATOM 108 CG2 VAL A 22 32.035 34.355 128.499 1.00 50.33 C
ATOM 109 N VAL A 23 28.923 31.021 127.680 1.00 48.17 N
ATOM 110 CA VAL A 23 28.479 29.627 127.541 1.00 45.34 C
ATOM 111 C VAL A 23 29.283 28.951 126.465 1.00 41.34 C
ATOM 112 O VAL A 23 29.404 29.481 125.365 1.00 38.08 O
ATOM 113 CB VAL A 23 27.000 29.509 127.104 1.00 47.38 C
ATOM 114 CG1 VAL A 23 26.625 28.037 126.971 1.00 45.81 C
ATOM 115 CG2 VAL A 23 26.089 30.201 128.110 1.00 50.50 C
ATOM 116 N VAL A 24 29.818 27.776 126.767 1.00 40.80 N
ATOM 117 CA VAL A 24 30.599 27.049 125.772 1.00 42.97 C
ATOM 118 C VAL A 24 29.919 25.753 125.369 1.00 40.53 C
ATOM 119 O VAL A 24 29.889 24.795 126.131 1.00 41.29 O
ATOM 120 CB VAL A 24 32.039 26.716 126.271 1.00 43.68 C
ATOM 121 CG1 VAL A 24 32.801 25.972 125.190 1.00 35.94 C
ATOM 122 CG2 VAL A 24 32.774 27.988 126.652 1.00 40.59 C
ATOM 123 N GLY A 25 29.382 25.745 124.155 1.00 41.76 N
ATOM 124 CA GLY A 25 28.700 24.573 123.630 1.00 44.31 C
ATOM 125 C GLY A 25 27.241 24.888 123.352 1.00 43.65 C
ATOM 126 O GLY A 25 26.591 25.544 124.176 1.00 44.83 O
ATOM 127 N ALA A 26 26.716 24.429 122.216 1.00 41.13 N
ATOM 128 CA ALA A 26 25.314 24.698 121.882 1.00 39.66 C
ATOM 129 C ALA A 26 24.525 23.452 121.553 1.00 40.24 C
ATOM 130 O ALA A 26 23.830 23.371 120.541 1.00 39.97 O
ATOM 131 CB ALA A 26 25.198 25.696 120.742 1.00 37.65 C
ATOM 132 N GLY A 27 24.666 22.458 122.406 1.00 38.88 N
ATOM 133 CA GLY A 27 23.871 21.260 122.235 1.00 40.63 C
ATOM 134 C GLY A 27 22.703 21.452 123.197 1.00 36.67 C
ATOM 135 O GLY A 27 22.303 22.589 123.481 1.00 32.32 O
ATOM 136 N GLY A 28 22.173 20.356 123.725 1.00 38.40 N
ATOM 137 CA GLY A 28 21.063 20.471 124.655 1.00 41.67 C
ATOM 138 C GLY A 28 21.393 21.354 125.845 1.00 43.22 C
ATOM 139 O GLY A 28 20.758 22.393 126.090 1.00 45.48 O
ATOM 140 N ALA A 29 22.396 20.934 126.598 1.00 41.38 N
ATOM 141 CA ALA A 29 22.825 21.666 127.773 1.00 38.65 C
ATOM 142 C ALA A 29 23.140 23.125 127.464 1.00 39.63 C
ATOM 143 O ALA A 29 22.614 24.035 128.111 1.00 41.09 O
ATOM 144 CB ALA A 29 24.036 20.981 128.368 1.00 41.41 C
ATOM 145 N GLY A 30 23.992 23.342 126.466 1.00 41.97 N
ATOM 146 CA GLY A 30 24.393 24.691 126.081 1.00 41.65 C
ATOM 147 C GLY A 30 23.295 25.706 125.802 1.00 41.03 C
ATOM 148 O GLY A 30 23.210 26.770 126.437 1.00 37.63 O
ATOM 149 N LEU A 31 22.448 25.389 124.832 1.00 43.40 N
ATOM 150 CA LEU A 31 21.375 26.294 124.483 1.00 43.40 C
ATOM 151 C LEU A 31 20.523 26.640 125.698 1.00 40.98 C
ATOM 152 O LEU A 31 20.226 27.816 125.937 1.00 43.04 O
ATOM 153 CB LEU A 31 20.512 25.688 123.373 1.00 46.68 C
ATOM 154 CG LEU A 31 21.184 25.486 122.009 1.00 48.02 C
ATOM 155 CD1 LEU A 31 20.221 24.799 121.041 1.00 49.34 C
ATOM 156 CD2 LEU A 31 21.619 26.828 121.448 1.00 49.53 C
ATOM 157 N ARG A 32 20.153 25.634 126.479 1.00 37.39 N
ATOM 158 CA ARG A 32 19.308 25.868 127.653 1.00 39.23 C
ATOM 159 C ARG A 32 19.905 26.753 128.760 1.00 40.17 C
ATOM 160 O ARG A 32 19.175 27.430 129.488 1.00 35.89 O
ATOM 161 CB ARG A 32 18.884 24.538 128.265 1.00 38.81 C
ATOM 162 CG ARG A 32 17.761 24.705 129.275 1.00 41.01 C
ATOM 163 CD ARG A 32 16.480 25.160 128.590 1.00 39.88 C
ATOM 164 NE ARG A 32 15.414 25.464 129.537 1.00 40.16 N
ATOM 165 CZ ARG A 32 15.403 26.535 130.323 1.00 42.73 C
ATOM 166 NH1 ARG A 32 16.397 27.414 130.277 1.00 42.58 N
ATOM 167 NH2 ARG A 32 14.410 26.719 131.171 1.00 41.49 N
ATOM 168 N ALA A 33 21.228 26.739 128.903 1.00 43.14 N
ATOM 169 CA ALA A 33 21.869 27.554 129.933 1.00 43.55 C
ATOM 170 C ALA A 33 22.053 28.952 129.384 1.00 42.92 C
ATOM 171 O ALA A 33 21.915 29.944 130.105 1.00 46.99 O
ATOM 172 CB ALA A 33 23.230 26.961 130.324 1.00 47.18 C
ATOM 173 N ALA A 34 22.356 29.020 128.093 1.00 43.02 N
ATOM 174 CA ALA A 34 22.572 30.284 127.420 1.00 40.73 C
ATOM 175 C ALA A 34 21.321 31.153 127.430 1.00 41.75 C
ATOM 176 O ALA A 34 21.343 32.245 127.999 1.00 43.64 O
ATOM 177 CB ALA A 34 23.044 30.034 126.013 1.00 39.44 C
ATOM 178 N PHE A 35 20.215 30.703 126.835 1.00 43.45 N
ATOM 179 CA PHE A 35 19.045 31.572 126.879 1.00 44.96 C
ATOM 180 C PHE A 35 18.413 31.618 128.254 1.00 47.56 C
ATOM 181 O PHE A 35 17.601 32.488 128.532 1.00 52.82 O
ATOM 182 CB PHE A 35 18.022 31.263 125.758 1.00 44.86 C
ATOM 183 CG PHE A 35 17.168 30.035 125.965 1.00 45.74 C
ATOM 184 CD1 PHE A 35 16.059 30.068 126.816 1.00 45.65 C
ATOM 185 CD2 PHE A 35 17.404 28.875 125.211 1.00 43.79 C
ATOM 186 CE1 PHE A 35 15.195 28.965 126.903 1.00 48.07 C
ATOM 187 CE2 PHE A 35 16.547 27.768 125.290 1.00 43.24 C
ATOM 188 CZ PHE A 35 15.442 27.810 126.132 1.00 44.79 C
ATOM 189 N GLY A 36 18.798 30.708 129.137 1.00 46.29 N
ATOM 190 CA GLY A 36 18.248 30.785 130.473 1.00 48.50 C
ATOM 191 C GLY A 36 18.847 32.030 131.122 1.00 52.03 C
ATOM 192 O GLY A 36 18.157 32.805 131.792 1.00 51.10 O
ATOM 193 N LEU A 37 20.146 32.229 130.916 1.00 50.14 N
ATOM 194 CA LEU A 37 20.815 33.392 131.470 1.00 52.07 C
ATOM 195 C LEU A 37 20.244 34.674 130.869 1.00 54.31 C
ATOM 196 O LEU A 37 19.801 35.551 131.596 1.00 58.23 O
ATOM 197 CB LEU A 37 22.321 33.309 131.217 1.00 52.23 C
ATOM 198 CG LEU A 37 22.994 32.178 131.995 1.00 49.82 C
ATOM 199 CD1 LEU A 37 24.426 31.981 131.566 1.00 48.56 C
ATOM 200 CD2 LEU A 37 22.922 32.523 133.467 1.00 54.30 C
ATOM 201 N SER A 38 20.248 34.794 129.549 1.00 56.52 N
ATOM 202 CA SER A 38 19.695 35.986 128.916 1.00 60.70 C
ATOM 203 C SER A 38 18.251 36.198 129.358 1.00 62.62 C
ATOM 204 O SER A 38 17.776 37.325 129.444 1.00 63.62 O
ATOM 205 CB SER A 38 19.762 35.866 127.399 1.00 61.66 C
ATOM 206 OG SER A 38 21.027 36.296 126.926 1.00 68.04 O
ATOM 207 N GLU A 39 17.555 35.104 129.635 1.00 63.87 N
ATOM 208 CA GLU A 39 16.183 35.180 130.098 1.00 65.19 C
ATOM 209 C GLU A 39 16.190 35.804 131.495 1.00 67.56 C
ATOM 210 O GLU A 39 15.185 36.346 131.946 1.00 68.01 O
ATOM 211 CB GLU A 39 15.585 33.777 130.137 1.00 65.99 C
ATOM 212 CG GLU A 39 14.321 33.625 130.972 1.00 71.37 C
ATOM 213 CD GLU A 39 13.812 32.179 131.015 1.00 74.23 C
ATOM 214 OE1 GLU A 39 14.616 31.269 131.351 1.00 73.85 O
ATOM 215 OE2 GLU A 39 12.610 31.965 130.718 1.00 71.08 O
ATOM 216 N ALA A 40 17.334 35.735 132.174 1.00 68.75 N
ATOM 217 CA ALA A 40 17.471 36.296 133.524 1.00 68.44 C
ATOM 218 C ALA A 40 18.070 37.712 133.572 1.00 67.92 C
ATOM 219 O ALA A 40 18.266 38.278 134.650 1.00 68.14 O
ATOM 220 CB ALA A 40 18.295 35.357 134.394 1.00 67.70 C
ATOM 221 N GLY A 41 18.371 38.278 132.408 1.00 67.36 N
ATOM 222 CA GLY A 41 18.908 39.625 132.374 1.00 63.62 C
ATOM 223 C GLY A 41 20.401 39.767 132.153 1.00 63.47 C
ATOM 224 O GLY A 41 20.881 40.882 131.961 1.00 64.45 O
ATOM 225 N PHE A 42 21.153 38.672 132.174 1.00 58.71 N
ATOM 226 CA PHE A 42 22.593 38.798 131.972 1.00 57.64 C
ATOM 227 C PHE A 42 22.958 38.917 130.492 1.00 58.89 C
ATOM 228 O PHE A 42 22.217 38.477 129.610 1.00 58.15 O
ATOM 229 CB PHE A 42 23.343 37.608 132.576 1.00 54.93 C
ATOM 230 CG PHE A 42 23.064 37.373 134.033 1.00 50.59 C
ATOM 231 CD1 PHE A 42 21.811 36.938 134.459 1.00 49.12 C
ATOM 232 CD2 PHE A 42 24.075 37.536 134.977 1.00 47.99 C
ATOM 233 CE1 PHE A 42 21.572 36.665 135.799 1.00 42.35 C
ATOM 234 CE2 PHE A 42 23.851 37.264 136.320 1.00 44.75 C
ATOM 235 CZ PHE A 42 22.589 36.825 136.731 1.00 44.04 C
ATOM 236 N ASN A 43 24.110 39.520 130.227 1.00 61.18 N
ATOM 237 CA ASN A 43 24.577 39.688 128.862 1.00 62.06 C
ATOM 238 C ASN A 43 25.388 38.432 128.570 1.00 63.27 C
ATOM 239 O ASN A 43 26.587 38.351 128.848 1.00 65.04 O
ATOM 240 CB ASN A 43 25.431 40.954 128.747 1.00 62.95 C
ATOM 241 CG ASN A 43 25.667 41.369 127.311 1.00 64.58 C
ATOM 242 OD1 ASN A 43 24.792 41.219 126.460 1.00 68.11 O
ATOM 243 ND2 ASN A 43 26.847 41.913 127.036 1.00 64.01 N
ATOM 244 N THR A 44 24.701 37.443 128.018 1.00 61.61 N
ATOM 245 CA THR A 44 25.297 36.159 127.712 1.00 58.62 C
ATOM 246 C THR A 44 25.939 36.088 126.346 1.00 57.98 C
ATOM 247 O THR A 44 25.558 36.801 125.425 1.00 59.79 O
ATOM 248 CB THR A 44 24.233 35.083 127.795 1.00 56.63 C
ATOM 249 OG1 THR A 44 23.458 35.308 128.978 1.00 58.41 O
ATOM 250 CG2 THR A 44 24.860 33.704 127.844 1.00 54.52 C
ATOM 251 N ALA A 45 26.924 35.209 126.231 1.00 57.86 N
ATOM 252 CA ALA A 45 27.639 34.980 124.979 1.00 55.78 C
ATOM 253 C ALA A 45 27.761 33.466 124.823 1.00 53.14 C
ATOM 254 O ALA A 45 28.205 32.791 125.749 1.00 53.61 O
ATOM 255 CB ALA A 45 29.025 35.619 125.035 1.00 53.90 C
ATOM 256 N CYS A 46 27.349 32.930 123.675 1.00 52.00 N
ATOM 257 CA CYS A 46 27.433 31.487 123.438 1.00 50.03 C
ATOM 258 C CYS A 46 28.479 31.211 122.372 1.00 49.73 C
ATOM 259 O CYS A 46 28.391 31.710 121.248 1.00 52.71 O
ATOM 260 CB CYS A 46 26.077 30.919 123.003 1.00 50.27 C
ATOM 261 SG CYS A 46 25.975 29.086 122.936 1.00 57.89 S
ATOM 262 N VAL A 47 29.475 30.415 122.744 1.00 48.42 N
ATOM 263 CA VAL A 47 30.571 30.050 121.861 1.00 42.30 C
ATOM 264 C VAL A 47 30.440 28.568 121.547 1.00 42.34 C
ATOM 265 O VAL A 47 30.386 27.740 122.449 1.00 46.58 O
ATOM 266 CB VAL A 47 31.904 30.337 122.557 1.00 42.35 C
ATOM 267 CG1 VAL A 47 33.065 29.749 121.783 1.00 39.67 C
ATOM 268 CG2 VAL A 47 32.065 31.835 122.700 1.00 44.39 C
ATOM 269 N THR A 48 30.384 28.234 120.265 1.00 36.81 N
ATOM 270 CA THR A 48 30.222 26.856 119.853 1.00 35.44 C
ATOM 271 C THR A 48 31.088 26.638 118.631 1.00 37.62 C
ATOM 272 O THR A 48 31.360 27.583 117.898 1.00 35.79 O
ATOM 273 CB THR A 48 28.702 26.557 119.543 1.00 34.28 C
ATOM 274 OG1 THR A 48 28.569 25.364 118.753 1.00 27.51 O
ATOM 275 CG2 THR A 48 28.069 27.728 118.813 1.00 31.43 C
ATOM 276 N LYS A 49 31.521 25.406 118.393 1.00 38.29 N
ATOM 277 CA LYS A 49 32.379 25.175 117.238 1.00 41.66 C
ATOM 278 C LYS A 49 31.576 24.676 116.058 1.00 43.35 C
ATOM 279 O LYS A 49 32.093 24.516 114.944 1.00 44.35 O
ATOM 280 CB LYS A 49 33.496 24.180 117.582 1.00 42.77 C
ATOM 281 CG LYS A 49 33.008 22.789 117.912 1.00 43.88 C
ATOM 282 CD LYS A 49 34.172 21.841 118.086 1.00 45.55 C
ATOM 283 CE LYS A 49 33.702 20.399 118.197 1.00 43.47 C
ATOM 284 NZ LYS A 49 34.860 19.472 118.351 1.00 45.35 N
ATOM 285 N LEU A 50 30.305 24.412 116.314 1.00 42.34 N
ATOM 286 CA LEU A 50 29.413 23.946 115.270 1.00 41.83 C
ATOM 287 C LEU A 50 28.202 24.851 115.287 1.00 42.27 C
ATOM 288 O LEU A 50 27.967 25.565 116.263 1.00 44.56 O
ATOM 289 CB LEU A 50 28.951 22.516 115.545 1.00 39.47 C
ATOM 290 CG LEU A 50 29.958 21.380 115.494 1.00 39.60 C
ATOM 291 CD1 LEU A 50 29.315 20.100 115.994 1.00 42.83 C
ATOM 292 CD2 LEU A 50 30.443 21.225 114.078 1.00 42.39 C
ATOM 293 N PHE A 51 27.449 24.847 114.197 1.00 42.54 N
ATOM 294 CA PHE A 51 26.217 25.615 114.164 1.00 39.21 C
ATOM 295 C PHE A 51 25.370 24.779 115.138 1.00 36.44 C
ATOM 296 O PHE A 51 25.346 23.543 115.063 1.00 35.84 O
ATOM 297 CB PHE A 51 25.615 25.634 112.743 1.00 37.17 C
ATOM 298 CG PHE A 51 24.349 26.433 112.636 1.00 35.80 C
ATOM 299 CD1 PHE A 51 24.368 27.818 112.817 1.00 35.70 C
ATOM 300 CD2 PHE A 51 23.115 25.788 112.476 1.00 32.31 C
ATOM 301 CE1 PHE A 51 23.168 28.552 112.851 1.00 40.77 C
ATOM 302 CE2 PHE A 51 21.911 26.506 112.511 1.00 33.34 C
ATOM 303 CZ PHE A 51 21.932 27.890 112.700 1.00 35.55 C
ATOM 304 N PRO A 52 24.697 25.442 116.084 1.00 35.54 N
ATOM 305 CA PRO A 52 23.867 24.771 117.078 1.00 36.68 C
ATOM 306 C PRO A 52 23.198 23.476 116.667 1.00 39.85 C
ATOM 307 O PRO A 52 23.431 22.442 117.283 1.00 45.96 O
ATOM 308 CB PRO A 52 22.865 25.845 117.460 1.00 34.01 C
ATOM 309 CG PRO A 52 23.715 27.070 117.426 1.00 33.40 C
ATOM 310 CD PRO A 52 24.488 26.902 116.141 1.00 37.06 C
ATOM 311 N THR A 53 22.378 23.514 115.627 1.00 37.52 N
ATOM 312 CA THR A 53 21.664 22.317 115.231 1.00 35.84 C
ATOM 313 C THR A 53 22.491 21.112 114.761 1.00 35.96 C
ATOM 314 O THR A 53 21.927 20.052 114.517 1.00 33.16 O
ATOM 315 CB THR A 53 20.603 22.660 114.165 1.00 38.82 C
ATOM 316 OG1 THR A 53 21.204 23.464 113.138 1.00 42.52 O
ATOM 317 CG2 THR A 53 19.417 23.428 114.802 1.00 25.99 C
ATOM 318 N ARG A 54 23.816 21.255 114.653 1.00 36.05 N
ATOM 319 CA ARG A 54 24.653 20.142 114.194 1.00 34.67 C
ATOM 320 C ARG A 54 25.187 19.294 115.340 1.00 37.07 C
ATOM 321 O ARG A 54 25.773 18.239 115.102 1.00 39.27 O
ATOM 322 CB ARG A 54 25.842 20.637 113.361 1.00 32.45 C
ATOM 323 CG ARG A 54 25.523 21.692 112.294 1.00 36.60 C
ATOM 324 CD ARG A 54 24.616 21.230 111.150 1.00 38.25 C
ATOM 325 NE ARG A 54 24.456 22.296 110.156 1.00 38.29 N
ATOM 326 CZ ARG A 54 23.404 22.461 109.352 1.00 35.26 C
ATOM 327 NH1 ARG A 54 22.374 21.626 109.392 1.00 37.43 N
ATOM 328 NH2 ARG A 54 23.367 23.491 108.521 1.00 35.36 N
ATOM 329 N SER A 55 24.974 19.751 116.576 1.00 38.96 N
ATOM 330 CA SER A 55 25.423 19.064 117.787 1.00 36.14 C
ATOM 331 C SER A 55 25.010 17.600 117.881 1.00 41.98 C
ATOM 332 O SER A 55 23.957 17.198 117.362 1.00 46.04 O
ATOM 333 CB SER A 55 24.889 19.805 118.994 1.00 35.51 C
ATOM 334 OG SER A 55 25.275 21.162 118.914 1.00 44.20 O
ATOM 335 N HIS A 56 25.814 16.793 118.572 1.00 40.35 N
ATOM 336 CA HIS A 56 25.484 15.373 118.686 1.00 39.30 C
ATOM 337 C HIS A 56 24.123 15.117 119.297 1.00 36.93 C
ATOM 338 O HIS A 56 23.578 14.039 119.094 1.00 36.82 O
ATOM 339 CB HIS A 56 26.530 14.594 119.493 1.00 34.14 C
ATOM 340 CG HIS A 56 26.376 13.105 119.385 1.00 34.50 C
ATOM 341 ND1 HIS A 56 26.497 12.430 118.189 1.00 33.64 N
ATOM 342 CD2 HIS A 56 26.109 12.160 120.324 1.00 35.61 C
ATOM 343 CE1 HIS A 56 26.315 11.135 118.395 1.00 31.83 C
ATOM 344 NE2 HIS A 56 26.077 10.944 119.683 1.00 34.85 N
ATOM 345 N THR A 57 23.591 16.080 120.054 1.00 37.92 N
ATOM 346 CA THR A 57 22.270 15.924 120.688 1.00 42.86 C
ATOM 347 C THR A 57 21.180 15.602 119.653 1.00 41.32 C
ATOM 348 O THR A 57 20.323 14.770 119.890 1.00 43.51 O
ATOM 349 CB THR A 57 21.831 17.187 121.455 1.00 41.95 C
ATOM 350 OG1 THR A 57 22.731 17.457 122.539 1.00 38.78 O
ATOM 351 CG2 THR A 57 20.440 16.968 122.022 1.00 45.92 C
ATOM 352 N VAL A 58 21.261 16.254 118.498 1.00 43.09 N
ATOM 353 CA VAL A 58 20.341 16.073 117.373 1.00 44.17 C
ATOM 354 C VAL A 58 20.251 14.636 116.846 1.00 39.77 C
ATOM 355 O VAL A 58 19.380 14.302 116.055 1.00 42.29 O
ATOM 356 CB VAL A 58 20.772 16.978 116.184 1.00 49.69 C
ATOM 357 CG1 VAL A 58 21.924 16.324 115.395 1.00 51.55 C
ATOM 358 CG2 VAL A 58 19.599 17.248 115.276 1.00 53.37 C
ATOM 359 N ALA A 59 21.158 13.787 117.279 1.00 39.04 N
ATOM 360 CA ALA A 59 21.178 12.420 116.812 1.00 37.95 C
ATOM 361 C ALA A 59 20.458 11.500 117.768 1.00 38.30 C
ATOM 362 O ALA A 59 20.234 10.341 117.445 1.00 38.40 O
ATOM 363 CB ALA A 59 22.609 11.964 116.660 1.00 38.34 C
ATOM 364 N ALA A 60 20.129 11.998 118.957 1.00 37.67 N
ATOM 365 CA ALA A 60 19.444 11.172 119.957 1.00 43.24 C
ATOM 366 C ALA A 60 18.072 10.654 119.469 1.00 44.95 C
ATOM 367 O ALA A 60 17.320 11.378 118.791 1.00 41.13 O
ATOM 368 CB ALA A 60 19.309 11.945 121.276 1.00 43.88 C
ATOM 369 N GLN A 61 17.746 9.407 119.824 1.00 45.23 N
ATOM 370 CA GLN A 61 16.510 8.796 119.360 1.00 46.83 C
ATOM 371 C GLN A 61 15.449 8.422 120.388 1.00 48.62 C
ATOM 372 O GLN A 61 14.348 8.972 120.369 1.00 49.21 O
ATOM 373 CB GLN A 61 16.843 7.547 118.545 1.00 49.75 C
ATOM 374 CG GLN A 61 18.213 7.558 117.909 1.00 52.46 C
ATOM 375 CD GLN A 61 18.446 6.351 117.021 1.00 53.73 C
ATOM 376 OE1 GLN A 61 18.047 5.229 117.350 1.00 55.68 O
ATOM 377 NE2 GLN A 61 19.106 6.572 115.894 1.00 51.11 N
ATOM 378 N GLY A 62 15.790 7.459 121.249 1.00 51.19 N
ATOM 379 CA GLY A 62 14.899 6.928 122.282 1.00 50.19 C
ATOM 380 C GLY A 62 13.929 7.813 123.048 1.00 48.26 C
ATOM 381 O GLY A 62 12.713 7.648 122.941 1.00 52.35 O
ATOM 382 N GLY A 63 14.448 8.724 123.861 1.00 46.51 N
ATOM 383 CA GLY A 63 13.562 9.602 124.597 1.00 46.59 C
ATOM 384 C GLY A 63 14.168 10.343 125.767 1.00 46.89 C
ATOM 385 O GLY A 63 15.388 10.440 125.921 1.00 49.96 O
ATOM 386 N ILE A 64 13.290 10.873 126.604 1.00 44.62 N
ATOM 387 CA ILE A 64 13.707 11.594 127.784 1.00 43.66 C
ATOM 388 C ILE A 64 12.692 11.220 128.861 1.00 46.12 C
ATOM 389 O ILE A 64 11.485 11.433 128.688 1.00 47.23 O
ATOM 390 CB ILE A 64 13.739 13.131 127.516 1.00 40.62 C
ATOM 391 CG1 ILE A 64 14.215 13.867 128.771 1.00 40.10 C
ATOM 392 CG2 ILE A 64 12.369 13.610 127.001 1.00 42.58 C
ATOM 393 CD1 ILE A 64 14.228 15.389 128.650 1.00 31.33 C
ATOM 394 N ASN A 65 13.194 10.629 129.947 1.00 45.06 N
ATOM 395 CA ASN A 65 12.373 10.171 131.064 1.00 48.09 C
ATOM 396 C ASN A 65 11.763 11.262 131.942 1.00 49.20 C
ATOM 397 O ASN A 65 12.393 12.278 132.234 1.00 52.40 O
ATOM 398 CB ASN A 65 13.176 9.228 131.971 1.00 47.18 C
ATOM 399 CG ASN A 65 13.716 7.998 131.232 1.00 51.39 C
ATOM 400 OD1 ASN A 65 12.962 7.250 130.589 1.00 41.97 O
ATOM 401 ND2 ASN A 65 15.036 7.777 131.338 1.00 52.80 N
ATOM 402 N ALA A 66 10.530 11.013 132.375 1.00 47.65 N
ATOM 403 CA ALA A 66 9.784 11.920 133.237 1.00 44.85 C
ATOM 404 C ALA A 66 8.588 11.138 133.773 1.00 45.11 C
ATOM 405 O ALA A 66 7.972 10.358 133.043 1.00 45.02 O
ATOM 406 CB ALA A 66 9.313 13.143 132.444 1.00 44.79 C
ATOM 407 N ALA A 67 8.267 11.340 135.048 1.00 43.73 N
ATOM 408 CA ALA A 67 7.155 10.649 135.677 1.00 45.20 C
ATOM 409 C ALA A 67 5.821 11.376 135.437 1.00 49.08 C
ATOM 410 O ALA A 67 5.166 11.818 136.378 1.00 50.47 O
ATOM 411 CB ALA A 67 7.424 10.511 137.162 1.00 40.49 C
ATOM 412 N LEU A 68 5.417 11.487 134.175 1.00 49.62 N
ATOM 413 CA LEU A 68 4.174 12.173 133.837 1.00 52.26 C
ATOM 414 C LEU A 68 2.894 11.399 134.144 1.00 53.24 C
ATOM 415 O LEU A 68 1.888 11.992 134.535 1.00 50.13 O
ATOM 416 CB LEU A 68 4.168 12.577 132.360 1.00 49.30 C
ATOM 417 CG LEU A 68 5.068 13.741 131.986 1.00 50.97 C
ATOM 418 CD1 LEU A 68 4.682 14.198 130.598 1.00 52.90 C
ATOM 419 CD2 LEU A 68 4.903 14.874 132.985 1.00 49.52 C
ATOM 420 N GLY A 69 2.926 10.087 133.941 1.00 55.92 N
ATOM 421 CA GLY A 69 1.752 9.273 134.211 1.00 55.57 C
ATOM 422 C GLY A 69 0.722 9.243 133.093 1.00 55.30 C
ATOM 423 O GLY A 69 -0.450 8.960 133.330 1.00 56.55 O
ATOM 424 N ASN A 70 1.156 9.520 131.872 1.00 53.28 N
ATOM 425 CA ASN A 70 0.253 9.509 130.731 1.00 53.01 C
ATOM 426 C ASN A 70 -0.048 8.093 130.258 1.00 55.58 C
ATOM 427 O ASN A 70 -0.911 7.879 129.405 1.00 59.85 O
ATOM 428 CB ASN A 70 0.871 10.294 129.586 1.00 43.76 C
ATOM 429 CG ASN A 70 1.109 11.707 129.945 1.00 33.76 C
ATOM 430 OD1 ASN A 70 1.104 12.062 131.118 1.00 38.36 O
ATOM 431 ND2 ASN A 70 1.330 12.539 128.949 1.00 42.53 N
ATOM 432 N MET A 71 0.662 7.122 130.804 1.00 55.74 N
ATOM 433 CA MET A 71 0.449 5.745 130.394 1.00 59.45 C
ATOM 434 C MET A 71 -0.040 4.880 131.559 1.00 61.52 C
ATOM 435 O MET A 71 -0.624 3.813 131.356 1.00 61.49 O
ATOM 436 CB MET A 71 1.749 5.192 129.804 1.00 58.59 C
ATOM 437 CG MET A 71 2.402 6.128 128.774 1.00 57.54 C
ATOM 438 SD MET A 71 1.398 6.491 127.297 1.00 56.63 S
ATOM 439 CE MET A 71 1.309 4.794 126.563 1.00 50.68 C
ATOM 440 N GLU A 72 0.188 5.365 132.777 1.00 63.46 N
ATOM 441 CA GLU A 72 -0.229 4.677 133.994 1.00 67.06 C
ATOM 442 C GLU A 72 0.187 5.552 135.188 1.00 67.84 C
ATOM 443 O GLU A 72 0.921 6.524 135.013 1.00 69.31 O
ATOM 444 CB GLU A 72 0.438 3.296 134.067 1.00 66.64 C
ATOM 445 CG GLU A 72 1.957 3.328 134.201 1.00 71.92 C
ATOM 446 CD GLU A 72 2.654 2.402 133.216 1.00 75.69 C
ATOM 447 OE1 GLU A 72 2.114 1.305 132.957 1.00 78.57 O
ATOM 448 OE2 GLU A 72 3.743 2.763 132.711 1.00 74.45 O
ATOM 449 N ASP A 73 -0.291 5.229 136.386 1.00 66.45 N
ATOM 450 CA ASP A 73 0.079 6.009 137.566 1.00 66.80 C
ATOM 451 C ASP A 73 1.583 5.859 137.790 1.00 63.58 C
ATOM 452 O ASP A 73 2.122 4.757 137.700 1.00 60.47 O
ATOM 453 CB ASP A 73 -0.675 5.511 138.805 1.00 70.79 C
ATOM 454 CG ASP A 73 -2.193 5.568 138.639 1.00 77.03 C
ATOM 455 OD1 ASP A 73 -2.733 6.684 138.475 1.00 80.56 O
ATOM 456 OD2 ASP A 73 -2.849 4.497 138.679 1.00 77.45 O
ATOM 457 N ASP A 74 2.256 6.971 138.078 1.00 60.43 N
ATOM 458 CA ASP A 74 3.696 6.950 138.298 1.00 55.82 C
ATOM 459 C ASP A 74 4.067 7.786 139.530 1.00 53.35 C
ATOM 460 O ASP A 74 3.204 8.429 140.132 1.00 53.87 O
ATOM 461 CB ASP A 74 4.417 7.489 137.048 1.00 55.75 C
ATOM 462 CG ASP A 74 5.830 6.930 136.899 1.00 56.27 C
ATOM 463 OD1 ASP A 74 6.239 6.160 137.791 1.00 53.21 O
ATOM 464 OD2 ASP A 74 6.526 7.250 135.901 1.00 52.49 O
ATOM 465 N ASN A 75 5.344 7.753 139.906 1.00 48.53 N
ATOM 466 CA ASN A 75 5.849 8.514 141.046 1.00 47.60 C
ATOM 467 C ASN A 75 7.323 8.872 140.731 1.00 49.25 C
ATOM 468 O ASN A 75 8.157 7.984 140.489 1.00 45.08 O
ATOM 469 CB ASN A 75 5.745 7.656 142.308 1.00 46.46 C
ATOM 470 CG ASN A 75 5.720 8.477 143.602 1.00 49.77 C
ATOM 471 OD1 ASN A 75 6.610 9.289 143.876 1.00 42.17 O
ATOM 472 ND2 ASN A 75 4.695 8.242 144.416 1.00 50.24 N
ATOM 473 N TRP A 76 7.640 10.167 140.714 1.00 48.45 N
ATOM 474 CA TRP A 76 9.000 10.587 140.397 1.00 49.79 C
ATOM 475 C TRP A 76 10.022 9.971 141.335 1.00 49.48 C
ATOM 476 O TRP A 76 11.206 9.934 141.022 1.00 50.16 O
ATOM 477 CB TRP A 76 9.150 12.126 140.400 1.00 51.50 C
ATOM 478 CG TRP A 76 9.142 12.811 141.773 1.00 54.22 C
ATOM 479 CD1 TRP A 76 8.093 13.477 142.356 1.00 53.67 C
ATOM 480 CD2 TRP A 76 10.228 12.884 142.717 1.00 52.11 C
ATOM 481 NE1 TRP A 76 8.459 13.950 143.595 1.00 49.72 N
ATOM 482 CE2 TRP A 76 9.760 13.599 143.841 1.00 49.38 C
ATOM 483 CE3 TRP A 76 11.549 12.414 142.721 1.00 53.38 C
ATOM 484 CZ2 TRP A 76 10.561 13.853 144.954 1.00 47.24 C
ATOM 485 CZ3 TRP A 76 12.348 12.674 143.842 1.00 51.68 C
ATOM 486 CH2 TRP A 76 11.844 13.384 144.936 1.00 48.00 C
ATOM 487 N ARG A 77 9.571 9.487 142.483 1.00 48.53 N
ATOM 488 CA ARG A 77 10.490 8.870 143.422 1.00 47.53 C
ATOM 489 C ARG A 77 10.877 7.467 142.954 1.00 48.77 C
ATOM 490 O ARG A 77 11.975 6.984 143.246 1.00 49.67 O
ATOM 491 CB ARG A 77 9.872 8.842 144.810 1.00 42.67 C
ATOM 492 CG ARG A 77 9.639 10.227 145.346 1.00 39.90 C
ATOM 493 CD ARG A 77 8.941 10.209 146.692 1.00 44.03 C
ATOM 494 NE ARG A 77 8.402 11.524 147.041 1.00 42.60 N
ATOM 495 CZ ARG A 77 7.347 12.091 146.450 1.00 43.58 C
ATOM 496 NH1 ARG A 77 6.694 11.454 145.477 1.00 34.19 N
ATOM 497 NH2 ARG A 77 6.966 13.319 146.812 1.00 40.15 N
ATOM 498 N TRP A 78 9.982 6.805 142.231 1.00 51.67 N
ATOM 499 CA TRP A 78 10.303 5.481 141.707 1.00 51.98 C
ATOM 500 C TRP A 78 11.352 5.685 140.601 1.00 52.72 C
ATOM 501 O TRP A 78 12.231 4.848 140.413 1.00 51.44 O
ATOM 502 CB TRP A 78 9.056 4.806 141.130 1.00 52.45 C
ATOM 503 CG TRP A 78 7.950 4.677 142.113 1.00 52.62 C
ATOM 504 CD1 TRP A 78 8.025 4.878 143.458 1.00 56.99 C
ATOM 505 CD2 TRP A 78 6.590 4.333 141.835 1.00 55.06 C
ATOM 506 NE1 TRP A 78 6.794 4.687 144.044 1.00 55.80 N
ATOM 507 CE2 TRP A 78 5.892 4.352 143.069 1.00 57.42 C
ATOM 508 CE3 TRP A 78 5.886 4.015 140.664 1.00 56.82 C
ATOM 509 CZ2 TRP A 78 4.520 4.065 143.165 1.00 55.87 C
ATOM 510 CZ3 TRP A 78 4.517 3.729 140.761 1.00 57.14 C
ATOM 511 CH2 TRP A 78 3.854 3.758 142.005 1.00 56.51 C
ATOM 512 N HIS A 79 11.251 6.809 139.885 1.00 49.85 N
ATOM 513 CA HIS A 79 12.191 7.151 138.817 1.00 47.82 C
ATOM 514 C HIS A 79 13.566 7.368 139.460 1.00 48.34 C
ATOM 515 O HIS A 79 14.591 6.931 138.949 1.00 47.28 O
ATOM 516 CB HIS A 79 11.731 8.436 138.116 1.00 45.79 C
ATOM 517 CG HIS A 79 12.551 8.812 136.920 1.00 43.41 C
ATOM 518 ND1 HIS A 79 12.649 10.109 136.468 1.00 44.81 N
ATOM 519 CD2 HIS A 79 13.321 8.069 136.093 1.00 43.40 C
ATOM 520 CE1 HIS A 79 13.448 10.151 135.419 1.00 43.45 C
ATOM 521 NE2 HIS A 79 13.871 8.925 135.173 1.00 43.32 N
ATOM 522 N PHE A 80 13.558 8.059 140.591 1.00 52.00 N
ATOM 523 CA PHE A 80 14.757 8.337 141.362 1.00 56.94 C
ATOM 524 C PHE A 80 15.426 7.018 141.677 1.00 57.78 C
ATOM 525 O PHE A 80 16.605 6.824 141.393 1.00 59.81 O
ATOM 526 CB PHE A 80 14.387 9.019 142.684 1.00 59.05 C
ATOM 527 CG PHE A 80 15.478 8.960 143.728 1.00 59.17 C
ATOM 528 CD1 PHE A 80 16.539 9.876 143.708 1.00 58.56 C
ATOM 529 CD2 PHE A 80 15.438 7.998 144.735 1.00 57.09 C
ATOM 530 CE1 PHE A 80 17.545 9.841 144.683 1.00 54.72 C
ATOM 531 CE2 PHE A 80 16.433 7.951 145.712 1.00 55.89 C
ATOM 532 CZ PHE A 80 17.490 8.879 145.686 1.00 57.00 C
ATOM 533 N TYR A 81 14.656 6.129 142.293 1.00 57.83 N
ATOM 534 CA TYR A 81 15.134 4.805 142.675 1.00 58.99 C
ATOM 535 C TYR A 81 15.852 4.104 141.529 1.00 56.78 C
ATOM 536 O TYR A 81 16.970 3.611 141.676 1.00 56.40 O
ATOM 537 CB TYR A 81 13.951 3.943 143.115 1.00 59.37 C
ATOM 538 CG TYR A 81 14.314 2.516 143.446 1.00 57.97 C
ATOM 539 CD1 TYR A 81 14.855 2.182 144.680 1.00 56.43 C
ATOM 540 CD2 TYR A 81 14.133 1.500 142.508 1.00 59.26 C
ATOM 541 CE1 TYR A 81 15.209 0.867 144.975 1.00 58.31 C
ATOM 542 CE2 TYR A 81 14.485 0.185 142.793 1.00 57.90 C
ATOM 543 CZ TYR A 81 15.021 -0.124 144.025 1.00 57.30 C
ATOM 544 OH TYR A 81 15.369 -1.423 144.307 1.00 58.72 O
ATOM 545 N ASP A 82 15.191 4.064 140.382 1.00 56.85 N
ATOM 546 CA ASP A 82 15.740 3.398 139.215 1.00 57.61 C
ATOM 547 C ASP A 82 17.152 3.879 138.900 1.00 57.34 C
ATOM 548 O ASP A 82 18.071 3.072 138.730 1.00 55.95 O
ATOM 549 CB ASP A 82 14.808 3.587 137.996 1.00 55.41 C
ATOM 550 CG ASP A 82 13.451 2.856 138.157 1.00 56.74 C
ATOM 551 OD1 ASP A 82 13.397 1.852 138.911 1.00 57.14 O
ATOM 552 OD2 ASP A 82 12.447 3.276 137.520 1.00 52.09 O
ATOM 553 N THR A 83 17.319 5.196 138.844 1.00 56.68 N
ATOM 554 CA THR A 83 18.609 5.800 138.534 1.00 56.83 C
ATOM 555 C THR A 83 19.703 5.503 139.581 1.00 58.74 C
ATOM 556 O THR A 83 20.868 5.308 139.227 1.00 59.02 O
ATOM 557 CB THR A 83 18.456 7.327 138.357 1.00 53.66 C
ATOM 558 OG1 THR A 83 17.455 7.595 137.365 1.00 50.86 O
ATOM 559 CG2 THR A 83 19.770 7.947 137.904 1.00 48.83 C
ATOM 560 N VAL A 84 19.340 5.461 140.859 1.00 57.15 N
ATOM 561 CA VAL A 84 20.322 5.172 141.898 1.00 56.71 C
ATOM 562 C VAL A 84 20.805 3.721 141.777 1.00 58.83 C
ATOM 563 O VAL A 84 22.011 3.434 141.854 1.00 58.75 O
ATOM 564 CB VAL A 84 19.729 5.388 143.312 1.00 54.64 C
ATOM 565 CG1 VAL A 84 20.668 4.816 144.359 1.00 53.07 C
ATOM 566 CG2 VAL A 84 19.514 6.858 143.569 1.00 46.58 C
ATOM 567 N LYS A 85 19.859 2.805 141.601 1.00 59.31 N
ATOM 568 CA LYS A 85 20.201 1.398 141.455 1.00 60.05 C
ATOM 569 C LYS A 85 20.968 1.284 140.155 1.00 60.37 C
ATOM 570 O LYS A 85 21.944 0.538 140.055 1.00 60.46 O
ATOM 571 CB LYS A 85 18.936 0.536 141.387 1.00 62.82 C
ATOM 572 CG LYS A 85 19.195 -0.967 141.212 1.00 63.17 C
ATOM 573 CD LYS A 85 17.882 -1.747 141.145 1.00 63.27 C
ATOM 574 CE LYS A 85 18.100 -3.213 140.774 1.00 64.04 C
ATOM 575 NZ LYS A 85 16.811 -3.949 140.553 1.00 63.89 N
ATOM 576 N GLY A 86 20.508 2.037 139.161 1.00 57.63 N
ATOM 577 CA GLY A 86 21.161 2.029 137.876 1.00 56.41 C
ATOM 578 C GLY A 86 22.633 2.361 138.020 1.00 59.35 C
ATOM 579 O GLY A 86 23.483 1.651 137.498 1.00 60.68 O
ATOM 580 N SER A 87 22.946 3.427 138.748 1.00 60.81 N
ATOM 581 CA SER A 87 24.334 3.846 138.906 1.00 61.99 C
ATOM 582 C SER A 87 25.144 3.006 139.884 1.00 61.56 C
ATOM 583 O SER A 87 26.079 3.510 140.492 1.00 63.94 O
ATOM 584 CB SER A 87 24.397 5.324 139.323 1.00 61.09 C
ATOM 585 OG SER A 87 23.954 5.524 140.655 1.00 57.75 O
ATOM 586 N ASP A 88 24.794 1.733 140.034 1.00 60.49 N
ATOM 587 CA ASP A 88 25.518 0.847 140.944 1.00 59.25 C
ATOM 588 C ASP A 88 26.068 1.623 142.146 1.00 57.83 C
ATOM 589 O ASP A 88 27.232 1.471 142.528 1.00 56.40 O
ATOM 590 CB ASP A 88 26.677 0.181 140.203 1.00 60.63 C
ATOM 591 CG ASP A 88 26.977 -1.215 140.721 1.00 62.35 C
ATOM 592 OD1 ASP A 88 26.897 -1.431 141.946 1.00 64.40 O
ATOM 593 OD2 ASP A 88 27.302 -2.097 139.899 1.00 63.88 O
ATOM 594 N TRP A 89 25.223 2.480 142.711 1.00 57.90 N
ATOM 595 CA TRP A 89 25.561 3.309 143.875 1.00 57.50 C
ATOM 596 C TRP A 89 26.801 4.189 143.777 1.00 59.00 C
ATOM 597 O TRP A 89 27.484 4.412 144.785 1.00 57.33 O
ATOM 598 CB TRP A 89 25.638 2.445 145.146 1.00 55.42 C
ATOM 599 CG TRP A 89 24.273 2.149 145.685 1.00 53.55 C
ATOM 600 CD1 TRP A 89 23.528 2.950 146.496 1.00 52.35 C
ATOM 601 CD2 TRP A 89 23.408 1.085 145.270 1.00 51.70 C
ATOM 602 NE1 TRP A 89 22.247 2.465 146.599 1.00 51.31 N
ATOM 603 CE2 TRP A 89 22.145 1.321 145.853 1.00 51.05 C
ATOM 604 CE3 TRP A 89 23.575 -0.044 144.447 1.00 53.09 C
ATOM 605 CZ2 TRP A 89 21.051 0.474 145.640 1.00 47.26 C
ATOM 606 CZ3 TRP A 89 22.480 -0.890 144.234 1.00 45.96 C
ATOM 607 CH2 TRP A 89 21.239 -0.621 144.829 1.00 47.36 C
ATOM 608 N LEU A 90 27.084 4.703 142.578 1.00 57.87 N
ATOM 609 CA LEU A 90 28.237 5.586 142.403 1.00 58.61 C
ATOM 610 C LEU A 90 27.723 6.991 142.129 1.00 57.12 C
ATOM 611 O LEU A 90 28.484 7.966 142.120 1.00 55.17 O
ATOM 612 CB LEU A 90 29.141 5.130 141.244 1.00 56.81 C
ATOM 613 CG LEU A 90 30.409 5.987 141.071 1.00 56.93 C
ATOM 614 CD1 LEU A 90 31.341 5.785 142.260 1.00 58.95 C
ATOM 615 CD2 LEU A 90 31.123 5.617 139.793 1.00 57.69 C
ATOM 616 N GLY A 91 26.414 7.085 141.926 1.00 56.82 N
ATOM 617 CA GLY A 91 25.810 8.373 141.643 1.00 55.40 C
ATOM 618 C GLY A 91 25.456 9.159 142.884 1.00 52.67 C
ATOM 619 O GLY A 91 24.988 8.594 143.865 1.00 52.71 O
ATOM 620 N ASP A 92 25.690 10.465 142.841 1.00 51.56 N
ATOM 621 CA ASP A 92 25.372 11.322 143.965 1.00 52.09 C
ATOM 622 C ASP A 92 23.848 11.475 144.006 1.00 53.61 C
ATOM 623 O ASP A 92 23.247 12.140 143.159 1.00 53.31 O
ATOM 624 CB ASP A 92 26.070 12.666 143.783 1.00 53.62 C
ATOM 625 CG ASP A 92 27.579 12.517 143.620 1.00 56.76 C
ATOM 626 OD1 ASP A 92 28.135 11.490 144.072 1.00 56.04 O
ATOM 627 OD2 ASP A 92 28.214 13.427 143.050 1.00 61.54 O
ATOM 628 N GLN A 93 23.223 10.843 144.992 1.00 52.63 N
ATOM 629 CA GLN A 93 21.771 10.865 145.098 1.00 53.47 C
ATOM 630 C GLN A 93 21.106 12.240 145.238 1.00 52.78 C
ATOM 631 O GLN A 93 19.936 12.398 144.886 1.00 52.69 O
ATOM 632 CB GLN A 93 21.326 9.919 146.213 1.00 50.03 C
ATOM 633 CG GLN A 93 21.925 8.524 146.071 1.00 49.81 C
ATOM 634 CD GLN A 93 21.353 7.526 147.079 1.00 53.11 C
ATOM 635 OE1 GLN A 93 20.131 7.383 147.202 1.00 50.39 O
ATOM 636 NE2 GLN A 93 22.238 6.824 147.798 1.00 47.23 N
ATOM 637 N ASP A 94 21.831 13.238 145.735 1.00 53.35 N
ATOM 638 CA ASP A 94 21.231 14.573 145.841 1.00 53.57 C
ATOM 639 C ASP A 94 21.048 15.045 144.414 1.00 52.37 C
ATOM 640 O ASP A 94 19.987 15.551 144.044 1.00 56.77 O
ATOM 641 CB ASP A 94 22.132 15.543 146.625 1.00 56.02 C
ATOM 642 CG ASP A 94 23.548 15.623 146.071 1.00 57.77 C
ATOM 643 OD1 ASP A 94 24.063 14.595 145.582 1.00 60.04 O
ATOM 644 OD2 ASP A 94 24.153 16.714 146.147 1.00 57.65 O
ATOM 645 N ALA A 95 22.077 14.837 143.601 1.00 48.60 N
ATOM 646 CA ALA A 95 22.012 15.224 142.202 1.00 44.43 C
ATOM 647 C ALA A 95 20.863 14.453 141.566 1.00 41.72 C
ATOM 648 O ALA A 95 20.062 15.025 140.827 1.00 40.69 O
ATOM 649 CB ALA A 95 23.343 14.897 141.482 1.00 36.05 C
ATOM 650 N ILE A 96 20.791 13.158 141.873 1.00 42.42 N
ATOM 651 CA ILE A 96 19.757 12.290 141.322 1.00 43.97 C
ATOM 652 C ILE A 96 18.388 12.670 141.870 1.00 47.99 C
ATOM 653 O ILE A 96 17.368 12.372 141.256 1.00 48.74 O
ATOM 654 CB ILE A 96 20.036 10.799 141.635 1.00 40.24 C
ATOM 655 CG1 ILE A 96 21.313 10.362 140.922 1.00 40.13 C
ATOM 656 CG2 ILE A 96 18.860 9.926 141.191 1.00 36.34 C
ATOM 657 CD1 ILE A 96 21.713 8.899 141.149 1.00 31.63 C
ATOM 658 N HIS A 97 18.363 13.338 143.017 1.00 49.75 N
ATOM 659 CA HIS A 97 17.087 13.736 143.585 1.00 52.01 C
ATOM 660 C HIS A 97 16.529 14.839 142.709 1.00 52.04 C
ATOM 661 O HIS A 97 15.405 14.751 142.193 1.00 53.15 O
ATOM 662 CB HIS A 97 17.265 14.264 145.011 1.00 54.92 C
ATOM 663 CG HIS A 97 15.973 14.600 145.698 1.00 57.72 C
ATOM 664 ND1 HIS A 97 15.914 15.069 146.995 1.00 58.07 N
ATOM 665 CD2 HIS A 97 14.691 14.520 145.272 1.00 56.68 C
ATOM 666 CE1 HIS A 97 14.654 15.262 147.336 1.00 55.38 C
ATOM 667 NE2 HIS A 97 13.891 14.937 146.308 1.00 59.55 N
ATOM 668 N TYR A 98 17.334 15.879 142.549 1.00 48.17 N
ATOM 669 CA TYR A 98 16.951 17.028 141.756 1.00 47.00 C
ATOM 670 C TYR A 98 16.573 16.617 140.347 1.00 49.22 C
ATOM 671 O TYR A 98 15.477 16.928 139.874 1.00 51.61 O
ATOM 672 CB TYR A 98 18.103 18.022 141.728 1.00 46.91 C
ATOM 673 CG TYR A 98 17.788 19.351 141.099 1.00 46.90 C
ATOM 674 CD1 TYR A 98 17.970 19.558 139.735 1.00 46.17 C
ATOM 675 CD2 TYR A 98 17.326 20.410 141.868 1.00 47.83 C
ATOM 676 CE1 TYR A 98 17.706 20.785 139.152 1.00 46.45 C
ATOM 677 CE2 TYR A 98 17.053 21.651 141.290 1.00 49.42 C
ATOM 678 CZ TYR A 98 17.247 21.827 139.926 1.00 48.62 C
ATOM 679 OH TYR A 98 16.965 23.038 139.334 1.00 45.78 O
ATOM 680 N MET A 99 17.465 15.891 139.679 1.00 49.79 N
ATOM 681 CA MET A 99 17.174 15.488 138.315 1.00 47.88 C
ATOM 682 C MET A 99 15.775 14.884 138.160 1.00 45.66 C
ATOM 683 O MET A 99 14.988 15.393 137.380 1.00 41.23 O
ATOM 684 CB MET A 99 18.225 14.515 137.763 1.00 42.73 C
ATOM 685 CG MET A 99 17.856 14.059 136.347 1.00 48.50 C
ATOM 686 SD MET A 99 19.002 13.034 135.396 1.00 45.26 S
ATOM 687 CE MET A 99 18.874 11.540 136.211 1.00 43.68 C
ATOM 688 N THR A 100 15.460 13.835 138.919 1.00 45.60 N
ATOM 689 CA THR A 100 14.155 13.158 138.819 1.00 46.06 C
ATOM 690 C THR A 100 12.886 13.874 139.326 1.00 47.52 C
ATOM 691 O THR A 100 11.777 13.518 138.933 1.00 48.75 O
ATOM 692 CB THR A 100 14.203 11.762 139.494 1.00 45.78 C
ATOM 693 OG1 THR A 100 14.728 11.881 140.832 1.00 40.16 O
ATOM 694 CG2 THR A 100 15.058 10.810 138.665 1.00 39.40 C
ATOM 695 N GLU A 101 13.034 14.866 140.192 1.00 46.05 N
ATOM 696 CA GLU A 101 11.867 15.575 140.706 1.00 49.74 C
ATOM 697 C GLU A 101 11.536 16.778 139.815 1.00 50.81 C
ATOM 698 O GLU A 101 10.411 17.284 139.807 1.00 47.68 O
ATOM 699 CB GLU A 101 12.144 16.022 142.147 1.00 57.43 C
ATOM 700 CG GLU A 101 11.182 17.058 142.730 1.00 58.25 C
ATOM 701 CD GLU A 101 11.614 17.530 144.118 1.00 59.28 C
ATOM 702 OE1 GLU A 101 12.812 17.840 144.297 1.00 58.12 O
ATOM 703 OE2 GLU A 101 10.758 17.595 145.026 1.00 59.72 O
ATOM 704 N GLN A 102 12.525 17.227 139.052 1.00 48.98 N
ATOM 705 CA GLN A 102 12.331 18.359 138.163 1.00 46.19 C
ATOM 706 C GLN A 102 11.895 17.899 136.771 1.00 45.71 C
ATOM 707 O GLN A 102 11.394 18.708 135.970 1.00 46.66 O
ATOM 708 CB GLN A 102 13.637 19.149 138.039 1.00 47.97 C
ATOM 709 CG GLN A 102 14.136 19.803 139.324 1.00 48.92 C
ATOM 710 CD GLN A 102 13.204 20.887 139.842 1.00 50.45 C
ATOM 711 OE1 GLN A 102 12.598 21.637 139.066 1.00 54.61 O
ATOM 712 NE2 GLN A 102 13.096 20.987 141.163 1.00 51.25 N
ATOM 713 N ALA A 103 12.084 16.605 136.491 1.00 40.50 N
ATOM 714 CA ALA A 103 11.762 16.026 135.185 1.00 35.75 C
ATOM 715 C ALA A 103 10.411 16.401 134.566 1.00 36.99 C
ATOM 716 O ALA A 103 10.377 16.972 133.469 1.00 39.69 O
ATOM 717 CB ALA A 103 11.909 14.514 135.241 1.00 36.44 C
ATOM 718 N PRO A 104 9.283 16.076 135.234 1.00 34.55 N
ATOM 719 CA PRO A 104 7.948 16.410 134.691 1.00 36.46 C
ATOM 720 C PRO A 104 7.901 17.861 134.230 1.00 38.74 C
ATOM 721 O PRO A 104 7.430 18.187 133.139 1.00 40.99 O
ATOM 722 CB PRO A 104 7.018 16.178 135.880 1.00 36.16 C
ATOM 723 CG PRO A 104 7.705 15.083 136.643 1.00 36.90 C
ATOM 724 CD PRO A 104 9.172 15.462 136.569 1.00 34.84 C
ATOM 725 N ALA A 105 8.395 18.737 135.089 1.00 42.03 N
ATOM 726 CA ALA A 105 8.435 20.144 134.766 1.00 44.98 C
ATOM 727 C ALA A 105 9.328 20.380 133.543 1.00 47.18 C
ATOM 728 O ALA A 105 8.933 21.103 132.641 1.00 51.63 O
ATOM 729 CB ALA A 105 8.947 20.914 135.945 1.00 43.51 C
ATOM 730 N ALA A 106 10.521 19.778 133.511 1.00 47.74 N
ATOM 731 CA ALA A 106 11.446 19.946 132.384 1.00 46.83 C
ATOM 732 C ALA A 106 10.814 19.552 131.051 1.00 50.67 C
ATOM 733 O ALA A 106 10.908 20.287 130.066 1.00 53.46 O
ATOM 734 CB ALA A 106 12.703 19.124 132.610 1.00 46.82 C
ATOM 735 N VAL A 107 10.176 18.388 131.021 1.00 49.60 N
ATOM 736 CA VAL A 107 9.526 17.903 129.809 1.00 51.09 C
ATOM 737 C VAL A 107 8.360 18.797 129.373 1.00 52.48 C
ATOM 738 O VAL A 107 8.257 19.190 128.212 1.00 54.79 O
ATOM 739 CB VAL A 107 9.012 16.443 130.013 1.00 52.32 C
ATOM 740 CG1 VAL A 107 8.018 16.055 128.904 1.00 46.32 C
ATOM 741 CG2 VAL A 107 10.206 15.482 130.039 1.00 48.30 C
ATOM 742 N ILE A 108 7.478 19.123 130.303 1.00 52.38 N
ATOM 743 CA ILE A 108 6.343 19.962 129.962 1.00 54.63 C
ATOM 744 C ILE A 108 6.800 21.270 129.328 1.00 51.93 C
ATOM 745 O ILE A 108 6.161 21.776 128.411 1.00 53.53 O
ATOM 746 CB ILE A 108 5.457 20.220 131.213 1.00 56.77 C
ATOM 747 CG1 ILE A 108 4.726 18.915 131.584 1.00 54.72 C
ATOM 748 CG2 ILE A 108 4.473 21.373 130.942 1.00 55.81 C
ATOM 749 CD1 ILE A 108 3.876 18.972 132.856 1.00 46.25 C
ATOM 750 N GLU A 109 7.915 21.803 129.817 1.00 52.07 N
ATOM 751 CA GLU A 109 8.501 23.039 129.294 1.00 50.05 C
ATOM 752 C GLU A 109 8.819 22.863 127.803 1.00 48.96 C
ATOM 753 O GLU A 109 8.611 23.763 126.985 1.00 47.97 O
ATOM 754 CB GLU A 109 9.805 23.363 130.045 1.00 50.82 C
ATOM 755 CG GLU A 109 10.543 24.577 129.499 1.00 55.78 C
ATOM 756 CD GLU A 109 11.793 24.934 130.277 1.00 58.47 C
ATOM 757 OE1 GLU A 109 12.786 24.177 130.208 1.00 63.07 O
ATOM 758 OE2 GLU A 109 11.782 25.978 130.959 1.00 59.45 O
ATOM 759 N LEU A 110 9.331 21.687 127.463 1.00 47.15 N
ATOM 760 CA LEU A 110 9.695 21.391 126.095 1.00 45.56 C
ATOM 761 C LEU A 110 8.467 21.354 125.210 1.00 45.31 C
ATOM 762 O LEU A 110 8.456 21.953 124.125 1.00 38.06 O
ATOM 763 CB LEU A 110 10.460 20.060 126.033 1.00 47.28 C
ATOM 764 CG LEU A 110 11.838 20.129 126.719 1.00 47.01 C
ATOM 765 CD1 LEU A 110 12.516 18.764 126.725 1.00 47.33 C
ATOM 766 CD2 LEU A 110 12.715 21.164 125.998 1.00 49.57 C
ATOM 767 N GLU A 111 7.425 20.663 125.667 1.00 45.29 N
ATOM 768 CA GLU A 111 6.197 20.580 124.880 1.00 41.38 C
ATOM 769 C GLU A 111 5.622 22.004 124.751 1.00 39.09 C
ATOM 770 O GLU A 111 5.252 22.444 123.661 1.00 34.89 O
ATOM 771 CB GLU A 111 5.235 19.606 125.558 1.00 42.99 C
ATOM 772 CG GLU A 111 3.953 19.317 124.801 1.00 49.86 C
ATOM 773 CD GLU A 111 2.984 20.481 124.855 1.00 53.64 C
ATOM 774 OE1 GLU A 111 2.679 20.951 125.971 1.00 54.90 O
ATOM 775 OE2 GLU A 111 2.531 20.933 123.783 1.00 55.97 O
ATOM 776 N ASN A 112 5.603 22.761 125.842 1.00 39.95 N
ATOM 777 CA ASN A 112 5.091 24.135 125.769 1.00 43.15 C
ATOM 778 C ASN A 112 5.897 25.047 124.836 1.00 43.43 C
ATOM 779 O ASN A 112 5.412 26.099 124.418 1.00 44.40 O
ATOM 780 CB ASN A 112 5.011 24.758 127.170 1.00 44.87 C
ATOM 781 CG ASN A 112 3.811 24.247 127.972 1.00 45.33 C
ATOM 782 OD1 ASN A 112 3.613 24.619 129.127 1.00 45.74 O
ATOM 783 ND2 ASN A 112 3.007 23.393 127.351 1.00 39.27 N
ATOM 784 N TYR A 113 7.131 24.648 124.527 1.00 44.08 N
ATOM 785 CA TYR A 113 7.999 25.393 123.623 1.00 39.17 C
ATOM 786 C TYR A 113 7.631 25.059 122.162 1.00 42.70 C
ATOM 787 O TYR A 113 7.697 25.921 121.270 1.00 40.89 O
ATOM 788 CB TYR A 113 9.451 24.996 123.842 1.00 37.64 C
ATOM 789 CG TYR A 113 10.156 25.606 125.025 1.00 42.08 C
ATOM 790 CD1 TYR A 113 11.473 25.260 125.306 1.00 44.28 C
ATOM 791 CD2 TYR A 113 9.537 26.546 125.847 1.00 46.11 C
ATOM 792 CE1 TYR A 113 12.168 25.832 126.375 1.00 49.92 C
ATOM 793 CE2 TYR A 113 10.222 27.128 126.927 1.00 47.44 C
ATOM 794 CZ TYR A 113 11.545 26.764 127.187 1.00 50.24 C
ATOM 795 OH TYR A 113 12.252 27.301 128.258 1.00 53.58 O
ATOM 796 N GLY A 114 7.275 23.798 121.918 1.00 40.84 N
ATOM 797 CA GLY A 114 6.913 23.378 120.574 1.00 37.97 C
ATOM 798 C GLY A 114 7.211 21.935 120.216 1.00 35.38 C
ATOM 799 O GLY A 114 6.731 21.408 119.212 1.00 36.98 O
ATOM 800 N MET A 115 8.000 21.279 121.046 1.00 38.44 N
ATOM 801 CA MET A 115 8.372 19.890 120.806 1.00 39.29 C
ATOM 802 C MET A 115 7.224 18.975 120.358 1.00 34.71 C
ATOM 803 O MET A 115 6.316 18.685 121.121 1.00 36.41 O
ATOM 804 CB MET A 115 9.033 19.319 122.059 1.00 41.34 C
ATOM 805 CG MET A 115 9.973 18.169 121.744 1.00 45.05 C
ATOM 806 SD MET A 115 11.361 18.070 122.873 1.00 49.38 S
ATOM 807 CE MET A 115 11.603 16.237 122.851 1.00 48.91 C
ATOM 808 N PRO A 116 7.269 18.491 119.109 1.00 35.90 N
ATOM 809 CA PRO A 116 6.234 17.604 118.553 1.00 34.51 C
ATOM 810 C PRO A 116 6.121 16.204 119.108 1.00 35.73 C
ATOM 811 O PRO A 116 6.126 15.233 118.341 1.00 39.70 O
ATOM 812 CB PRO A 116 6.550 17.581 117.053 1.00 31.95 C
ATOM 813 CG PRO A 116 8.013 17.847 117.006 1.00 33.95 C
ATOM 814 CD PRO A 116 8.192 18.931 118.050 1.00 34.86 C
ATOM 815 N PHE A 117 6.003 16.090 120.426 1.00 35.95 N
ATOM 816 CA PHE A 117 5.871 14.781 121.065 1.00 38.62 C
ATOM 817 C PHE A 117 4.745 13.945 120.456 1.00 43.80 C
ATOM 818 O PHE A 117 3.664 14.467 120.140 1.00 41.76 O
ATOM 819 CB PHE A 117 5.573 14.943 122.558 1.00 40.85 C
ATOM 820 CG PHE A 117 6.776 15.220 123.400 1.00 42.97 C
ATOM 821 CD1 PHE A 117 7.737 14.240 123.600 1.00 42.83 C
ATOM 822 CD2 PHE A 117 6.945 16.458 124.004 1.00 43.91 C
ATOM 823 CE1 PHE A 117 8.840 14.488 124.385 1.00 41.04 C
ATOM 824 CE2 PHE A 117 8.049 16.715 124.792 1.00 41.38 C
ATOM 825 CZ PHE A 117 8.997 15.731 124.983 1.00 43.82 C
ATOM 826 N SER A 118 5.000 12.647 120.287 1.00 45.07 N
ATOM 827 CA SER A 118 3.975 11.755 119.768 1.00 42.48 C
ATOM 828 C SER A 118 2.914 11.757 120.843 1.00 44.41 C
ATOM 829 O SER A 118 3.229 11.851 122.025 1.00 39.76 O
ATOM 830 CB SER A 118 4.518 10.347 119.563 1.00 43.99 C
ATOM 831 OG SER A 118 5.309 10.300 118.387 1.00 47.18 O
ATOM 832 N ARG A 119 1.659 11.640 120.422 1.00 49.64 N
ATOM 833 CA ARG A 119 0.510 11.696 121.322 1.00 49.29 C
ATOM 834 C ARG A 119 -0.194 10.393 121.677 1.00 50.08 C
ATOM 835 O ARG A 119 -0.071 9.388 120.975 1.00 51.31 O
ATOM 836 CB ARG A 119 -0.509 12.653 120.717 1.00 47.10 C
ATOM 837 CG ARG A 119 0.063 14.028 120.506 1.00 50.45 C
ATOM 838 CD ARG A 119 0.393 14.688 121.849 1.00 48.67 C
ATOM 839 NE ARG A 119 1.228 15.862 121.647 1.00 49.82 N
ATOM 840 CZ ARG A 119 1.362 16.844 122.524 1.00 47.46 C
ATOM 841 NH1 ARG A 119 0.705 16.793 123.670 1.00 39.12 N
ATOM 842 NH2 ARG A 119 2.158 17.873 122.254 1.00 46.31 N
ATOM 843 N THR A 120 -0.942 10.441 122.779 1.00 51.81 N
ATOM 844 CA THR A 120 -1.737 9.317 123.267 1.00 52.85 C
ATOM 845 C THR A 120 -3.158 9.555 122.783 1.00 56.60 C
ATOM 846 O THR A 120 -3.422 10.512 122.060 1.00 54.61 O
ATOM 847 CB THR A 120 -1.798 9.282 124.798 1.00 50.17 C
ATOM 848 OG1 THR A 120 -2.612 10.369 125.270 1.00 40.31 O
ATOM 849 CG2 THR A 120 -0.383 9.399 125.384 1.00 51.89 C
ATOM 850 N GLU A 121 -4.072 8.683 123.193 1.00 61.64 N
ATOM 851 CA GLU A 121 -5.474 8.827 122.819 1.00 65.08 C
ATOM 852 C GLU A 121 -6.126 9.974 123.593 1.00 63.68 C
ATOM 853 O GLU A 121 -7.192 10.465 123.216 1.00 65.33 O
ATOM 854 CB GLU A 121 -6.232 7.521 123.079 1.00 66.99 C
ATOM 855 CG GLU A 121 -6.136 6.498 121.946 1.00 73.70 C
ATOM 856 CD GLU A 121 -6.767 6.992 120.638 1.00 77.94 C
ATOM 857 OE1 GLU A 121 -7.893 7.540 120.682 1.00 81.45 O
ATOM 858 OE2 GLU A 121 -6.143 6.818 119.565 1.00 78.94 O
ATOM 859 N GLU A 122 -5.472 10.404 124.664 1.00 59.75 N