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1yq3_IF10316.pdb
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1yq3_IF10316.pdb
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HEADER Entry: 1yq3 InterfaceID: 1 3/8/2022
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 E Author Chain A Entity 5 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 F Author Chain A Entity 6 Symmetry Operator 1_555
Remark 300 Name MALATE LIKE INTERMEDIATE Sequence TEO PDB Sequence Number 1002 Author Sequence Number 2
Remark 300 Interface Chain A For Asymmetric Chain G Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1003 Author Sequence Number 206
Remark 300 Interface Chain A For Asymmetric Chain H Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1004 Author Sequence Number 207
Remark 300 Interface Chain A For Asymmetric Chain I Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1005 Author Sequence Number 208
Remark 300 Interface Chain A For Asymmetric Chain J Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1006 Author Sequence Number 210
Remark 300 Interface Chain A For Asymmetric Chain K Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1007 Author Sequence Number 213
Remark 300 Interface Chain A For Asymmetric Chain L Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1008 Author Sequence Number 214
Remark 300 Interface Chain A For Asymmetric Chain M Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1009 Author Sequence Number 215
Remark 300 Interface Chain A For Asymmetric Chain N Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1010 Author Sequence Number 217
Remark 300 Interface Chain A For Asymmetric Chain O Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1011 Author Sequence Number 220
Remark 300 Interface Chain A For Asymmetric Chain P Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1012 Author Sequence Number 222
Remark 300 Interface Chain A For Asymmetric Chain Q Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1013 Author Sequence Number 223
Remark 300 Interface Chain A For Asymmetric Chain R Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1014 Author Sequence Number 224
Remark 300 Interface Chain A For Asymmetric Chain S Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1015 Author Sequence Number 227
Remark 300 Interface Chain A For Asymmetric Chain T Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1016 Author Sequence Number 229
Remark 300 Interface Chain A For Asymmetric Chain TA Author Chain A Entity 16 Symmetry Operator 1_555
Remark 300 Name water Sequence - PDB Sequence Number 1018-1457 Author Sequence Number 1018-1457
Remark 300 Interface Chain A For Asymmetric Chain U Author Chain A Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1017 Author Sequence Number 230
Remark 300 Interface Chain B For Asymmetric Chain AA Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1007 Author Sequence Number 202
Remark 300 Interface Chain B For Asymmetric Chain BA Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1008 Author Sequence Number 216
Remark 300 Interface Chain B For Asymmetric Chain CA Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1009 Author Sequence Number 219
Remark 300 Interface Chain B For Asymmetric Chain DA Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1010 Author Sequence Number 221
Remark 300 Interface Chain B For Asymmetric Chain EA Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1011 Author Sequence Number 225
Remark 300 Interface Chain B For Asymmetric Chain FA Author Chain B Entity 12 Symmetry Operator 1_555
Remark 300 Name GLYCEROL Sequence GOL PDB Sequence Number 1012 Author Sequence Number 19
Remark 300 Interface Chain B For Asymmetric Chain UA Author Chain B Entity 16 Symmetry Operator 1_555
Remark 300 Name water Sequence - PDB Sequence Number 1013-1225 Author Sequence Number 1013-1225
Remark 300 Interface Chain B For Asymmetric Chain V Author Chain B Entity 8 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 W Author Chain B Entity 9 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 X Author Chain B Entity 10 Symmetry Operator 1_555
Remark 300 Name FE3-S4 CLUSTER Sequence F3S PDB Sequence Number 1004 Author Sequence Number 1004
Remark 300 Interface Chain B For Asymmetric Chain Y Author Chain B Entity 11 Symmetry Operator 1_555
Remark 300 Name Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer Sequence UQ PDB Sequence Number 1005 Author Sequence Number 1
Remark 300 Interface Chain B For Asymmetric Chain Z Author Chain B Entity 7 Symmetry Operator 1_555
Remark 300 Name UNKNOWN LIGAND Sequence UNL PDB Sequence Number 1006 Author Sequence Number 201
Remark 350 Interface surface area: 2576.1
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 N ILE A 8 56.542 37.639 121.615 1.00129.74 N
ATOM 2 CA ILE A 8 56.150 36.456 120.782 1.00129.59 C
ATOM 3 C ILE A 8 55.833 36.875 119.330 1.00129.40 C
ATOM 4 O ILE A 8 56.276 36.229 118.364 1.00130.40 O
ATOM 5 CB ILE A 8 54.908 35.730 121.389 1.00128.86 C
ATOM 6 N SER A 9 55.073 37.967 119.199 1.00127.97 N
ATOM 7 CA SER A 9 54.632 38.540 117.916 1.00124.92 C
ATOM 8 C SER A 9 53.221 38.054 117.476 1.00121.97 C
ATOM 9 O SER A 9 52.920 36.836 117.359 1.00121.44 O
ATOM 10 CB SER A 9 55.669 38.287 116.807 1.00125.29 C
ATOM 11 OG SER A 9 55.535 39.260 115.793 1.00126.37 O
ATOM 12 N THR A 10 52.354 39.041 117.268 1.00117.26 N
ATOM 13 CA THR A 10 50.998 38.777 116.849 1.00111.81 C
ATOM 14 C THR A 10 50.981 38.666 115.297 1.00107.28 C
ATOM 15 O THR A 10 50.816 39.664 114.565 1.00106.60 O
ATOM 16 CB THR A 10 50.022 39.901 117.424 1.00112.43 C
ATOM 17 OG1 THR A 10 48.656 39.488 117.304 1.00112.27 O
ATOM 18 CG2 THR A 10 50.204 41.229 116.703 1.00112.60 C
ATOM 19 N GLN A 11 51.228 37.442 114.806 1.00100.84 N
ATOM 20 CA GLN A 11 51.174 37.157 113.363 1.00 92.96 C
ATOM 21 C GLN A 11 49.640 36.977 113.157 1.00 87.00 C
ATOM 22 O GLN A 11 49.125 36.943 112.032 1.00 84.72 O
ATOM 23 CB GLN A 11 51.960 35.862 113.028 1.00 93.78 C
ATOM 24 CG GLN A 11 52.870 35.342 114.191 1.00 97.05 C
ATOM 25 CD GLN A 11 54.342 35.033 113.788 1.00 98.63 C
ATOM 26 OE1 GLN A 11 55.246 35.046 114.639 1.00 99.62 O
ATOM 27 NE2 GLN A 11 54.574 34.751 112.507 1.00 98.76 N
ATOM 28 N TYR A 12 48.937 36.877 114.296 1.00 79.49 N
ATOM 29 CA TYR A 12 47.494 36.726 114.352 1.00 71.61 C
ATOM 30 C TYR A 12 46.818 37.932 114.991 1.00 70.59 C
ATOM 31 O TYR A 12 47.119 38.328 116.110 1.00 67.83 O
ATOM 32 CB TYR A 12 47.120 35.518 115.161 1.00 63.35 C
ATOM 33 CG TYR A 12 47.611 34.251 114.593 1.00 56.97 C
ATOM 34 CD1 TYR A 12 48.939 33.922 114.698 1.00 54.76 C
ATOM 35 CD2 TYR A 12 46.762 33.373 113.938 1.00 53.54 C
ATOM 36 CE1 TYR A 12 49.427 32.761 114.172 1.00 51.75 C
ATOM 37 CE2 TYR A 12 47.246 32.185 113.401 1.00 50.83 C
ATOM 38 CZ TYR A 12 48.591 31.896 113.527 1.00 50.42 C
ATOM 39 OH TYR A 12 49.171 30.779 112.996 1.00 47.52 O
ATOM 40 N PRO A 13 45.903 38.564 114.256 1.00 70.77 N
ATOM 41 CA PRO A 13 45.222 39.724 114.875 1.00 70.31 C
ATOM 42 C PRO A 13 44.228 39.170 115.942 1.00 67.55 C
ATOM 43 O PRO A 13 43.575 38.113 115.730 1.00 66.82 O
ATOM 44 CB PRO A 13 44.524 40.422 113.679 1.00 71.62 C
ATOM 45 CG PRO A 13 44.330 39.295 112.642 1.00 71.85 C
ATOM 46 CD PRO A 13 45.536 38.358 112.832 1.00 70.89 C
ATOM 47 N VAL A 14 44.130 39.861 117.069 1.00 63.44 N
ATOM 48 CA VAL A 14 43.283 39.409 118.175 1.00 59.70 C
ATOM 49 C VAL A 14 42.092 40.325 118.458 1.00 57.14 C
ATOM 50 O VAL A 14 42.289 41.498 118.661 1.00 59.79 O
ATOM 51 CB VAL A 14 44.135 39.316 119.440 1.00 58.24 C
ATOM 52 CG1 VAL A 14 43.302 38.892 120.663 1.00 56.08 C
ATOM 53 CG2 VAL A 14 45.258 38.380 119.189 1.00 57.07 C
ATOM 54 N VAL A 15 40.873 39.804 118.494 1.00 52.68 N
ATOM 55 CA VAL A 15 39.691 40.640 118.763 1.00 48.68 C
ATOM 56 C VAL A 15 39.213 40.340 120.169 1.00 47.48 C
ATOM 57 O VAL A 15 39.053 39.176 120.546 1.00 46.60 O
ATOM 58 CB VAL A 15 38.561 40.267 117.784 1.00 50.09 C
ATOM 59 CG1 VAL A 15 37.267 41.130 117.991 1.00 49.82 C
ATOM 60 CG2 VAL A 15 39.082 40.362 116.408 1.00 47.37 C
ATOM 61 N ASP A 16 38.968 41.369 120.946 1.00 47.36 N
ATOM 62 CA ASP A 16 38.495 41.161 122.306 1.00 49.72 C
ATOM 63 C ASP A 16 37.037 41.504 122.481 1.00 47.14 C
ATOM 64 O ASP A 16 36.563 42.518 121.976 1.00 48.53 O
ATOM 65 CB ASP A 16 39.379 41.950 123.297 1.00 50.61 C
ATOM 66 CG ASP A 16 40.674 41.190 123.607 1.00 57.19 C
ATOM 67 OD1 ASP A 16 40.686 40.168 124.343 1.00 56.20 O
ATOM 68 OD2 ASP A 16 41.708 41.601 123.061 1.00 64.50 O
ATOM 69 N HIS A 17 36.310 40.662 123.184 1.00 45.28 N
ATOM 70 CA HIS A 17 34.851 40.917 123.425 1.00 44.02 C
ATOM 71 C HIS A 17 34.586 40.877 124.919 1.00 43.26 C
ATOM 72 O HIS A 17 35.300 40.231 125.658 1.00 44.57 O
ATOM 73 CB HIS A 17 33.983 39.824 122.783 1.00 39.62 C
ATOM 74 CG HIS A 17 34.305 39.545 121.363 1.00 39.16 C
ATOM 75 ND1 HIS A 17 33.581 40.102 120.326 1.00 41.01 N
ATOM 76 CD2 HIS A 17 35.179 38.670 120.794 1.00 39.11 C
ATOM 77 CE1 HIS A 17 33.978 39.554 119.182 1.00 40.65 C
ATOM 78 NE2 HIS A 17 34.945 38.682 119.436 1.00 39.65 N
ATOM 79 N GLU A 18 33.539 41.514 125.368 1.00 44.61 N
ATOM 80 CA GLU A 18 33.264 41.500 126.765 1.00 48.11 C
ATOM 81 C GLU A 18 31.799 41.154 126.829 1.00 48.32 C
ATOM 82 O GLU A 18 30.973 41.750 126.169 1.00 47.66 O
ATOM 83 CB GLU A 18 33.423 42.897 127.393 1.00 53.42 C
ATOM 84 CG GLU A 18 34.809 43.404 127.795 1.00 59.69 C
ATOM 85 CD GLU A 18 34.847 44.983 128.125 1.00 67.15 C
ATOM 86 OE1 GLU A 18 34.037 45.507 128.993 1.00 68.91 O
ATOM 87 OE2 GLU A 18 35.708 45.695 127.491 1.00 69.39 O
ATOM 88 N PHE A 19 31.463 40.169 127.622 1.00 46.69 N
ATOM 89 CA PHE A 19 30.053 39.803 127.771 1.00 43.20 C
ATOM 90 C PHE A 19 29.871 39.495 129.266 1.00 43.08 C
ATOM 91 O PHE A 19 30.894 39.342 130.010 1.00 41.78 O
ATOM 92 CB PHE A 19 29.756 38.504 127.006 1.00 37.84 C
ATOM 93 CG PHE A 19 29.614 38.680 125.553 1.00 38.58 C
ATOM 94 CD1 PHE A 19 30.728 38.598 124.700 1.00 36.73 C
ATOM 95 CD2 PHE A 19 28.316 38.945 124.996 1.00 39.46 C
ATOM 96 CE1 PHE A 19 30.584 38.776 123.285 1.00 34.73 C
ATOM 97 CE2 PHE A 19 28.154 39.117 123.629 1.00 36.82 C
ATOM 98 CZ PHE A 19 29.301 39.031 122.759 1.00 40.36 C
ATOM 99 N ASP A 20 28.611 39.435 129.703 1.00 40.69 N
ATOM 100 CA ASP A 20 28.331 39.005 131.057 1.00 40.08 C
ATOM 101 C ASP A 20 28.677 37.515 131.130 1.00 40.69 C
ATOM 102 O ASP A 20 29.232 37.063 132.153 1.00 41.30 O
ATOM 103 CB ASP A 20 26.845 39.110 131.368 1.00 40.32 C
ATOM 104 CG ASP A 20 26.389 40.535 131.540 1.00 45.53 C
ATOM 105 OD1 ASP A 20 27.259 41.390 131.847 1.00 48.29 O
ATOM 106 OD2 ASP A 20 25.168 40.821 131.375 1.00 45.62 O
ATOM 107 N ALA A 21 28.331 36.745 130.078 1.00 41.37 N
ATOM 108 CA ALA A 21 28.539 35.262 130.079 1.00 42.47 C
ATOM 109 C ALA A 21 28.819 34.677 128.715 1.00 41.30 C
ATOM 110 O ALA A 21 28.374 35.226 127.734 1.00 42.17 O
ATOM 111 CB ALA A 21 27.314 34.590 130.624 1.00 40.22 C
ATOM 112 N VAL A 22 29.536 33.557 128.645 1.00 40.65 N
ATOM 113 CA VAL A 22 29.881 32.933 127.375 1.00 39.18 C
ATOM 114 C VAL A 22 29.488 31.476 127.473 1.00 36.98 C
ATOM 115 O VAL A 22 29.898 30.847 128.409 1.00 33.15 O
ATOM 116 CB VAL A 22 31.415 32.776 127.110 1.00 41.64 C
ATOM 117 CG1 VAL A 22 31.651 32.276 125.719 1.00 41.40 C
ATOM 118 CG2 VAL A 22 32.070 33.950 127.227 1.00 43.61 C
ATOM 119 N VAL A 23 28.809 30.934 126.459 1.00 34.41 N
ATOM 120 CA VAL A 23 28.415 29.519 126.456 1.00 34.42 C
ATOM 121 C VAL A 23 29.183 28.934 125.322 1.00 34.66 C
ATOM 122 O VAL A 23 29.137 29.490 124.212 1.00 36.22 O
ATOM 123 CB VAL A 23 26.892 29.256 126.119 1.00 33.04 C
ATOM 124 CG1 VAL A 23 26.664 27.785 126.118 1.00 30.66 C
ATOM 125 CG2 VAL A 23 26.000 29.832 127.241 1.00 34.79 C
ATOM 126 N VAL A 24 29.933 27.866 125.599 1.00 30.94 N
ATOM 127 CA VAL A 24 30.670 27.248 124.529 1.00 31.55 C
ATOM 128 C VAL A 24 29.956 25.975 124.157 1.00 31.75 C
ATOM 129 O VAL A 24 29.913 25.072 124.945 1.00 28.25 O
ATOM 130 CB VAL A 24 32.181 26.922 124.924 1.00 32.01 C
ATOM 131 CG1 VAL A 24 32.894 26.462 123.724 1.00 29.51 C
ATOM 132 CG2 VAL A 24 32.894 28.205 125.502 1.00 29.64 C
ATOM 133 N GLY A 25 29.408 25.918 122.927 1.00 32.76 N
ATOM 134 CA GLY A 25 28.652 24.733 122.483 1.00 29.46 C
ATOM 135 C GLY A 25 27.196 25.131 122.077 1.00 30.39 C
ATOM 136 O GLY A 25 26.594 26.010 122.694 1.00 30.82 O
ATOM 137 N ALA A 26 26.624 24.507 121.061 1.00 29.92 N
ATOM 138 CA ALA A 26 25.256 24.951 120.730 1.00 35.92 C
ATOM 139 C ALA A 26 24.397 23.777 120.333 1.00 32.65 C
ATOM 140 O ALA A 26 23.699 23.798 119.374 1.00 35.19 O
ATOM 141 CB ALA A 26 25.246 26.058 119.617 1.00 34.65 C
ATOM 142 N GLY A 27 24.574 22.714 121.075 1.00 32.54 N
ATOM 143 CA GLY A 27 23.735 21.551 120.950 1.00 32.46 C
ATOM 144 C GLY A 27 22.586 21.852 121.930 1.00 27.06 C
ATOM 145 O GLY A 27 22.270 23.024 122.271 1.00 28.13 O
ATOM 146 N GLY A 28 21.963 20.805 122.397 1.00 29.33 N
ATOM 147 CA GLY A 28 20.828 20.914 123.292 1.00 29.50 C
ATOM 148 C GLY A 28 21.170 21.635 124.582 1.00 35.14 C
ATOM 149 O GLY A 28 20.442 22.583 125.005 1.00 37.48 O
ATOM 150 N ALA A 29 22.269 21.249 125.223 1.00 32.40 N
ATOM 151 CA ALA A 29 22.628 21.901 126.480 1.00 27.71 C
ATOM 152 C ALA A 29 23.030 23.308 126.254 1.00 29.46 C
ATOM 153 O ALA A 29 22.521 24.185 126.914 1.00 31.91 O
ATOM 154 CB ALA A 29 23.784 21.179 127.147 1.00 31.33 C
ATOM 155 N GLY A 30 23.948 23.566 125.316 1.00 28.59 N
ATOM 156 CA GLY A 30 24.346 24.968 125.149 1.00 31.55 C
ATOM 157 C GLY A 30 23.240 25.924 124.675 1.00 32.98 C
ATOM 158 O GLY A 30 23.106 27.055 125.185 1.00 30.17 O
ATOM 159 N LEU A 31 22.446 25.517 123.684 1.00 34.51 N
ATOM 160 CA LEU A 31 21.388 26.449 123.292 1.00 35.69 C
ATOM 161 C LEU A 31 20.512 26.716 124.517 1.00 32.70 C
ATOM 162 O LEU A 31 20.267 27.896 124.838 1.00 39.28 O
ATOM 163 CB LEU A 31 20.534 25.939 122.094 1.00 34.15 C
ATOM 164 CG LEU A 31 21.214 25.759 120.748 1.00 35.35 C
ATOM 165 CD1 LEU A 31 20.235 25.140 119.688 1.00 34.84 C
ATOM 166 CD2 LEU A 31 21.718 27.117 120.253 1.00 38.72 C
ATOM 167 N ARG A 32 20.100 25.694 125.271 1.00 34.22 N
ATOM 168 CA ARG A 32 19.201 25.986 126.412 1.00 32.94 C
ATOM 169 C ARG A 32 19.841 26.907 127.477 1.00 35.79 C
ATOM 170 O ARG A 32 19.171 27.847 128.077 1.00 28.99 O
ATOM 171 CB ARG A 32 18.740 24.724 127.089 1.00 31.77 C
ATOM 172 CG ARG A 32 17.746 25.056 128.324 1.00 28.44 C
ATOM 173 CD ARG A 32 16.355 25.482 127.760 1.00 28.88 C
ATOM 174 NE ARG A 32 15.347 25.897 128.726 1.00 27.58 N
ATOM 175 CZ ARG A 32 15.352 27.110 129.283 1.00 37.99 C
ATOM 176 NH1 ARG A 32 16.338 27.982 128.996 1.00 36.84 N
ATOM 177 NH2 ARG A 32 14.338 27.508 130.040 1.00 35.17 N
ATOM 178 N ALA A 33 21.150 26.665 127.713 1.00 35.80 N
ATOM 179 CA ALA A 33 21.830 27.548 128.647 1.00 36.16 C
ATOM 180 C ALA A 33 21.967 28.961 128.070 1.00 34.67 C
ATOM 181 O ALA A 33 21.778 29.927 128.805 1.00 31.22 O
ATOM 182 CB ALA A 33 23.290 27.014 129.013 1.00 36.89 C
ATOM 183 N ALA A 34 22.353 29.068 126.799 1.00 31.72 N
ATOM 184 CA ALA A 34 22.625 30.406 126.227 1.00 34.93 C
ATOM 185 C ALA A 34 21.319 31.267 126.158 1.00 35.54 C
ATOM 186 O ALA A 34 21.308 32.358 126.653 1.00 38.42 O
ATOM 187 CB ALA A 34 23.283 30.273 124.822 1.00 29.25 C
ATOM 188 N PHE A 35 20.218 30.823 125.570 1.00 36.22 N
ATOM 189 CA PHE A 35 19.065 31.738 125.690 1.00 34.92 C
ATOM 190 C PHE A 35 18.488 31.791 127.097 1.00 35.83 C
ATOM 191 O PHE A 35 17.872 32.805 127.453 1.00 39.69 O
ATOM 192 CB PHE A 35 17.968 31.505 124.623 1.00 32.26 C
ATOM 193 CG PHE A 35 17.148 30.226 124.793 1.00 34.01 C
ATOM 194 CD1 PHE A 35 16.028 30.162 125.669 1.00 35.17 C
ATOM 195 CD2 PHE A 35 17.400 29.146 123.968 1.00 32.80 C
ATOM 196 CE1 PHE A 35 15.172 29.023 125.694 1.00 30.36 C
ATOM 197 CE2 PHE A 35 16.516 27.987 123.976 1.00 32.98 C
ATOM 198 CZ PHE A 35 15.443 27.926 124.797 1.00 28.58 C
ATOM 199 N GLY A 36 18.691 30.770 127.952 1.00 35.57 N
ATOM 200 CA GLY A 36 18.160 30.917 129.309 1.00 32.39 C
ATOM 201 C GLY A 36 18.817 32.166 129.957 1.00 37.78 C
ATOM 202 O GLY A 36 18.139 32.963 130.664 1.00 38.19 O
ATOM 203 N LEU A 37 20.145 32.295 129.751 1.00 33.62 N
ATOM 204 CA LEU A 37 20.924 33.370 130.249 1.00 37.59 C
ATOM 205 C LEU A 37 20.357 34.705 129.651 1.00 39.84 C
ATOM 206 O LEU A 37 20.118 35.696 130.394 1.00 43.31 O
ATOM 207 CB LEU A 37 22.422 33.151 129.878 1.00 34.19 C
ATOM 208 CG LEU A 37 23.143 32.273 130.910 1.00 37.57 C
ATOM 209 CD1 LEU A 37 24.498 31.844 130.463 1.00 32.53 C
ATOM 210 CD2 LEU A 37 23.326 33.093 132.175 1.00 36.72 C
ATOM 211 N SER A 38 20.177 34.776 128.335 1.00 37.75 N
ATOM 212 CA SER A 38 19.609 36.010 127.745 1.00 40.74 C
ATOM 213 C SER A 38 18.174 36.277 128.280 1.00 41.44 C
ATOM 214 O SER A 38 17.848 37.393 128.653 1.00 44.38 O
ATOM 215 CB SER A 38 19.540 35.918 126.240 1.00 40.00 C
ATOM 216 OG SER A 38 20.834 35.922 125.732 1.00 43.20 O
ATOM 217 N GLU A 39 17.348 35.255 128.364 1.00 42.64 N
ATOM 218 CA GLU A 39 16.021 35.439 128.895 1.00 44.14 C
ATOM 219 C GLU A 39 16.139 36.046 130.311 1.00 45.88 C
ATOM 220 O GLU A 39 15.322 36.868 130.711 1.00 44.78 O
ATOM 221 CB GLU A 39 15.339 34.112 128.922 1.00 44.54 C
ATOM 222 CG GLU A 39 14.068 34.052 129.710 1.00 52.31 C
ATOM 223 CD GLU A 39 13.171 32.799 129.346 1.00 55.64 C
ATOM 224 OE1 GLU A 39 13.722 31.673 129.150 1.00 54.06 O
ATOM 225 OE2 GLU A 39 11.920 32.954 129.257 1.00 58.56 O
ATOM 226 N ALA A 40 17.178 35.681 131.059 1.00 43.49 N
ATOM 227 CA ALA A 40 17.324 36.224 132.417 1.00 43.16 C
ATOM 228 C ALA A 40 17.959 37.666 132.407 1.00 45.02 C
ATOM 229 O ALA A 40 18.150 38.291 133.445 1.00 41.57 O
ATOM 230 CB ALA A 40 18.165 35.277 133.280 1.00 38.84 C
ATOM 231 N GLY A 41 18.294 38.181 131.224 1.00 45.16 N
ATOM 232 CA GLY A 41 18.805 39.529 131.202 1.00 42.75 C
ATOM 233 C GLY A 41 20.267 39.562 130.978 1.00 42.25 C
ATOM 234 O GLY A 41 20.794 40.618 130.797 1.00 44.58 O
ATOM 235 N PHE A 42 20.917 38.420 130.901 1.00 42.22 N
ATOM 236 CA PHE A 42 22.355 38.438 130.731 1.00 40.11 C
ATOM 237 C PHE A 42 22.798 38.604 129.259 1.00 43.30 C
ATOM 238 O PHE A 42 22.295 37.911 128.352 1.00 39.41 O
ATOM 239 CB PHE A 42 22.936 37.147 131.365 1.00 38.10 C
ATOM 240 CG PHE A 42 22.916 37.130 132.865 1.00 35.95 C
ATOM 241 CD1 PHE A 42 21.791 36.771 133.538 1.00 34.08 C
ATOM 242 CD2 PHE A 42 24.067 37.540 133.619 1.00 37.39 C
ATOM 243 CE1 PHE A 42 21.742 36.800 134.944 1.00 33.79 C
ATOM 244 CE2 PHE A 42 24.053 37.575 135.027 1.00 37.45 C
ATOM 245 CZ PHE A 42 22.841 37.192 135.687 1.00 38.50 C
ATOM 246 N ASN A 43 23.709 39.563 129.014 1.00 43.92 N
ATOM 247 CA ASN A 43 24.263 39.782 127.654 1.00 43.94 C
ATOM 248 C ASN A 43 25.153 38.556 127.433 1.00 43.23 C
ATOM 249 O ASN A 43 26.268 38.478 127.956 1.00 42.07 O
ATOM 250 CB ASN A 43 25.111 41.047 127.663 1.00 43.94 C
ATOM 251 CG ASN A 43 25.691 41.371 126.345 1.00 45.84 C
ATOM 252 OD1 ASN A 43 26.573 42.215 126.254 1.00 48.74 O
ATOM 253 ND2 ASN A 43 25.219 40.714 125.294 1.00 44.47 N
ATOM 254 N THR A 44 24.696 37.647 126.584 1.00 44.30 N
ATOM 255 CA THR A 44 25.372 36.344 126.434 1.00 42.06 C
ATOM 256 C THR A 44 25.930 36.053 125.077 1.00 41.02 C
ATOM 257 O THR A 44 25.298 36.381 124.120 1.00 42.36 O
ATOM 258 CB THR A 44 24.349 35.224 126.742 1.00 43.44 C
ATOM 259 OG1 THR A 44 23.685 35.527 127.981 1.00 41.52 O
ATOM 260 CG2 THR A 44 25.004 33.874 126.768 1.00 40.30 C
ATOM 261 N ALA A 45 27.107 35.418 124.995 1.00 39.99 N
ATOM 262 CA ALA A 45 27.698 35.047 123.724 1.00 39.85 C
ATOM 263 C ALA A 45 27.592 33.554 123.578 1.00 37.45 C
ATOM 264 O ALA A 45 27.735 32.900 124.542 1.00 39.28 O
ATOM 265 CB ALA A 45 29.173 35.465 123.692 1.00 39.80 C
ATOM 266 N CYS A 46 27.312 32.983 122.419 1.00 37.47 N
ATOM 267 CA CYS A 46 27.307 31.491 122.320 1.00 36.85 C
ATOM 268 C CYS A 46 28.348 31.172 121.254 1.00 35.49 C
ATOM 269 O CYS A 46 28.235 31.643 120.175 1.00 38.12 O
ATOM 270 CB CYS A 46 25.921 30.895 121.999 1.00 33.96 C
ATOM 271 SG CYS A 46 25.954 29.137 121.532 1.00 35.71 S
ATOM 272 N VAL A 47 29.375 30.373 121.579 1.00 36.12 N
ATOM 273 CA VAL A 47 30.484 30.106 120.666 1.00 33.11 C
ATOM 274 C VAL A 47 30.398 28.655 120.209 1.00 32.68 C
ATOM 275 O VAL A 47 30.480 27.762 121.021 1.00 29.07 O
ATOM 276 CB VAL A 47 31.849 30.341 121.412 1.00 34.92 C
ATOM 277 CG1 VAL A 47 33.043 30.020 120.464 1.00 32.44 C
ATOM 278 CG2 VAL A 47 31.957 31.848 121.842 1.00 33.98 C
ATOM 279 N THR A 48 30.338 28.376 118.902 1.00 30.39 N
ATOM 280 CA THR A 48 30.184 26.960 118.608 1.00 29.91 C
ATOM 281 C THR A 48 31.006 26.607 117.368 1.00 31.79 C
ATOM 282 O THR A 48 31.118 27.419 116.422 1.00 32.02 O
ATOM 283 CB THR A 48 28.570 26.656 118.400 1.00 24.98 C
ATOM 284 OG1 THR A 48 28.402 25.504 117.558 1.00 26.27 O
ATOM 285 CG2 THR A 48 27.926 27.815 117.609 1.00 25.15 C
ATOM 286 N LYS A 49 31.527 25.395 117.296 1.00 32.12 N
ATOM 287 CA LYS A 49 32.362 25.171 116.135 1.00 36.55 C
ATOM 288 C LYS A 49 31.542 24.731 114.895 1.00 36.65 C
ATOM 289 O LYS A 49 32.034 24.697 113.752 1.00 39.66 O
ATOM 290 CB LYS A 49 33.516 24.192 116.469 1.00 34.42 C
ATOM 291 CG LYS A 49 33.058 22.731 116.678 1.00 36.26 C
ATOM 292 CD LYS A 49 34.212 21.783 116.916 1.00 38.05 C
ATOM 293 CE LYS A 49 33.764 20.317 116.882 1.00 38.43 C
ATOM 294 NZ LYS A 49 34.988 19.541 117.272 1.00 31.35 N
ATOM 295 N LEU A 50 30.273 24.455 115.128 1.00 36.18 N
ATOM 296 CA LEU A 50 29.334 24.040 114.085 1.00 33.05 C
ATOM 297 C LEU A 50 28.162 25.030 114.053 1.00 33.97 C
ATOM 298 O LEU A 50 27.840 25.655 115.060 1.00 33.06 O
ATOM 299 CB LEU A 50 28.731 22.649 114.474 1.00 29.96 C
ATOM 300 CG LEU A 50 29.677 21.450 114.426 1.00 32.90 C
ATOM 301 CD1 LEU A 50 28.992 20.106 114.797 1.00 29.26 C
ATOM 302 CD2 LEU A 50 30.194 21.409 112.968 1.00 33.64 C
ATOM 303 N PHE A 51 27.439 25.069 112.935 1.00 33.77 N
ATOM 304 CA PHE A 51 26.221 25.855 112.911 1.00 30.48 C
ATOM 305 C PHE A 51 25.413 25.025 113.919 1.00 30.31 C
ATOM 306 O PHE A 51 25.427 23.757 113.844 1.00 30.89 O
ATOM 307 CB PHE A 51 25.615 25.812 111.517 1.00 31.38 C
ATOM 308 CG PHE A 51 24.264 26.472 111.436 1.00 29.91 C
ATOM 309 CD1 PHE A 51 24.147 27.883 111.535 1.00 33.03 C
ATOM 310 CD2 PHE A 51 23.130 25.693 111.401 1.00 28.10 C
ATOM 311 CE1 PHE A 51 22.847 28.519 111.638 1.00 32.70 C
ATOM 312 CE2 PHE A 51 21.852 26.263 111.470 1.00 27.27 C
ATOM 313 CZ PHE A 51 21.709 27.718 111.606 1.00 32.06 C
ATOM 314 N PRO A 52 24.662 25.688 114.847 1.00 30.19 N
ATOM 315 CA PRO A 52 23.931 24.892 115.833 1.00 29.16 C
ATOM 316 C PRO A 52 23.188 23.599 115.521 1.00 33.77 C
ATOM 317 O PRO A 52 23.302 22.676 116.309 1.00 34.56 O
ATOM 318 CB PRO A 52 23.026 25.891 116.515 1.00 28.17 C
ATOM 319 CG PRO A 52 23.767 27.265 116.312 1.00 27.53 C
ATOM 320 CD PRO A 52 24.390 27.152 114.997 1.00 28.11 C
ATOM 321 N THR A 53 22.465 23.510 114.401 1.00 31.78 N
ATOM 322 CA THR A 53 21.644 22.340 114.180 1.00 32.00 C
ATOM 323 C THR A 53 22.416 21.163 113.610 1.00 33.69 C
ATOM 324 O THR A 53 21.858 20.098 113.463 1.00 32.44 O
ATOM 325 CB THR A 53 20.382 22.663 113.269 1.00 30.40 C
ATOM 326 OG1 THR A 53 20.768 23.061 111.948 1.00 30.72 O
ATOM 327 CG2 THR A 53 19.617 23.764 113.819 1.00 30.50 C
ATOM 328 N ARG A 54 23.724 21.359 113.398 1.00 31.02 N
ATOM 329 CA ARG A 54 24.559 20.280 112.898 1.00 31.85 C
ATOM 330 C ARG A 54 25.067 19.515 114.070 1.00 32.74 C
ATOM 331 O ARG A 54 25.639 18.465 113.876 1.00 29.46 O
ATOM 332 CB ARG A 54 25.821 20.797 112.148 1.00 29.47 C
ATOM 333 CG ARG A 54 25.581 21.757 110.993 1.00 28.82 C
ATOM 334 CD ARG A 54 24.548 21.394 109.908 1.00 28.80 C
ATOM 335 NE ARG A 54 24.290 22.551 109.014 1.00 28.93 N
ATOM 336 CZ ARG A 54 23.172 22.703 108.276 1.00 29.33 C
ATOM 337 NH1 ARG A 54 22.186 21.813 108.266 1.00 26.89 N
ATOM 338 NH2 ARG A 54 23.050 23.758 107.572 1.00 30.32 N
ATOM 339 N SER A 55 24.877 20.022 115.303 1.00 34.14 N
ATOM 340 CA SER A 55 25.436 19.351 116.496 1.00 31.45 C
ATOM 341 C SER A 55 24.943 17.945 116.672 1.00 34.38 C
ATOM 342 O SER A 55 23.790 17.645 116.313 1.00 33.61 O
ATOM 343 CB SER A 55 25.077 20.143 117.726 1.00 30.74 C
ATOM 344 OG SER A 55 25.485 21.530 117.538 1.00 34.82 O
ATOM 345 N HIS A 56 25.741 17.122 117.353 1.00 31.67 N
ATOM 346 CA HIS A 56 25.382 15.734 117.487 1.00 32.77 C
ATOM 347 C HIS A 56 23.989 15.472 118.064 1.00 30.06 C
ATOM 348 O HIS A 56 23.432 14.440 117.795 1.00 30.74 O
ATOM 349 CB HIS A 56 26.456 14.897 118.305 1.00 30.95 C
ATOM 350 CG HIS A 56 26.196 13.406 118.262 1.00 29.85 C
ATOM 351 ND1 HIS A 56 26.305 12.677 117.112 1.00 27.45 N
ATOM 352 CD2 HIS A 56 25.777 12.533 119.210 1.00 29.98 C
ATOM 353 CE1 HIS A 56 25.970 11.417 117.336 1.00 27.63 C
ATOM 354 NE2 HIS A 56 25.639 11.305 118.601 1.00 30.82 N
ATOM 355 N THR A 57 23.539 16.339 118.947 1.00 29.88 N
ATOM 356 CA THR A 57 22.169 16.275 119.532 1.00 31.31 C
ATOM 357 C THR A 57 21.116 16.036 118.392 1.00 32.42 C
ATOM 358 O THR A 57 20.144 15.308 118.602 1.00 34.71 O
ATOM 359 CB THR A 57 21.770 17.635 120.194 1.00 28.89 C
ATOM 360 OG1 THR A 57 22.518 17.850 121.403 1.00 28.62 O
ATOM 361 CG2 THR A 57 20.181 17.629 120.596 1.00 30.07 C
ATOM 362 N VAL A 58 21.324 16.649 117.207 1.00 32.73 N
ATOM 363 CA VAL A 58 20.418 16.480 116.067 1.00 29.67 C
ATOM 364 C VAL A 58 20.178 15.004 115.623 1.00 33.01 C
ATOM 365 O VAL A 58 19.117 14.677 115.033 1.00 27.07 O
ATOM 366 CB VAL A 58 20.896 17.367 114.838 1.00 30.08 C
ATOM 367 CG1 VAL A 58 22.140 16.824 114.016 1.00 26.30 C
ATOM 368 CG2 VAL A 58 19.745 17.527 113.856 1.00 24.98 C
ATOM 369 N ALA A 59 21.117 14.110 115.978 1.00 30.79 N
ATOM 370 CA ALA A 59 21.066 12.692 115.534 1.00 28.07 C
ATOM 371 C ALA A 59 20.397 11.849 116.551 1.00 33.47 C
ATOM 372 O ALA A 59 20.282 10.629 116.315 1.00 33.01 O
ATOM 373 CB ALA A 59 22.486 12.139 115.349 1.00 30.59 C
ATOM 374 N ALA A 60 20.057 12.441 117.719 1.00 31.05 N
ATOM 375 CA ALA A 60 19.378 11.621 118.742 1.00 33.42 C
ATOM 376 C ALA A 60 18.025 11.089 118.278 1.00 33.50 C
ATOM 377 O ALA A 60 17.330 11.727 117.494 1.00 30.22 O
ATOM 378 CB ALA A 60 19.294 12.380 120.103 1.00 32.87 C
ATOM 379 N GLN A 61 17.681 9.873 118.724 1.00 36.94 N
ATOM 380 CA GLN A 61 16.492 9.237 118.194 1.00 34.70 C
ATOM 381 C GLN A 61 15.310 8.798 119.091 1.00 37.97 C
ATOM 382 O GLN A 61 14.185 9.315 118.933 1.00 34.79 O
ATOM 383 CB GLN A 61 16.921 8.036 117.386 1.00 36.51 C
ATOM 384 CG GLN A 61 17.964 8.241 116.222 1.00 35.08 C
ATOM 385 CD GLN A 61 18.399 6.852 115.600 1.00 37.23 C
ATOM 386 OE1 GLN A 61 17.838 5.777 115.977 1.00 37.95 O
ATOM 387 NE2 GLN A 61 19.381 6.861 114.700 1.00 33.96 N
ATOM 388 N GLY A 62 15.550 7.844 119.989 1.00 35.84 N
ATOM 389 CA GLY A 62 14.472 7.274 120.781 1.00 36.59 C
ATOM 390 C GLY A 62 13.627 8.151 121.703 1.00 37.73 C
ATOM 391 O GLY A 62 12.404 7.931 121.846 1.00 41.07 O
ATOM 392 N GLY A 63 14.221 9.145 122.342 1.00 32.78 N
ATOM 393 CA GLY A 63 13.387 9.962 123.200 1.00 31.84 C
ATOM 394 C GLY A 63 14.054 10.673 124.341 1.00 30.43 C
ATOM 395 O GLY A 63 15.325 10.751 124.453 1.00 30.01 O
ATOM 396 N ILE A 64 13.205 11.208 125.207 1.00 30.64 N
ATOM 397 CA ILE A 64 13.674 11.975 126.413 1.00 28.97 C
ATOM 398 C ILE A 64 12.695 11.567 127.500 1.00 31.60 C
ATOM 399 O ILE A 64 11.490 11.563 127.281 1.00 36.52 O
ATOM 400 CB ILE A 64 13.674 13.553 126.130 1.00 28.26 C
ATOM 401 CG1 ILE A 64 14.000 14.370 127.409 1.00 26.07 C
ATOM 402 CG2 ILE A 64 12.320 13.956 125.446 1.00 28.90 C
ATOM 403 CD1 ILE A 64 14.125 15.941 127.066 1.00 29.21 C
ATOM 404 N ASN A 65 13.191 11.170 128.666 1.00 34.13 N
ATOM 405 CA ASN A 65 12.329 10.712 129.737 1.00 31.55 C
ATOM 406 C ASN A 65 11.707 11.784 130.622 1.00 34.16 C
ATOM 407 O ASN A 65 12.352 12.790 130.930 1.00 31.96 O
ATOM 408 CB ASN A 65 13.126 9.762 130.652 1.00 32.78 C
ATOM 409 CG ASN A 65 13.636 8.497 129.920 1.00 34.49 C
ATOM 410 OD1 ASN A 65 12.890 7.875 129.225 1.00 35.10 O
ATOM 411 ND2 ASN A 65 14.932 8.133 130.107 1.00 34.74 N
ATOM 412 N ALA A 66 10.450 11.546 131.025 1.00 29.87 N
ATOM 413 CA ALA A 66 9.788 12.404 131.981 1.00 31.34 C
ATOM 414 C ALA A 66 8.579 11.644 132.412 1.00 31.81 C
ATOM 415 O ALA A 66 7.901 11.023 131.608 1.00 30.99 O
ATOM 416 CB ALA A 66 9.399 13.741 131.422 1.00 22.87 C
ATOM 417 N ALA A 67 8.309 11.689 133.700 1.00 33.23 N
ATOM 418 CA ALA A 67 7.170 10.935 134.218 1.00 37.17 C
ATOM 419 C ALA A 67 5.929 11.779 133.991 1.00 35.15 C
ATOM 420 O ALA A 67 5.385 12.323 134.888 1.00 36.38 O
ATOM 421 CB ALA A 67 7.382 10.584 135.729 1.00 31.45 C
ATOM 422 N LEU A 68 5.508 11.929 132.756 1.00 34.47 N
ATOM 423 CA LEU A 68 4.317 12.724 132.518 1.00 36.06 C
ATOM 424 C LEU A 68 3.110 11.871 132.858 1.00 37.86 C
ATOM 425 O LEU A 68 2.068 12.380 133.095 1.00 39.34 O
ATOM 426 CB LEU A 68 4.242 13.159 131.038 1.00 34.16 C
ATOM 427 CG LEU A 68 5.277 14.243 130.633 1.00 37.05 C
ATOM 428 CD1 LEU A 68 5.151 14.607 129.119 1.00 29.72 C
ATOM 429 CD2 LEU A 68 5.002 15.475 131.470 1.00 34.93 C
ATOM 430 N GLY A 69 3.246 10.552 132.849 1.00 39.24 N
ATOM 431 CA GLY A 69 2.087 9.724 133.107 1.00 37.45 C
ATOM 432 C GLY A 69 1.037 9.797 131.985 1.00 38.79 C
ATOM 433 O GLY A 69 -0.171 9.680 132.221 1.00 35.79 O
ATOM 434 N ASN A 70 1.458 9.952 130.744 1.00 36.41 N
ATOM 435 CA ASN A 70 0.480 9.992 129.713 1.00 35.94 C
ATOM 436 C ASN A 70 0.068 8.530 129.239 1.00 39.87 C
ATOM 437 O ASN A 70 -0.916 8.335 128.451 1.00 37.72 O
ATOM 438 CB ASN A 70 1.031 10.719 128.520 1.00 36.34 C
ATOM 439 CG ASN A 70 1.309 12.155 128.770 1.00 36.42 C
ATOM 440 OD1 ASN A 70 0.773 12.762 129.668 1.00 33.59 O
ATOM 441 ND2 ASN A 70 2.162 12.724 127.938 1.00 35.89 N
ATOM 442 N MET A 71 0.771 7.501 129.689 1.00 37.98 N
ATOM 443 CA MET A 71 0.374 6.161 129.178 1.00 38.25 C
ATOM 444 C MET A 71 -0.137 5.323 130.359 1.00 41.88 C
ATOM 445 O MET A 71 -0.879 4.370 130.165 1.00 45.34 O
ATOM 446 CB MET A 71 1.567 5.391 128.526 1.00 37.66 C
ATOM 447 CG MET A 71 2.443 6.097 127.412 1.00 33.06 C
ATOM 448 SD MET A 71 1.544 7.005 126.206 1.00 39.70 S
ATOM 449 CE MET A 71 1.381 5.656 125.068 1.00 29.89 C
ATOM 450 N GLU A 72 0.284 5.668 131.575 1.00 39.58 N
ATOM 451 CA GLU A 72 -0.147 4.963 132.753 1.00 42.00 C
ATOM 452 C GLU A 72 0.287 5.934 133.838 1.00 41.43 C
ATOM 453 O GLU A 72 1.073 6.834 133.572 1.00 45.30 O
ATOM 454 CB GLU A 72 0.613 3.617 132.881 1.00 40.73 C
ATOM 455 CG GLU A 72 2.091 3.796 133.286 1.00 43.43 C
ATOM 456 CD GLU A 72 3.067 3.555 132.135 1.00 49.28 C
ATOM 457 OE1 GLU A 72 3.013 2.455 131.516 1.00 51.58 O
ATOM 458 OE2 GLU A 72 3.893 4.455 131.830 1.00 47.02 O
ATOM 459 N ASP A 73 -0.216 5.764 135.038 1.00 39.62 N
ATOM 460 CA ASP A 73 0.186 6.560 136.167 1.00 40.87 C
ATOM 461 C ASP A 73 1.691 6.334 136.393 1.00 38.45 C
ATOM 462 O ASP A 73 2.213 5.191 136.282 1.00 39.04 O
ATOM 463 CB ASP A 73 -0.580 6.134 137.420 1.00 42.95 C
ATOM 464 CG ASP A 73 -2.040 6.586 137.387 1.00 51.19 C
ATOM 465 OD1 ASP A 73 -2.435 7.395 136.492 1.00 51.53 O
ATOM 466 OD2 ASP A 73 -2.809 6.140 138.277 1.00 55.96 O
ATOM 467 N ASP A 74 2.367 7.412 136.764 1.00 37.47 N
ATOM 468 CA ASP A 74 3.821 7.345 136.916 1.00 38.20 C
ATOM 469 C ASP A 74 4.207 8.200 138.125 1.00 39.42 C
ATOM 470 O ASP A 74 3.336 8.756 138.822 1.00 38.54 O
ATOM 471 CB ASP A 74 4.451 7.790 135.587 1.00 31.91 C
ATOM 472 CG ASP A 74 5.936 7.356 135.444 1.00 39.69 C
ATOM 473 OD1 ASP A 74 6.468 6.765 136.391 1.00 34.73 O
ATOM 474 OD2 ASP A 74 6.605 7.589 134.392 1.00 34.71 O
ATOM 475 N ASN A 75 5.490 8.264 138.438 1.00 39.08 N
ATOM 476 CA ASN A 75 5.916 9.036 139.583 1.00 37.90 C
ATOM 477 C ASN A 75 7.364 9.404 139.251 1.00 38.39 C
ATOM 478 O ASN A 75 8.142 8.557 138.841 1.00 36.56 O
ATOM 479 CB ASN A 75 5.819 8.138 140.825 1.00 37.65 C
ATOM 480 CG ASN A 75 6.081 8.894 142.120 1.00 39.90 C
ATOM 481 OD1 ASN A 75 7.075 9.637 142.255 1.00 39.22 O
ATOM 482 ND2 ASN A 75 5.192 8.712 143.087 1.00 41.70 N
ATOM 483 N TRP A 76 7.746 10.657 139.419 1.00 36.66 N
ATOM 484 CA TRP A 76 9.091 10.978 139.013 1.00 35.64 C
ATOM 485 C TRP A 76 10.091 10.263 139.886 1.00 36.84 C
ATOM 486 O TRP A 76 11.224 9.998 139.464 1.00 39.16 O
ATOM 487 CB TRP A 76 9.303 12.519 138.965 1.00 33.53 C
ATOM 488 CG TRP A 76 9.263 13.185 140.329 1.00 37.49 C
ATOM 489 CD1 TRP A 76 8.148 13.806 140.967 1.00 33.15 C
ATOM 490 CD2 TRP A 76 10.316 13.241 141.269 1.00 37.43 C
ATOM 491 NE1 TRP A 76 8.509 14.204 142.196 1.00 32.93 N
ATOM 492 CE2 TRP A 76 9.814 13.884 142.425 1.00 33.93 C
ATOM 493 CE3 TRP A 76 11.651 12.818 141.252 1.00 39.38 C
ATOM 494 CZ2 TRP A 76 10.586 14.118 143.548 1.00 35.92 C
ATOM 495 CZ3 TRP A 76 12.425 13.060 142.403 1.00 38.89 C
ATOM 496 CH2 TRP A 76 11.882 13.711 143.524 1.00 35.75 C
ATOM 497 N ARG A 77 9.680 9.934 141.107 1.00 36.12 N
ATOM 498 CA ARG A 77 10.576 9.232 141.995 1.00 35.61 C
ATOM 499 C ARG A 77 10.890 7.807 141.502 1.00 36.61 C
ATOM 500 O ARG A 77 12.001 7.275 141.779 1.00 36.01 O
ATOM 501 CB ARG A 77 10.025 9.210 143.402 1.00 35.60 C
ATOM 502 CG ARG A 77 9.754 10.623 143.881 1.00 37.46 C
ATOM 503 CD ARG A 77 8.866 10.564 145.204 1.00 33.33 C
ATOM 504 NE ARG A 77 8.430 11.884 145.618 1.00 30.54 N
ATOM 505 CZ ARG A 77 7.431 12.531 145.026 1.00 35.16 C
ATOM 506 NH1 ARG A 77 6.800 11.927 144.007 1.00 33.93 N
ATOM 507 NH2 ARG A 77 7.078 13.772 145.428 1.00 33.23 N
ATOM 508 N TRP A 78 9.975 7.226 140.742 1.00 33.79 N
ATOM 509 CA TRP A 78 10.227 5.917 140.119 1.00 36.83 C
ATOM 510 C TRP A 78 11.377 6.075 139.071 1.00 37.39 C
ATOM 511 O TRP A 78 12.254 5.178 138.946 1.00 32.58 O
ATOM 512 CB TRP A 78 8.976 5.443 139.403 1.00 34.97 C
ATOM 513 CG TRP A 78 7.939 5.159 140.390 1.00 35.94 C
ATOM 514 CD1 TRP A 78 8.103 5.083 141.751 1.00 36.70 C
ATOM 515 CD2 TRP A 78 6.569 4.828 140.122 1.00 38.30 C
ATOM 516 NE1 TRP A 78 6.907 4.727 142.365 1.00 39.39 N
ATOM 517 CE2 TRP A 78 5.944 4.571 141.385 1.00 39.39 C
ATOM 518 CE3 TRP A 78 5.808 4.707 138.943 1.00 36.22 C
ATOM 519 CZ2 TRP A 78 4.562 4.218 141.495 1.00 37.40 C
ATOM 520 CZ3 TRP A 78 4.444 4.347 139.047 1.00 38.70 C
ATOM 521 CH2 TRP A 78 3.834 4.114 140.331 1.00 37.57 C
ATOM 522 N HIS A 79 11.391 7.255 138.401 1.00 33.64 N
ATOM 523 CA HIS A 79 12.382 7.566 137.414 1.00 33.20 C
ATOM 524 C HIS A 79 13.708 7.755 138.134 1.00 35.25 C
ATOM 525 O HIS A 79 14.752 7.270 137.659 1.00 36.38 O
ATOM 526 CB HIS A 79 11.911 8.796 136.653 1.00 32.81 C
ATOM 527 CG HIS A 79 12.775 9.210 135.508 1.00 36.28 C
ATOM 528 ND1 HIS A 79 12.578 10.404 134.829 1.00 34.57 N
ATOM 529 CD2 HIS A 79 13.891 8.650 134.975 1.00 34.08 C
ATOM 530 CE1 HIS A 79 13.535 10.558 133.933 1.00 34.50 C
ATOM 531 NE2 HIS A 79 14.351 9.507 134.004 1.00 35.22 N
ATOM 532 N PHE A 80 13.653 8.437 139.287 1.00 36.78 N
ATOM 533 CA PHE A 80 14.841 8.710 140.119 1.00 39.14 C
ATOM 534 C PHE A 80 15.522 7.391 140.446 1.00 40.04 C
ATOM 535 O PHE A 80 16.743 7.200 140.256 1.00 39.98 O
ATOM 536 CB PHE A 80 14.439 9.433 141.426 1.00 38.50 C
ATOM 537 CG PHE A 80 15.507 9.394 142.532 1.00 37.94 C
ATOM 538 CD1 PHE A 80 16.551 10.336 142.563 1.00 36.43 C
ATOM 539 CD2 PHE A 80 15.465 8.417 143.533 1.00 36.16 C
ATOM 540 CE1 PHE A 80 17.541 10.325 143.526 1.00 34.93 C
ATOM 541 CE2 PHE A 80 16.472 8.391 144.524 1.00 37.47 C
ATOM 542 CZ PHE A 80 17.529 9.363 144.504 1.00 34.22 C
ATOM 543 N TYR A 81 14.705 6.464 140.891 1.00 40.88 N
ATOM 544 CA TYR A 81 15.178 5.149 141.270 1.00 42.52 C
ATOM 545 C TYR A 81 15.833 4.365 140.140 1.00 40.80 C
ATOM 546 O TYR A 81 16.856 3.679 140.319 1.00 40.29 O
ATOM 547 CB TYR A 81 14.005 4.346 141.818 1.00 41.20 C
ATOM 548 CG TYR A 81 14.380 2.917 142.166 1.00 40.38 C
ATOM 549 CD1 TYR A 81 14.944 2.615 143.401 1.00 41.84 C
ATOM 550 CD2 TYR A 81 14.223 1.897 141.239 1.00 36.67 C
ATOM 551 CE1 TYR A 81 15.354 1.306 143.692 1.00 44.08 C
ATOM 552 CE2 TYR A 81 14.615 0.607 141.496 1.00 38.12 C
ATOM 553 CZ TYR A 81 15.190 0.314 142.719 1.00 44.39 C
ATOM 554 OH TYR A 81 15.721 -0.934 142.968 1.00 48.28 O
ATOM 555 N ASP A 82 15.160 4.398 138.998 1.00 38.34 N
ATOM 556 CA ASP A 82 15.644 3.737 137.834 1.00 35.58 C
ATOM 557 C ASP A 82 17.000 4.317 137.475 1.00 36.08 C
ATOM 558 O ASP A 82 17.875 3.599 137.111 1.00 35.55 O
ATOM 559 CB ASP A 82 14.654 3.894 136.650 1.00 35.63 C
ATOM 560 CG ASP A 82 13.345 3.020 136.814 1.00 42.54 C
ATOM 561 OD1 ASP A 82 13.428 1.931 137.478 1.00 42.28 O
ATOM 562 OD2 ASP A 82 12.228 3.388 136.276 1.00 38.04 O
ATOM 563 N THR A 83 17.177 5.629 137.606 1.00 34.22 N
ATOM 564 CA THR A 83 18.399 6.239 137.203 1.00 32.88 C
ATOM 565 C THR A 83 19.520 5.939 138.173 1.00 34.48 C
ATOM 566 O THR A 83 20.655 5.681 137.751 1.00 37.65 O
ATOM 567 CB THR A 83 18.162 7.765 137.004 1.00 35.60 C
ATOM 568 OG1 THR A 83 17.110 7.932 136.019 1.00 36.66 O
ATOM 569 CG2 THR A 83 19.448 8.469 136.534 1.00 26.81 C
ATOM 570 N VAL A 84 19.210 5.960 139.465 1.00 36.17 N
ATOM 571 CA VAL A 84 20.171 5.649 140.458 1.00 36.40 C
ATOM 572 C VAL A 84 20.598 4.174 140.290 1.00 38.41 C
ATOM 573 O VAL A 84 21.820 3.855 140.298 1.00 39.14 O
ATOM 574 CB VAL A 84 19.645 5.840 141.892 1.00 36.93 C
ATOM 575 CG1 VAL A 84 20.708 5.246 142.844 1.00 35.32 C
ATOM 576 CG2 VAL A 84 19.415 7.363 142.250 1.00 34.03 C
ATOM 577 N LYS A 85 19.650 3.268 140.149 1.00 36.48 N
ATOM 578 CA LYS A 85 20.068 1.868 140.004 1.00 37.53 C
ATOM 579 C LYS A 85 20.886 1.732 138.721 1.00 40.56 C
ATOM 580 O LYS A 85 21.968 1.082 138.705 1.00 39.04 O
ATOM 581 CB LYS A 85 18.883 0.970 139.881 1.00 37.50 C
ATOM 582 CG LYS A 85 19.264 -0.504 139.615 1.00 38.96 C
ATOM 583 CD LYS A 85 18.019 -1.370 139.460 1.00 40.33 C
ATOM 584 CE LYS A 85 18.395 -2.823 139.219 1.00 42.71 C
ATOM 585 NZ LYS A 85 17.216 -3.706 138.993 1.00 45.58 N
ATOM 586 N GLY A 86 20.375 2.348 137.649 1.00 39.36 N
ATOM 587 CA GLY A 86 21.081 2.292 136.395 1.00 36.39 C
ATOM 588 C GLY A 86 22.496 2.852 136.547 1.00 37.26 C
ATOM 589 O GLY A 86 23.402 2.380 135.932 1.00 38.81 O
ATOM 590 N SER A 87 22.723 3.892 137.330 1.00 38.03 N
ATOM 591 CA SER A 87 24.064 4.409 137.403 1.00 36.86 C
ATOM 592 C SER A 87 25.006 3.493 138.184 1.00 37.49 C
ATOM 593 O SER A 87 26.181 3.778 138.286 1.00 36.79 O
ATOM 594 CB SER A 87 24.041 5.797 138.082 1.00 36.26 C
ATOM 595 OG SER A 87 23.899 5.647 139.494 1.00 40.32 O
ATOM 596 N ASP A 88 24.469 2.435 138.791 1.00 40.97 N
ATOM 597 CA ASP A 88 25.208 1.461 139.589 1.00 38.01 C
ATOM 598 C ASP A 88 25.864 2.126 140.723 1.00 39.70 C
ATOM 599 O ASP A 88 26.987 1.824 141.073 1.00 37.22 O
ATOM 600 CB ASP A 88 26.272 0.714 138.760 1.00 40.45 C
ATOM 601 CG ASP A 88 26.489 -0.760 139.228 1.00 40.40 C
ATOM 602 OD1 ASP A 88 25.935 -1.124 140.289 1.00 36.22 O
ATOM 603 OD2 ASP A 88 27.202 -1.522 138.528 1.00 36.79 O
ATOM 604 N TRP A 89 25.166 3.106 141.270 1.00 40.69 N
ATOM 605 CA TRP A 89 25.607 3.820 142.456 1.00 37.36 C
ATOM 606 C TRP A 89 26.870 4.593 142.324 1.00 40.95 C
ATOM 607 O TRP A 89 27.585 4.869 143.345 1.00 39.25 O
ATOM 608 CB TRP A 89 25.630 2.891 143.702 1.00 37.77 C
ATOM 609 CG TRP A 89 24.130 2.575 144.202 1.00 35.30 C
ATOM 610 CD1 TRP A 89 23.308 3.337 145.022 1.00 32.39 C
ATOM 611 CD2 TRP A 89 23.310 1.531 143.681 1.00 32.19 C
ATOM 612 NE1 TRP A 89 22.016 2.807 145.012 1.00 34.06 N
ATOM 613 CE2 TRP A 89 22.003 1.704 144.198 1.00 32.58 C
ATOM 614 CE3 TRP A 89 23.562 0.468 142.815 1.00 32.87 C
ATOM 615 CZ2 TRP A 89 20.960 0.836 143.892 1.00 35.61 C
ATOM 616 CZ3 TRP A 89 22.482 -0.444 142.480 1.00 34.30 C
ATOM 617 CH2 TRP A 89 21.212 -0.241 143.032 1.00 32.09 C
ATOM 618 N LEU A 90 27.132 5.021 141.086 1.00 39.05 N
ATOM 619 CA LEU A 90 28.278 5.899 140.950 1.00 38.78 C
ATOM 620 C LEU A 90 27.650 7.309 140.644 1.00 40.60 C
ATOM 621 O LEU A 90 28.359 8.324 140.470 1.00 37.72 O
ATOM 622 CB LEU A 90 29.192 5.408 139.848 1.00 37.68 C
ATOM 623 CG LEU A 90 30.416 6.301 139.805 1.00 43.12 C
ATOM 624 CD1 LEU A 90 31.367 6.127 141.076 1.00 45.20 C
ATOM 625 CD2 LEU A 90 31.101 5.928 138.531 1.00 42.26 C
ATOM 626 N GLY A 91 26.308 7.361 140.625 1.00 37.52 N
ATOM 627 CA GLY A 91 25.651 8.615 140.327 1.00 35.24 C
ATOM 628 C GLY A 91 25.397 9.401 141.566 1.00 35.06 C
ATOM 629 O GLY A 91 25.163 8.811 142.605 1.00 35.67 O
ATOM 630 N ASP A 92 25.449 10.711 141.466 1.00 32.31 N
ATOM 631 CA ASP A 92 25.219 11.548 142.605 1.00 34.29 C
ATOM 632 C ASP A 92 23.683 11.720 142.677 1.00 35.50 C
ATOM 633 O ASP A 92 23.048 12.254 141.767 1.00 35.27 O
ATOM 634 CB ASP A 92 25.990 12.869 142.367 1.00 35.82 C
ATOM 635 CG ASP A 92 27.476 12.612 142.171 1.00 39.39 C
ATOM 636 OD1 ASP A 92 28.110 11.885 142.985 1.00 40.12 O
ATOM 637 OD2 ASP A 92 28.049 13.115 141.205 1.00 45.28 O
ATOM 638 N GLN A 93 23.095 11.335 143.785 1.00 37.65 N
ATOM 639 CA GLN A 93 21.618 11.356 143.890 1.00 35.42 C
ATOM 640 C GLN A 93 20.976 12.702 144.047 1.00 36.31 C
ATOM 641 O GLN A 93 19.732 12.863 143.871 1.00 38.91 O
ATOM 642 CB GLN A 93 21.241 10.358 144.999 1.00 38.57 C
ATOM 643 CG GLN A 93 21.805 8.974 144.677 1.00 32.20 C
ATOM 644 CD GLN A 93 21.274 7.927 145.643 1.00 38.31 C
ATOM 645 OE1 GLN A 93 20.112 7.999 146.080 1.00 37.91 O
ATOM 646 NE2 GLN A 93 22.107 6.937 145.972 1.00 31.98 N
ATOM 647 N ASP A 94 21.795 13.703 144.375 1.00 34.52 N
ATOM 648 CA ASP A 94 21.234 15.038 144.501 1.00 35.62 C
ATOM 649 C ASP A 94 20.965 15.502 143.084 1.00 36.41 C
ATOM 650 O ASP A 94 19.854 15.905 142.791 1.00 38.10 O
ATOM 651 CB ASP A 94 22.139 15.985 145.304 1.00 36.73 C
ATOM 652 CG ASP A 94 23.622 16.070 144.769 1.00 38.51 C
ATOM 653 OD1 ASP A 94 24.109 15.215 143.999 1.00 37.09 O
ATOM 654 OD2 ASP A 94 24.292 17.040 145.162 1.00 42.51 O
ATOM 655 N ALA A 95 21.928 15.296 142.181 1.00 36.53 N
ATOM 656 CA ALA A 95 21.789 15.670 140.760 1.00 35.06 C
ATOM 657 C ALA A 95 20.697 14.843 140.134 1.00 33.44 C
ATOM 658 O ALA A 95 19.880 15.392 139.385 1.00 34.69 O
ATOM 659 CB ALA A 95 23.098 15.438 139.986 1.00 33.56 C
ATOM 660 N ILE A 96 20.677 13.522 140.424 1.00 32.02 N
ATOM 661 CA ILE A 96 19.670 12.643 139.876 1.00 28.21 C
ATOM 662 C ILE A 96 18.320 13.058 140.412 1.00 29.21 C
ATOM 663 O ILE A 96 17.364 13.008 139.709 1.00 33.49 O
ATOM 664 CB ILE A 96 19.929 11.188 140.232 1.00 29.26 C
ATOM 665 CG1 ILE A 96 21.298 10.764 139.640 1.00 30.19 C
ATOM 666 CG2 ILE A 96 18.748 10.345 139.734 1.00 27.00 C
ATOM 667 CD1 ILE A 96 21.716 9.181 139.734 1.00 26.86 C
ATOM 668 N HIS A 97 18.247 13.496 141.651 1.00 32.76 N
ATOM 669 CA HIS A 97 16.959 13.910 142.184 1.00 37.24 C
ATOM 670 C HIS A 97 16.460 15.059 141.341 1.00 36.95 C
ATOM 671 O HIS A 97 15.302 15.041 140.849 1.00 35.38 O
ATOM 672 CB HIS A 97 17.091 14.381 143.649 1.00 35.39 C
ATOM 673 CG HIS A 97 15.827 14.911 144.271 1.00 39.20 C
ATOM 674 ND1 HIS A 97 15.622 14.901 145.632 1.00 38.52 N
ATOM 675 CD2 HIS A 97 14.763 15.586 143.749 1.00 43.56 C
ATOM 676 CE1 HIS A 97 14.505 15.553 145.926 1.00 40.22 C
ATOM 677 NE2 HIS A 97 13.971 15.988 144.800 1.00 40.86 N
ATOM 678 N TYR A 98 17.338 16.047 141.170 1.00 36.81 N
ATOM 679 CA TYR A 98 16.978 17.290 140.455 1.00 35.80 C
ATOM 680 C TYR A 98 16.583 16.993 139.043 1.00 36.65 C
ATOM 681 O TYR A 98 15.580 17.476 138.513 1.00 38.27 O
ATOM 682 CB TYR A 98 18.196 18.218 140.448 1.00 33.48 C
ATOM 683 CG TYR A 98 17.957 19.526 139.795 1.00 32.48 C
ATOM 684 CD1 TYR A 98 18.279 19.746 138.481 1.00 33.01 C
ATOM 685 CD2 TYR A 98 17.362 20.556 140.515 1.00 35.46 C
ATOM 686 CE1 TYR A 98 18.009 20.953 137.888 1.00 36.24 C
ATOM 687 CE2 TYR A 98 17.067 21.805 139.931 1.00 36.71 C
ATOM 688 CZ TYR A 98 17.387 21.984 138.605 1.00 39.08 C
ATOM 689 OH TYR A 98 16.913 23.109 137.987 1.00 37.11 O
ATOM 690 N MET A 99 17.371 16.128 138.410 1.00 38.60 N
ATOM 691 CA MET A 99 17.105 15.828 137.014 1.00 34.59 C
ATOM 692 C MET A 99 15.740 15.223 136.776 1.00 35.50 C
ATOM 693 O MET A 99 15.026 15.653 135.892 1.00 31.09 O
ATOM 694 CB MET A 99 18.159 14.886 136.460 1.00 35.93 C
ATOM 695 CG MET A 99 17.889 14.722 135.031 1.00 36.89 C
ATOM 696 SD MET A 99 19.003 13.700 134.012 1.00 39.46 S
ATOM 697 CE MET A 99 18.759 11.956 134.664 1.00 29.00 C
ATOM 698 N THR A 100 15.419 14.184 137.551 1.00 35.90 N
ATOM 699 CA THR A 100 14.152 13.493 137.423 1.00 32.55 C
ATOM 700 C THR A 100 12.938 14.281 137.938 1.00 34.84 C
ATOM 701 O THR A 100 11.840 14.163 137.379 1.00 34.12 O
ATOM 702 CB THR A 100 14.222 12.134 138.086 1.00 31.47 C
ATOM 703 OG1 THR A 100 14.660 12.271 139.470 1.00 26.53 O
ATOM 704 CG2 THR A 100 15.235 11.276 137.284 1.00 31.43 C
ATOM 705 N GLU A 101 13.118 15.106 138.954 1.00 35.52 N
ATOM 706 CA GLU A 101 11.944 15.814 139.385 1.00 38.02 C
ATOM 707 C GLU A 101 11.728 16.914 138.421 1.00 39.34 C
ATOM 708 O GLU A 101 10.587 17.280 138.153 1.00 35.55 O
ATOM 709 CB GLU A 101 12.103 16.370 140.785 1.00 42.39 C
ATOM 710 CG GLU A 101 10.904 17.165 141.343 1.00 46.28 C
ATOM 711 CD GLU A 101 11.262 17.893 142.700 1.00 47.73 C
ATOM 712 OE1 GLU A 101 12.433 17.994 143.090 1.00 45.67 O
ATOM 713 OE2 GLU A 101 10.362 18.368 143.391 1.00 50.44 O
ATOM 714 N GLN A 102 12.816 17.455 137.854 1.00 36.85 N
ATOM 715 CA GLN A 102 12.589 18.551 136.892 1.00 35.38 C
ATOM 716 C GLN A 102 12.115 18.037 135.529 1.00 33.52 C
ATOM 717 O GLN A 102 11.734 18.839 134.668 1.00 34.20 O
ATOM 718 CB GLN A 102 13.908 19.330 136.647 1.00 33.03 C
ATOM 719 CG GLN A 102 14.352 20.225 137.836 1.00 36.79 C
ATOM 720 CD GLN A 102 13.182 21.047 138.470 1.00 38.34 C
ATOM 721 OE1 GLN A 102 12.491 21.816 137.806 1.00 35.62 O
ATOM 722 NE2 GLN A 102 13.013 20.890 139.764 1.00 38.81 N
ATOM 723 N ALA A 103 12.132 16.718 135.281 1.00 30.00 N
ATOM 724 CA ALA A 103 11.846 16.286 133.916 1.00 25.92 C
ATOM 725 C ALA A 103 10.539 16.639 133.237 1.00 27.83 C
ATOM 726 O ALA A 103 10.516 17.021 132.075 1.00 29.75 O
ATOM 727 CB ALA A 103 12.167 14.663 133.735 1.00 28.13 C
ATOM 728 N PRO A 104 9.419 16.479 133.927 1.00 29.31 N
ATOM 729 CA PRO A 104 8.081 16.774 133.383 1.00 29.69 C
ATOM 730 C PRO A 104 8.037 18.226 132.956 1.00 31.52 C
ATOM 731 O PRO A 104 7.548 18.529 131.901 1.00 34.53 O
ATOM 732 CB PRO A 104 7.125 16.516 134.623 1.00 26.51 C
ATOM 733 CG PRO A 104 7.922 15.410 135.328 1.00 31.91 C
ATOM 734 CD PRO A 104 9.325 16.058 135.318 1.00 26.29 C
ATOM 735 N ALA A 105 8.571 19.126 133.777 1.00 31.80 N
ATOM 736 CA ALA A 105 8.478 20.540 133.415 1.00 32.10 C
ATOM 737 C ALA A 105 9.437 20.815 132.239 1.00 32.89 C
ATOM 738 O ALA A 105 9.189 21.642 131.375 1.00 35.65 O
ATOM 739 CB ALA A 105 8.854 21.430 134.682 1.00 28.63 C
ATOM 740 N ALA A 106 10.510 20.061 132.132 1.00 34.53 N
ATOM 741 CA ALA A 106 11.472 20.358 131.091 1.00 29.39 C
ATOM 742 C ALA A 106 10.897 19.925 129.750 1.00 31.25 C
ATOM 743 O ALA A 106 11.101 20.535 128.705 1.00 30.83 O
ATOM 744 CB ALA A 106 12.717 19.618 131.393 1.00 27.54 C
ATOM 745 N VAL A 107 10.178 18.831 129.775 1.00 33.05 N
ATOM 746 CA VAL A 107 9.622 18.326 128.567 1.00 31.54 C
ATOM 747 C VAL A 107 8.403 19.169 128.194 1.00 30.95 C
ATOM 748 O VAL A 107 8.213 19.474 127.018 1.00 32.50 O
ATOM 749 CB VAL A 107 9.211 16.831 128.739 1.00 30.93 C
ATOM 750 CG1 VAL A 107 8.233 16.464 127.643 1.00 30.86 C
ATOM 751 CG2 VAL A 107 10.470 15.937 128.600 1.00 27.09 C
ATOM 752 N ILE A 108 7.552 19.499 129.156 1.00 32.21 N
ATOM 753 CA ILE A 108 6.387 20.302 128.844 1.00 34.20 C
ATOM 754 C ILE A 108 6.916 21.588 128.208 1.00 34.94 C
ATOM 755 O ILE A 108 6.320 22.082 127.234 1.00 35.10 O
ATOM 756 CB ILE A 108 5.552 20.619 130.102 1.00 37.38 C
ATOM 757 CG1 ILE A 108 4.711 19.394 130.417 1.00 38.51 C
ATOM 758 CG2 ILE A 108 4.594 21.812 129.862 1.00 35.23 C
ATOM 759 CD1 ILE A 108 4.193 19.348 131.881 1.00 36.27 C
ATOM 760 N GLU A 109 8.059 22.069 128.695 1.00 32.89 N
ATOM 761 CA GLU A 109 8.674 23.275 128.133 1.00 33.19 C
ATOM 762 C GLU A 109 8.977 23.091 126.646 1.00 35.24 C
ATOM 763 O GLU A 109 8.700 23.995 125.781 1.00 34.46 O
ATOM 764 CB GLU A 109 10.043 23.588 128.826 1.00 34.81 C
ATOM 765 CG GLU A 109 10.577 24.937 128.452 1.00 35.08 C
ATOM 766 CD GLU A 109 11.929 25.280 129.107 1.00 42.02 C
ATOM 767 OE1 GLU A 109 12.950 24.627 128.742 1.00 41.94 O
ATOM 768 OE2 GLU A 109 11.947 26.224 129.944 1.00 39.34 O
ATOM 769 N LEU A 110 9.555 21.929 126.307 1.00 32.38 N
ATOM 770 CA LEU A 110 9.894 21.753 124.929 1.00 32.32 C
ATOM 771 C LEU A 110 8.594 21.714 124.130 1.00 31.34 C
ATOM 772 O LEU A 110 8.496 22.419 123.094 1.00 34.12 O
ATOM 773 CB LEU A 110 10.737 20.487 124.722 1.00 29.78 C
ATOM 774 CG LEU A 110 12.184 20.533 125.287 1.00 32.70 C
ATOM 775 CD1 LEU A 110 12.846 19.156 125.511 1.00 27.59 C
ATOM 776 CD2 LEU A 110 13.035 21.331 124.372 1.00 23.88 C
ATOM 777 N GLU A 111 7.589 20.954 124.596 1.00 31.13 N
ATOM 778 CA GLU A 111 6.335 20.848 123.810 1.00 30.16 C
ATOM 779 C GLU A 111 5.751 22.215 123.559 1.00 29.35 C
ATOM 780 O GLU A 111 5.433 22.526 122.406 1.00 32.91 O
ATOM 781 CB GLU A 111 5.350 19.907 124.433 1.00 31.71 C
ATOM 782 CG GLU A 111 4.191 19.534 123.536 1.00 29.23 C
ATOM 783 CD GLU A 111 3.176 20.679 123.577 1.00 30.84 C
ATOM 784 OE1 GLU A 111 3.026 21.290 124.634 1.00 34.51 O
ATOM 785 OE2 GLU A 111 2.553 21.017 122.574 1.00 35.93 O
ATOM 786 N ASN A 112 5.800 23.089 124.567 1.00 30.87 N
ATOM 787 CA ASN A 112 5.275 24.486 124.451 1.00 34.39 C
ATOM 788 C ASN A 112 6.088 25.374 123.522 1.00 33.89 C
ATOM 789 O ASN A 112 5.597 26.376 123.039 1.00 38.40 O
ATOM 790 CB ASN A 112 5.151 25.146 125.880 1.00 34.08 C
ATOM 791 CG ASN A 112 3.954 24.596 126.701 1.00 36.83 C
ATOM 792 OD1 ASN A 112 3.253 23.581 126.343 1.00 36.94 O
ATOM 793 ND2 ASN A 112 3.702 25.249 127.775 1.00 34.72 N
ATOM 794 N TYR A 113 7.356 25.044 123.326 1.00 32.99 N
ATOM 795 CA TYR A 113 8.188 25.739 122.425 1.00 29.52 C
ATOM 796 C TYR A 113 7.760 25.350 121.023 1.00 32.29 C
ATOM 797 O TYR A 113 8.112 26.034 120.033 1.00 34.81 O
ATOM 798 CB TYR A 113 9.643 25.336 122.581 1.00 28.26 C
ATOM 799 CG TYR A 113 10.268 25.915 123.761 1.00 34.31 C
ATOM 800 CD1 TYR A 113 11.491 25.417 124.218 1.00 33.98 C
ATOM 801 CD2 TYR A 113 9.692 26.987 124.445 1.00 35.92 C
ATOM 802 CE1 TYR A 113 12.112 25.959 125.287 1.00 34.24 C
ATOM 803 CE2 TYR A 113 10.321 27.548 125.556 1.00 31.92 C
ATOM 804 CZ TYR A 113 11.551 27.023 125.945 1.00 36.70 C
ATOM 805 OH TYR A 113 12.394 27.586 126.878 1.00 40.98 O
ATOM 806 N GLY A 114 7.036 24.231 120.891 1.00 35.06 N
ATOM 807 CA GLY A 114 6.559 23.796 119.572 1.00 29.34 C
ATOM 808 C GLY A 114 7.120 22.440 119.123 1.00 30.58 C
ATOM 809 O GLY A 114 6.861 21.988 118.031 1.00 30.81 O
ATOM 810 N MET A 115 7.895 21.776 119.969 1.00 30.85 N
ATOM 811 CA MET A 115 8.497 20.489 119.619 1.00 28.72 C
ATOM 812 C MET A 115 7.401 19.549 119.198 1.00 27.39 C
ATOM 813 O MET A 115 6.535 19.227 119.934 1.00 27.09 O
ATOM 814 CB MET A 115 9.300 19.911 120.784 1.00 26.48 C
ATOM 815 CG MET A 115 10.012 18.565 120.459 1.00 27.07 C
ATOM 816 SD MET A 115 11.322 18.384 121.697 1.00 33.30 S
ATOM 817 CE MET A 115 11.584 16.515 121.479 1.00 27.95 C
ATOM 818 N PRO A 116 7.481 19.048 117.994 1.00 27.12 N
ATOM 819 CA PRO A 116 6.423 18.170 117.562 1.00 27.40 C
ATOM 820 C PRO A 116 6.374 16.701 118.035 1.00 30.53 C
ATOM 821 O PRO A 116 6.468 15.802 117.186 1.00 28.20 O
ATOM 822 CB PRO A 116 6.525 18.272 116.016 1.00 26.62 C
ATOM 823 CG PRO A 116 8.094 18.255 115.867 1.00 22.64 C
ATOM 824 CD PRO A 116 8.518 19.220 116.953 1.00 25.42 C
ATOM 825 N PHE A 117 6.112 16.500 119.321 1.00 28.67 N
ATOM 826 CA PHE A 117 5.996 15.165 119.874 1.00 32.66 C
ATOM 827 C PHE A 117 4.866 14.416 119.236 1.00 35.93 C
ATOM 828 O PHE A 117 3.849 15.043 118.821 1.00 34.99 O
ATOM 829 CB PHE A 117 5.679 15.221 121.357 1.00 27.68 C
ATOM 830 CG PHE A 117 6.865 15.533 122.242 1.00 31.00 C
ATOM 831 CD1 PHE A 117 7.787 14.531 122.516 1.00 25.25 C
ATOM 832 CD2 PHE A 117 7.075 16.849 122.733 1.00 24.40 C
ATOM 833 CE1 PHE A 117 8.929 14.819 123.258 1.00 31.86 C
ATOM 834 CE2 PHE A 117 8.183 17.186 123.456 1.00 29.27 C
ATOM 835 CZ PHE A 117 9.166 16.136 123.735 1.00 28.70 C
ATOM 836 N SER A 118 5.062 13.091 119.141 1.00 34.29 N
ATOM 837 CA SER A 118 4.067 12.164 118.626 1.00 31.94 C
ATOM 838 C SER A 118 2.941 12.226 119.615 1.00 33.33 C
ATOM 839 O SER A 118 3.151 12.603 120.737 1.00 32.09 O
ATOM 840 CB SER A 118 4.648 10.706 118.566 1.00 35.41 C
ATOM 841 OG SER A 118 5.528 10.545 117.395 1.00 32.54 O
ATOM 842 N ARG A 119 1.738 11.816 119.247 1.00 34.92 N
ATOM 843 CA ARG A 119 0.615 11.978 120.165 1.00 34.47 C
ATOM 844 C ARG A 119 -0.201 10.714 120.523 1.00 37.13 C
ATOM 845 O ARG A 119 -0.215 9.711 119.787 1.00 37.64 O
ATOM 846 CB ARG A 119 -0.309 13.024 119.537 1.00 32.58 C
ATOM 847 CG ARG A 119 0.413 14.387 119.341 1.00 32.67 C
ATOM 848 CD ARG A 119 0.547 15.158 120.669 1.00 33.54 C
ATOM 849 NE ARG A 119 1.401 16.313 120.468 1.00 36.65 N
ATOM 850 CZ ARG A 119 1.435 17.298 121.322 1.00 36.44 C
ATOM 851 NH1 ARG A 119 0.667 17.162 122.362 1.00 37.57 N
ATOM 852 NH2 ARG A 119 2.147 18.438 121.111 1.00 36.36 N
ATOM 853 N THR A 120 -0.827 10.734 121.684 1.00 36.28 N
ATOM 854 CA THR A 120 -1.706 9.630 122.093 1.00 39.54 C
ATOM 855 C THR A 120 -3.160 9.946 121.697 1.00 41.94 C
ATOM 856 O THR A 120 -3.491 11.014 121.179 1.00 38.92 O
ATOM 857 CB THR A 120 -1.725 9.426 123.632 1.00 39.11 C
ATOM 858 OG1 THR A 120 -2.321 10.588 124.238 1.00 35.38 O
ATOM 859 CG2 THR A 120 -0.270 9.228 124.149 1.00 37.51 C
ATOM 860 N GLU A 121 -4.051 9.013 121.970 1.00 46.75 N
ATOM 861 CA GLU A 121 -5.457 9.264 121.597 1.00 49.36 C
ATOM 862 C GLU A 121 -6.038 10.414 122.373 1.00 48.73 C
ATOM 863 O GLU A 121 -7.106 10.866 122.000 1.00 50.24 O
ATOM 864 CB GLU A 121 -6.345 8.044 121.807 1.00 54.13 C
ATOM 865 CG GLU A 121 -6.366 7.063 120.617 1.00 63.54 C
ATOM 866 CD GLU A 121 -6.884 7.688 119.290 1.00 69.32 C
ATOM 867 OE1 GLU A 121 -7.451 8.830 119.327 1.00 72.78 O