HEADER TRANSPORT PROTEIN 02-MAY-19 6OT5
TITLE STRUCTURE OF THE TRPV3 K169A SENSITIZED MUTANT IN THE PRESENCE OF 2-
TITLE 2 APB AT 3.6 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V
COMPND 3 MEMBER 3,TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V
COMPND 4 MEMBER 3;
COMPND 5 CHAIN: A, B, C, D;
COMPND 6 SYNONYM: TRPV3,VANILLOID RECEPTOR-LIKE 3,VRL-3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TRPV3;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS ION CHANNEL, TRP CHANNEL, TRPV CHANNEL, METAL TRANSPORT, MEMBRANE
KEYWDS 2 TRANSPORT, MEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR L.ZUBCEVIC,W.F.BORSCHEL,A.L.HSU,M.J.BORGNIA,S.-Y.LEE
REVDAT 2 18-DEC-19 6OT5 1 CRYST1 SCALE
REVDAT 1 22-MAY-19 6OT5 0
JRNL AUTH L.ZUBCEVIC,W.F.BORSCHEL,A.L.HSU,M.J.BORGNIA,S.Y.LEE
JRNL TITL REGULATORY SWITCH AT THE CYTOPLASMIC INTERFACE CONTROLS TRPV
JRNL TITL 2 CHANNEL GATING.
JRNL REF ELIFE V. 8 2019
JRNL REFN ESSN 2050-084X
JRNL PMID 31070581
JRNL DOI 10.7554/ELIFE.47746
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.600
REMARK 3 NUMBER OF PARTICLES : 79006
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6OT5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1000241303.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HUMAN TRPV3 ION CHANNEL
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.50
REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : OTHER
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 42.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : OTHER
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 150
REMARK 465 ASP A 151
REMARK 465 GLU A 152
REMARK 465 ASP A 153
REMARK 465 PRO A 463
REMARK 465 ARG A 464
REMARK 465 GLU A 465
REMARK 465 GLU A 466
REMARK 465 GLU A 467
REMARK 465 ALA A 468
REMARK 465 ILE A 469
REMARK 465 PRO A 470
REMARK 465 HIS A 471
REMARK 465 PRO A 472
REMARK 465 LEU A 473
REMARK 465 ALA A 474
REMARK 465 LEU A 475
REMARK 465 THR A 476
REMARK 465 HIS A 477
REMARK 465 LYS A 478
REMARK 465 MET A 479
REMARK 465 ARG A 509
REMARK 465 PRO A 510
REMARK 465 SER A 511
REMARK 465 ASP A 512
REMARK 465 LEU A 513
REMARK 465 GLN A 514
REMARK 465 SER A 515
REMARK 465 ILE A 516
REMARK 465 LEU A 517
REMARK 465 GLU A 751
REMARK 465 ASP A 752
REMARK 465 PRO A 753
REMARK 465 GLY A 754
REMARK 465 PRO A 755
REMARK 465 VAL A 756
REMARK 465 ARG A 757
REMARK 465 ARG A 758
REMARK 465 THR A 759
REMARK 465 ASP A 760
REMARK 465 PHE A 761
REMARK 465 ASN A 762
REMARK 465 LYS A 763
REMARK 465 ILE A 764
REMARK 465 GLN A 765
REMARK 465 ASP A 766
REMARK 465 SER A 767
REMARK 465 SER A 768
REMARK 465 ARG A 769
REMARK 465 ASN A 770
REMARK 465 ASN A 771
REMARK 465 SER A 772
REMARK 465 LYS A 773
REMARK 465 THR A 774
REMARK 465 THR A 775
REMARK 465 LEU A 776
REMARK 465 ASN A 777
REMARK 465 ALA A 778
REMARK 465 PHE A 779
REMARK 465 GLU A 780
REMARK 465 GLU A 781
REMARK 465 VAL A 782
REMARK 465 GLU A 783
REMARK 465 GLU A 784
REMARK 465 PHE A 785
REMARK 465 PRO A 786
REMARK 465 GLU A 787
REMARK 465 THR A 788
REMARK 465 SER A 789
REMARK 465 VAL A 790
REMARK 465 VAL A 791
REMARK 465 ASP A 792
REMARK 465 ALA A 793
REMARK 465 GLY A 794
REMARK 465 LEU A 795
REMARK 465 GLU A 796
REMARK 465 VAL A 797
REMARK 465 LEU A 798
REMARK 465 PHE A 799
REMARK 465 GLN A 800
REMARK 465 GLY A 801
REMARK 465 ASP A 802
REMARK 465 TYR A 803
REMARK 465 LYS A 804
REMARK 465 ASP A 805
REMARK 465 ASP A 806
REMARK 465 ASP A 807
REMARK 465 ASP A 808
REMARK 465 LYS A 809
REMARK 465 ALA A 810
REMARK 465 HIS A 811
REMARK 465 HIS A 812
REMARK 465 HIS A 813
REMARK 465 HIS A 814
REMARK 465 HIS A 815
REMARK 465 HIS A 816
REMARK 465 HIS B 150
REMARK 465 ASP B 151
REMARK 465 GLU B 152
REMARK 465 ASP B 153
REMARK 465 PRO B 463
REMARK 465 ARG B 464
REMARK 465 GLU B 465
REMARK 465 GLU B 466
REMARK 465 GLU B 467
REMARK 465 ALA B 468
REMARK 465 ILE B 469
REMARK 465 PRO B 470
REMARK 465 HIS B 471
REMARK 465 PRO B 472
REMARK 465 LEU B 473
REMARK 465 ALA B 474
REMARK 465 LEU B 475
REMARK 465 THR B 476
REMARK 465 HIS B 477
REMARK 465 LYS B 478
REMARK 465 MET B 479
REMARK 465 ARG B 509
REMARK 465 PRO B 510
REMARK 465 SER B 511
REMARK 465 ASP B 512
REMARK 465 LEU B 513
REMARK 465 GLN B 514
REMARK 465 SER B 515
REMARK 465 ILE B 516
REMARK 465 LEU B 517
REMARK 465 GLU B 751
REMARK 465 ASP B 752
REMARK 465 PRO B 753
REMARK 465 GLY B 754
REMARK 465 PRO B 755
REMARK 465 VAL B 756
REMARK 465 ARG B 757
REMARK 465 ARG B 758
REMARK 465 THR B 759
REMARK 465 ASP B 760
REMARK 465 PHE B 761
REMARK 465 ASN B 762
REMARK 465 LYS B 763
REMARK 465 ILE B 764
REMARK 465 GLN B 765
REMARK 465 ASP B 766
REMARK 465 SER B 767
REMARK 465 SER B 768
REMARK 465 ARG B 769
REMARK 465 ASN B 770
REMARK 465 ASN B 771
REMARK 465 SER B 772
REMARK 465 LYS B 773
REMARK 465 THR B 774
REMARK 465 THR B 775
REMARK 465 LEU B 776
REMARK 465 ASN B 777
REMARK 465 ALA B 778
REMARK 465 PHE B 779
REMARK 465 GLU B 780
REMARK 465 GLU B 781
REMARK 465 VAL B 782
REMARK 465 GLU B 783
REMARK 465 GLU B 784
REMARK 465 PHE B 785
REMARK 465 PRO B 786
REMARK 465 GLU B 787
REMARK 465 THR B 788
REMARK 465 SER B 789
REMARK 465 VAL B 790
REMARK 465 VAL B 791
REMARK 465 ASP B 792
REMARK 465 ALA B 793
REMARK 465 GLY B 794
REMARK 465 LEU B 795
REMARK 465 GLU B 796
REMARK 465 VAL B 797
REMARK 465 LEU B 798
REMARK 465 PHE B 799
REMARK 465 GLN B 800
REMARK 465 GLY B 801
REMARK 465 ASP B 802
REMARK 465 TYR B 803
REMARK 465 LYS B 804
REMARK 465 ASP B 805
REMARK 465 ASP B 806
REMARK 465 ASP B 807
REMARK 465 ASP B 808
REMARK 465 LYS B 809
REMARK 465 ALA B 810
REMARK 465 HIS B 811
REMARK 465 HIS B 812
REMARK 465 HIS B 813
REMARK 465 HIS B 814
REMARK 465 HIS B 815
REMARK 465 HIS B 816
REMARK 465 HIS C 150
REMARK 465 ASP C 151
REMARK 465 GLU C 152
REMARK 465 ASP C 153
REMARK 465 PRO C 463
REMARK 465 ARG C 464
REMARK 465 GLU C 465
REMARK 465 GLU C 466
REMARK 465 GLU C 467
REMARK 465 ALA C 468
REMARK 465 ILE C 469
REMARK 465 PRO C 470
REMARK 465 HIS C 471
REMARK 465 PRO C 472
REMARK 465 LEU C 473
REMARK 465 ALA C 474
REMARK 465 LEU C 475
REMARK 465 THR C 476
REMARK 465 HIS C 477
REMARK 465 LYS C 478
REMARK 465 MET C 479
REMARK 465 ARG C 509
REMARK 465 PRO C 510
REMARK 465 SER C 511
REMARK 465 ASP C 512
REMARK 465 LEU C 513
REMARK 465 GLN C 514
REMARK 465 SER C 515
REMARK 465 ILE C 516
REMARK 465 LEU C 517
REMARK 465 GLU C 751
REMARK 465 ASP C 752
REMARK 465 PRO C 753
REMARK 465 GLY C 754
REMARK 465 PRO C 755
REMARK 465 VAL C 756
REMARK 465 ARG C 757
REMARK 465 ARG C 758
REMARK 465 THR C 759
REMARK 465 ASP C 760
REMARK 465 PHE C 761
REMARK 465 ASN C 762
REMARK 465 LYS C 763
REMARK 465 ILE C 764
REMARK 465 GLN C 765
REMARK 465 ASP C 766
REMARK 465 SER C 767
REMARK 465 SER C 768
REMARK 465 ARG C 769
REMARK 465 ASN C 770
REMARK 465 ASN C 771
REMARK 465 SER C 772
REMARK 465 LYS C 773
REMARK 465 THR C 774
REMARK 465 THR C 775
REMARK 465 LEU C 776
REMARK 465 ASN C 777
REMARK 465 ALA C 778
REMARK 465 PHE C 779
REMARK 465 GLU C 780
REMARK 465 GLU C 781
REMARK 465 VAL C 782
REMARK 465 GLU C 783
REMARK 465 GLU C 784
REMARK 465 PHE C 785
REMARK 465 PRO C 786
REMARK 465 GLU C 787
REMARK 465 THR C 788
REMARK 465 SER C 789
REMARK 465 VAL C 790
REMARK 465 VAL C 791
REMARK 465 ASP C 792
REMARK 465 ALA C 793
REMARK 465 GLY C 794
REMARK 465 LEU C 795
REMARK 465 GLU C 796
REMARK 465 VAL C 797
REMARK 465 LEU C 798
REMARK 465 PHE C 799
REMARK 465 GLN C 800
REMARK 465 GLY C 801
REMARK 465 ASP C 802
REMARK 465 TYR C 803
REMARK 465 LYS C 804
REMARK 465 ASP C 805
REMARK 465 ASP C 806
REMARK 465 ASP C 807
REMARK 465 ASP C 808
REMARK 465 LYS C 809
REMARK 465 ALA C 810
REMARK 465 HIS C 811
REMARK 465 HIS C 812
REMARK 465 HIS C 813
REMARK 465 HIS C 814
REMARK 465 HIS C 815
REMARK 465 HIS C 816
REMARK 465 HIS D 150
REMARK 465 ASP D 151
REMARK 465 GLU D 152
REMARK 465 ASP D 153
REMARK 465 PRO D 463
REMARK 465 ARG D 464
REMARK 465 GLU D 465
REMARK 465 GLU D 466
REMARK 465 GLU D 467
REMARK 465 ALA D 468
REMARK 465 ILE D 469
REMARK 465 PRO D 470
REMARK 465 HIS D 471
REMARK 465 PRO D 472
REMARK 465 LEU D 473
REMARK 465 ALA D 474
REMARK 465 LEU D 475
REMARK 465 THR D 476
REMARK 465 HIS D 477
REMARK 465 LYS D 478
REMARK 465 MET D 479
REMARK 465 ARG D 509
REMARK 465 PRO D 510
REMARK 465 SER D 511
REMARK 465 ASP D 512
REMARK 465 LEU D 513
REMARK 465 GLN D 514
REMARK 465 SER D 515
REMARK 465 ILE D 516
REMARK 465 LEU D 517
REMARK 465 GLU D 751
REMARK 465 ASP D 752
REMARK 465 PRO D 753
REMARK 465 GLY D 754
REMARK 465 PRO D 755
REMARK 465 VAL D 756
REMARK 465 ARG D 757
REMARK 465 ARG D 758
REMARK 465 THR D 759
REMARK 465 ASP D 760
REMARK 465 PHE D 761
REMARK 465 ASN D 762
REMARK 465 LYS D 763
REMARK 465 ILE D 764
REMARK 465 GLN D 765
REMARK 465 ASP D 766
REMARK 465 SER D 767
REMARK 465 SER D 768
REMARK 465 ARG D 769
REMARK 465 ASN D 770
REMARK 465 ASN D 771
REMARK 465 SER D 772
REMARK 465 LYS D 773
REMARK 465 THR D 774
REMARK 465 THR D 775
REMARK 465 LEU D 776
REMARK 465 ASN D 777
REMARK 465 ALA D 778
REMARK 465 PHE D 779
REMARK 465 GLU D 780
REMARK 465 GLU D 781
REMARK 465 VAL D 782
REMARK 465 GLU D 783
REMARK 465 GLU D 784
REMARK 465 PHE D 785
REMARK 465 PRO D 786
REMARK 465 GLU D 787
REMARK 465 THR D 788
REMARK 465 SER D 789
REMARK 465 VAL D 790
REMARK 465 VAL D 791
REMARK 465 ASP D 792
REMARK 465 ALA D 793
REMARK 465 GLY D 794
REMARK 465 LEU D 795
REMARK 465 GLU D 796
REMARK 465 VAL D 797
REMARK 465 LEU D 798
REMARK 465 PHE D 799
REMARK 465 GLN D 800
REMARK 465 GLY D 801
REMARK 465 ASP D 802
REMARK 465 TYR D 803
REMARK 465 LYS D 804
REMARK 465 ASP D 805
REMARK 465 ASP D 806
REMARK 465 ASP D 807
REMARK 465 ASP D 808
REMARK 465 LYS D 809
REMARK 465 ALA D 810
REMARK 465 HIS D 811
REMARK 465 HIS D 812
REMARK 465 HIS D 813
REMARK 465 HIS D 814
REMARK 465 HIS D 815
REMARK 465 HIS D 816
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 GLN A 112 CG CD OE1 NE2
REMARK 470 ARG A 113 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ARG A 117 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 118 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 119 CG CD1 CD2
REMARK 470 LYS A 120 CG CD CE NZ
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 123 CG1 CG2 CD1
REMARK 470 VAL A 127 CG1 CG2
REMARK 470 SER A 128 OG
REMARK 470 GLU A 129 CG CD OE1 OE2
REMARK 470 CYS A 131 SG
REMARK 470 VAL A 132 CG1 CG2
REMARK 470 GLU A 133 CG CD OE1 OE2
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 LEU A 135 CG CD1 CD2
REMARK 470 VAL A 136 CG1 CG2
REMARK 470 GLU A 137 CG CD OE1 OE2
REMARK 470 LEU A 138 CG CD1 CD2
REMARK 470 LEU A 139 CG CD1 CD2
REMARK 470 VAL A 140 CG1 CG2
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 GLU A 144 CG CD OE1 OE2
REMARK 470 LEU A 145 CG CD1 CD2
REMARK 470 CYS A 146 SG
REMARK 470 ARG A 147 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 149 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 156 CG OD1 OD2
REMARK 470 PHE A 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 159 CG SD CE
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 THR A 163 OG1 CG2
REMARK 470 SER A 165 OG
REMARK 470 ASP A 166 CG OD1 OD2
REMARK 470 THR A 167 OG1 CG2
REMARK 470 CYS A 171 SG
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 ASN A 178 CG OD1 ND2
REMARK 470 ILE A 179 CG1 CG2 CD1
REMARK 470 ASN A 182 CG OD1 ND2
REMARK 470 THR A 183 OG1 CG2
REMARK 470 LYS A 184 CG CD CE NZ
REMARK 470 GLU A 185 CG CD OE1 OE2
REMARK 470 VAL A 187 CG1 CG2
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 195 CG CD OE1 OE2
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 ASN A 197 CG OD1 ND2
REMARK 470 ASP A 198 CG OD1 OD2
REMARK 470 ILE A 199 CG1 CG2 CD1
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 205 CG OD1 ND2
REMARK 470 GLU A 207 CG CD OE1 OE2
REMARK 470 THR A 209 OG1 CG2
REMARK 470 GLU A 210 CG CD OE1 OE2
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 GLU A 214 CG CD OE1 OE2
REMARK 470 THR A 217 OG1 CG2
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 ASP A 229 CG OD1 OD2
REMARK 470 LEU A 234 CG CD1 CD2
REMARK 470 ILE A 235 CG1 CG2 CD1
REMARK 470 ASP A 240 CG OD1 OD2
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 TYR A 254 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS A 256 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 257 CG CD OE1 OE2
REMARK 470 CYS A 271 SG
REMARK 470 GLU A 276 CG CD OE1 OE2
REMARK 470 GLU A 283 CG CD OE1 OE2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 GLN A 286 CG CD OE1 NE2
REMARK 470 ASN A 297 CG OD1 ND2
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 PHE A 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 GLN A 313 CG CD OE1 NE2
REMARK 470 LYS A 318 CE NZ
REMARK 470 MET A 320 CE
REMARK 470 MET A 323 CE
REMARK 470 ARG A 327 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 330 CG OD1 ND2
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 THR A 335 OG1 CG2
REMARK 470 GLN A 346 CG CD OE1 NE2
REMARK 470 GLU A 355 CG CD OE1 OE2
REMARK 470 GLU A 364 CG CD OE1 OE2
REMARK 470 LYS A 366 CG CD CE NZ
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 SER A 374 OG
REMARK 470 THR A 399 OG1 CG2
REMARK 470 GLU A 405 CG CD OE1 OE2
REMARK 470 THR A 411 OG1 CG2
REMARK 470 ASN A 412 CG OD1 ND2
REMARK 470 ASP A 414 CG OD1 OD2
REMARK 470 GLU A 418 CG CD OE1 OE2
REMARK 470 GLU A 423 CG CD OE1 OE2
REMARK 470 PHE A 442 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 462 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 481 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 481 CZ3 CH2
REMARK 470 LEU A 482 CG CD1 CD2
REMARK 470 GLN A 483 CG CD OE1 NE2
REMARK 470 LEU A 484 CG CD1 CD2
REMARK 470 LEU A 485 CG CD1 CD2
REMARK 470 ARG A 487 CG CD NE CZ NH1 NH2
REMARK 470 MET A 488 CG SD CE
REMARK 470 LEU A 491 CG CD1 CD2
REMARK 470 ILE A 492 CG1 CG2 CD1
REMARK 470 MET A 495 CG SD CE
REMARK 470 SER A 498 OG
REMARK 470 VAL A 499 CG1 CG2
REMARK 470 GLU A 501 CG CD OE1 OE2
REMARK 470 ILE A 503 CG1 CG2 CD1
REMARK 470 ILE A 505 CG1 CG2 CD1
REMARK 470 PHE A 506 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 507 CG CD1 CD2
REMARK 470 LEU A 508 CG CD1 CD2
REMARK 470 SER A 518 OG
REMARK 470 ASP A 519 CG OD1 OD2
REMARK 470 PHE A 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 528 CG1 CG2 CD1
REMARK 470 ILE A 534 CD1
REMARK 470 SER A 536 OG
REMARK 470 VAL A 537 CG1 CG2
REMARK 470 PHE A 538 CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 541 CG CD1 CD2
REMARK 470 TYR A 544 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 MET A 574 CG SD CE
REMARK 470 MET A 578 CG SD CE
REMARK 470 ASP A 586 CG OD1 OD2
REMARK 470 ILE A 609 CG1 CG2 CD1
REMARK 470 GLU A 610 CG CD OE1 OE2
REMARK 470 LYS A 611 CG CD CE NZ
REMARK 470 CYS A 612 SG
REMARK 470 LYS A 614 CG CD CE NZ
REMARK 470 ASP A 615 CG OD1 OD2
REMARK 470 ASN A 616 CG OD1 ND2
REMARK 470 LYS A 617 CG CD CE NZ
REMARK 470 ASP A 618 CG OD1 OD2
REMARK 470 CYS A 619 SG
REMARK 470 SER A 624 OG
REMARK 470 ASP A 627 OD1 OD2
REMARK 470 ASP A 641 CG OD1 OD2
REMARK 470 GLN A 645 CG CD OE1 NE2
REMARK 470 ASN A 647 CG OD1 ND2
REMARK 470 SER A 648 OG
REMARK 470 LYS A 649 CG CD CE NZ
REMARK 470 GLU A 682 CG CD OE1 OE2
REMARK 470 ASN A 683 CG OD1 ND2
REMARK 470 LYS A 686 CG CD CE NZ
REMARK 470 GLU A 687 CG CD OE1 OE2
REMARK 470 GLU A 689 CG CD OE1 OE2
REMARK 470 ILE A 700 CD1
REMARK 470 GLU A 702 CG CD OE1 OE2
REMARK 470 GLU A 704 CG CD OE1 OE2
REMARK 470 LYS A 705 CD CE NZ
REMARK 470 GLU A 709 CG CD OE1 OE2
REMARK 470 LEU A 711 CG CD1 CD2
REMARK 470 ARG A 714 CG CD NE CZ NH1 NH2
REMARK 470 MET A 717 CE
REMARK 470 GLU A 725 CG CD OE1 OE2
REMARK 470 ASP A 726 CG OD1 OD2
REMARK 470 ASP A 727 CG OD1 OD2
REMARK 470 GLU A 741 CG CD OE1 OE2
REMARK 470 ASN A 750 CG OD1 ND2
REMARK 470 GLU B 110 CG CD OE1 OE2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 GLN B 112 CG CD OE1 NE2
REMARK 470 ARG B 113 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 ARG B 117 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 118 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 119 CG CD1 CD2
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 123 CG1 CG2 CD1
REMARK 470 VAL B 127 CG1 CG2
REMARK 470 SER B 128 OG
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 CYS B 131 SG
REMARK 470 VAL B 132 CG1 CG2
REMARK 470 GLU B 133 CG CD OE1 OE2
REMARK 470 GLU B 134 CG CD OE1 OE2
REMARK 470 LEU B 135 CG CD1 CD2
REMARK 470 VAL B 136 CG1 CG2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 LEU B 138 CG CD1 CD2
REMARK 470 LEU B 139 CG CD1 CD2
REMARK 470 VAL B 140 CG1 CG2
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 LEU B 142 CG CD1 CD2
REMARK 470 GLN B 143 CG CD OE1 NE2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LEU B 145 CG CD1 CD2
REMARK 470 CYS B 146 SG
REMARK 470 ARG B 147 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 149 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 156 CG OD1 OD2
REMARK 470 PHE B 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 159 CG SD CE
REMARK 470 LYS B 161 CG CD CE NZ
REMARK 470 THR B 163 OG1 CG2
REMARK 470 SER B 165 OG
REMARK 470 ASP B 166 CG OD1 OD2
REMARK 470 THR B 167 OG1 CG2
REMARK 470 CYS B 171 SG
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 ASN B 178 CG OD1 ND2
REMARK 470 ILE B 179 CG1 CG2 CD1
REMARK 470 ASN B 182 CG OD1 ND2
REMARK 470 THR B 183 OG1 CG2
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 GLU B 185 CG CD OE1 OE2
REMARK 470 VAL B 187 CG1 CG2
REMARK 470 ARG B 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 195 CG CD OE1 OE2
REMARK 470 GLU B 196 CG CD OE1 OE2
REMARK 470 ASN B 197 CG OD1 ND2
REMARK 470 ASP B 198 CG OD1 OD2
REMARK 470 ILE B 199 CG1 CG2 CD1
REMARK 470 ARG B 202 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 205 CG OD1 ND2
REMARK 470 GLU B 207 CG CD OE1 OE2
REMARK 470 THR B 209 OG1 CG2
REMARK 470 GLU B 210 CG CD OE1 OE2
REMARK 470 GLU B 211 CG CD OE1 OE2
REMARK 470 GLU B 214 CG CD OE1 OE2
REMARK 470 THR B 217 OG1 CG2
REMARK 470 GLU B 224 CG CD OE1 OE2
REMARK 470 ASP B 229 CG OD1 OD2
REMARK 470 LEU B 234 CG CD1 CD2
REMARK 470 ILE B 235 CG1 CG2 CD1
REMARK 470 ASP B 240 CG OD1 OD2
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 470 TYR B 254 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS B 256 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 257 CG CD OE1 OE2
REMARK 470 CYS B 271 SG
REMARK 470 GLU B 276 CG CD OE1 OE2
REMARK 470 GLU B 283 CG CD OE1 OE2
REMARK 470 GLU B 285 CG CD OE1 OE2
REMARK 470 GLN B 286 CG CD OE1 NE2
REMARK 470 ASN B 297 CG OD1 ND2
REMARK 470 GLU B 308 CG CD OE1 OE2
REMARK 470 PHE B 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 311 CG CD CE NZ
REMARK 470 GLN B 313 CG CD OE1 NE2
REMARK 470 LYS B 318 CE NZ
REMARK 470 MET B 320 CE
REMARK 470 MET B 323 CE
REMARK 470 ARG B 327 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 330 CG OD1 ND2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 THR B 335 OG1 CG2
REMARK 470 GLN B 346 CG CD OE1 NE2
REMARK 470 GLU B 355 CG CD OE1 OE2
REMARK 470 GLU B 364 CG CD OE1 OE2
REMARK 470 LYS B 366 CG CD CE NZ
REMARK 470 GLU B 367 CG CD OE1 OE2
REMARK 470 LYS B 368 CG CD CE NZ
REMARK 470 SER B 374 OG
REMARK 470 THR B 399 OG1 CG2
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 THR B 411 OG1 CG2
REMARK 470 ASN B 412 CG OD1 ND2
REMARK 470 ASP B 414 CG OD1 OD2
REMARK 470 GLU B 418 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 PHE B 442 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 462 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 481 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 481 CZ3 CH2
REMARK 470 LEU B 482 CG CD1 CD2
REMARK 470 GLN B 483 CG CD OE1 NE2
REMARK 470 LEU B 484 CG CD1 CD2
REMARK 470 LEU B 485 CG CD1 CD2
REMARK 470 ARG B 487 CG CD NE CZ NH1 NH2
REMARK 470 MET B 488 CG SD CE
REMARK 470 LEU B 491 CG CD1 CD2
REMARK 470 ILE B 492 CG1 CG2 CD1
REMARK 470 MET B 495 CG SD CE
REMARK 470 SER B 498 OG
REMARK 470 VAL B 499 CG1 CG2
REMARK 470 GLU B 501 CG CD OE1 OE2
REMARK 470 ILE B 503 CG1 CG2 CD1
REMARK 470 ILE B 505 CG1 CG2 CD1
REMARK 470 PHE B 506 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 507 CG CD1 CD2
REMARK 470 LEU B 508 CG CD1 CD2
REMARK 470 SER B 518 OG
REMARK 470 ASP B 519 CG OD1 OD2
REMARK 470 PHE B 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE B 528 CG1 CG2 CD1
REMARK 470 ILE B 534 CD1
REMARK 470 SER B 536 OG
REMARK 470 VAL B 537 CG1 CG2
REMARK 470 PHE B 538 CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 541 CG CD1 CD2
REMARK 470 TYR B 544 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 545 CG CD CE NZ
REMARK 470 MET B 574 CG SD CE
REMARK 470 MET B 578 CG SD CE
REMARK 470 ASP B 586 CG OD1 OD2
REMARK 470 ILE B 609 CG1 CG2 CD1
REMARK 470 GLU B 610 CG CD OE1 OE2
REMARK 470 LYS B 611 CG CD CE NZ
REMARK 470 CYS B 612 SG
REMARK 470 LYS B 614 CG CD CE NZ
REMARK 470 ASP B 615 CG OD1 OD2
REMARK 470 ASN B 616 CG OD1 ND2
REMARK 470 LYS B 617 CG CD CE NZ
REMARK 470 ASP B 618 CG OD1 OD2
REMARK 470 CYS B 619 SG
REMARK 470 SER B 624 OG
REMARK 470 ASP B 627 OD1 OD2
REMARK 470 ASP B 641 CG OD1 OD2
REMARK 470 GLN B 645 CG CD OE1 NE2
REMARK 470 ASN B 647 CG OD1 ND2
REMARK 470 SER B 648 OG
REMARK 470 LYS B 649 CG CD CE NZ
REMARK 470 GLU B 682 CG CD OE1 OE2
REMARK 470 ASN B 683 CG OD1 ND2
REMARK 470 LYS B 686 CG CD CE NZ
REMARK 470 GLU B 687 CG CD OE1 OE2
REMARK 470 GLU B 689 CG CD OE1 OE2
REMARK 470 ILE B 700 CD1
REMARK 470 GLU B 702 CG CD OE1 OE2
REMARK 470 GLU B 704 CG CD OE1 OE2
REMARK 470 LYS B 705 CD CE NZ
REMARK 470 GLU B 709 CG CD OE1 OE2
REMARK 470 LEU B 711 CG CD1 CD2
REMARK 470 ARG B 714 CG CD NE CZ NH1 NH2
REMARK 470 MET B 717 CE
REMARK 470 GLU B 725 CG CD OE1 OE2
REMARK 470 ASP B 726 CG OD1 OD2
REMARK 470 ASP B 727 CG OD1 OD2
REMARK 470 GLU B 741 CG CD OE1 OE2
REMARK 470 ASN B 750 CG OD1 ND2
REMARK 470 GLU C 110 CG CD OE1 OE2
REMARK 470 GLU C 111 CG CD OE1 OE2
REMARK 470 GLN C 112 CG CD OE1 NE2
REMARK 470 ARG C 113 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 115 CG CD CE NZ
REMARK 470 LYS C 116 CG CD CE NZ
REMARK 470 ARG C 117 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 118 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 119 CG CD1 CD2
REMARK 470 LYS C 120 CG CD CE NZ
REMARK 470 LYS C 121 CG CD CE NZ
REMARK 470 ARG C 122 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 123 CG1 CG2 CD1
REMARK 470 VAL C 127 CG1 CG2
REMARK 470 SER C 128 OG
REMARK 470 GLU C 129 CG CD OE1 OE2
REMARK 470 CYS C 131 SG
REMARK 470 VAL C 132 CG1 CG2
REMARK 470 GLU C 133 CG CD OE1 OE2
REMARK 470 GLU C 134 CG CD OE1 OE2
REMARK 470 LEU C 135 CG CD1 CD2
REMARK 470 VAL C 136 CG1 CG2
REMARK 470 GLU C 137 CG CD OE1 OE2
REMARK 470 LEU C 138 CG CD1 CD2
REMARK 470 LEU C 139 CG CD1 CD2
REMARK 470 VAL C 140 CG1 CG2
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 LEU C 142 CG CD1 CD2
REMARK 470 GLN C 143 CG CD OE1 NE2
REMARK 470 GLU C 144 CG CD OE1 OE2
REMARK 470 LEU C 145 CG CD1 CD2
REMARK 470 CYS C 146 SG
REMARK 470 ARG C 147 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 149 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 156 CG OD1 OD2
REMARK 470 PHE C 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET C 159 CG SD CE
REMARK 470 LYS C 161 CG CD CE NZ
REMARK 470 THR C 163 OG1 CG2
REMARK 470 SER C 165 OG
REMARK 470 ASP C 166 CG OD1 OD2
REMARK 470 THR C 167 OG1 CG2
REMARK 470 CYS C 171 SG
REMARK 470 LYS C 174 CG CD CE NZ
REMARK 470 ASN C 178 CG OD1 ND2
REMARK 470 ILE C 179 CG1 CG2 CD1
REMARK 470 ASN C 182 CG OD1 ND2
REMARK 470 THR C 183 OG1 CG2
REMARK 470 LYS C 184 CG CD CE NZ
REMARK 470 GLU C 185 CG CD OE1 OE2
REMARK 470 VAL C 187 CG1 CG2
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 GLU C 196 CG CD OE1 OE2
REMARK 470 ASN C 197 CG OD1 ND2
REMARK 470 ASP C 198 CG OD1 OD2
REMARK 470 ILE C 199 CG1 CG2 CD1
REMARK 470 ARG C 202 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 205 CG OD1 ND2
REMARK 470 GLU C 207 CG CD OE1 OE2
REMARK 470 THR C 209 OG1 CG2
REMARK 470 GLU C 210 CG CD OE1 OE2
REMARK 470 GLU C 211 CG CD OE1 OE2
REMARK 470 GLU C 214 CG CD OE1 OE2
REMARK 470 THR C 217 OG1 CG2
REMARK 470 GLU C 224 CG CD OE1 OE2
REMARK 470 ASP C 229 CG OD1 OD2
REMARK 470 LEU C 234 CG CD1 CD2
REMARK 470 ILE C 235 CG1 CG2 CD1
REMARK 470 ASP C 240 CG OD1 OD2
REMARK 470 LYS C 246 CG CD CE NZ
REMARK 470 LYS C 253 CG CD CE NZ
REMARK 470 TYR C 254 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS C 256 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 257 CG CD OE1 OE2
REMARK 470 CYS C 271 SG
REMARK 470 GLU C 276 CG CD OE1 OE2
REMARK 470 GLU C 283 CG CD OE1 OE2
REMARK 470 GLU C 285 CG CD OE1 OE2
REMARK 470 GLN C 286 CG CD OE1 NE2
REMARK 470 ASN C 297 CG OD1 ND2
REMARK 470 GLU C 308 CG CD OE1 OE2
REMARK 470 PHE C 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 311 CG CD CE NZ
REMARK 470 GLN C 313 CG CD OE1 NE2
REMARK 470 LYS C 318 CE NZ
REMARK 470 MET C 320 CE
REMARK 470 MET C 323 CE
REMARK 470 ARG C 327 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 330 CG OD1 ND2
REMARK 470 GLU C 332 CG CD OE1 OE2
REMARK 470 THR C 335 OG1 CG2
REMARK 470 GLN C 346 CG CD OE1 NE2
REMARK 470 GLU C 355 CG CD OE1 OE2
REMARK 470 GLU C 364 CG CD OE1 OE2
REMARK 470 LYS C 366 CG CD CE NZ
REMARK 470 GLU C 367 CG CD OE1 OE2
REMARK 470 LYS C 368 CG CD CE NZ
REMARK 470 SER C 374 OG
REMARK 470 THR C 399 OG1 CG2
REMARK 470 GLU C 405 CG CD OE1 OE2
REMARK 470 THR C 411 OG1 CG2
REMARK 470 ASN C 412 CG OD1 ND2
REMARK 470 ASP C 414 CG OD1 OD2
REMARK 470 GLU C 418 CG CD OE1 OE2
REMARK 470 GLU C 423 CG CD OE1 OE2
REMARK 470 PHE C 442 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 462 CG CD NE CZ NH1 NH2
REMARK 470 TRP C 481 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 481 CZ3 CH2
REMARK 470 LEU C 482 CG CD1 CD2
REMARK 470 GLN C 483 CG CD OE1 NE2
REMARK 470 LEU C 484 CG CD1 CD2
REMARK 470 LEU C 485 CG CD1 CD2
REMARK 470 ARG C 487 CG CD NE CZ NH1 NH2
REMARK 470 MET C 488 CG SD CE
REMARK 470 LEU C 491 CG CD1 CD2
REMARK 470 ILE C 492 CG1 CG2 CD1
REMARK 470 MET C 495 CG SD CE
REMARK 470 SER C 498 OG
REMARK 470 VAL C 499 CG1 CG2
REMARK 470 GLU C 501 CG CD OE1 OE2
REMARK 470 ILE C 503 CG1 CG2 CD1
REMARK 470 ILE C 505 CG1 CG2 CD1
REMARK 470 PHE C 506 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 507 CG CD1 CD2
REMARK 470 LEU C 508 CG CD1 CD2
REMARK 470 SER C 518 OG
REMARK 470 ASP C 519 CG OD1 OD2
REMARK 470 PHE C 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 528 CG1 CG2 CD1
REMARK 470 ILE C 534 CD1
REMARK 470 SER C 536 OG
REMARK 470 VAL C 537 CG1 CG2
REMARK 470 PHE C 538 CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU C 541 CG CD1 CD2
REMARK 470 TYR C 544 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 545 CG CD CE NZ
REMARK 470 MET C 574 CG SD CE
REMARK 470 MET C 578 CG SD CE
REMARK 470 ASP C 586 CG OD1 OD2
REMARK 470 ILE C 609 CG1 CG2 CD1
REMARK 470 GLU C 610 CG CD OE1 OE2
REMARK 470 LYS C 611 CG CD CE NZ
REMARK 470 CYS C 612 SG
REMARK 470 LYS C 614 CG CD CE NZ
REMARK 470 ASP C 615 CG OD1 OD2
REMARK 470 ASN C 616 CG OD1 ND2
REMARK 470 LYS C 617 CG CD CE NZ
REMARK 470 ASP C 618 CG OD1 OD2
REMARK 470 CYS C 619 SG
REMARK 470 SER C 624 OG
REMARK 470 ASP C 627 OD1 OD2
REMARK 470 ASP C 641 CG OD1 OD2
REMARK 470 GLN C 645 CG CD OE1 NE2
REMARK 470 ASN C 647 CG OD1 ND2
REMARK 470 SER C 648 OG
REMARK 470 LYS C 649 CG CD CE NZ
REMARK 470 GLU C 682 CG CD OE1 OE2
REMARK 470 ASN C 683 CG OD1 ND2
REMARK 470 LYS C 686 CG CD CE NZ
REMARK 470 GLU C 687 CG CD OE1 OE2
REMARK 470 GLU C 689 CG CD OE1 OE2
REMARK 470 ILE C 700 CD1
REMARK 470 GLU C 702 CG CD OE1 OE2
REMARK 470 GLU C 704 CG CD OE1 OE2
REMARK 470 LYS C 705 CD CE NZ
REMARK 470 GLU C 709 CG CD OE1 OE2
REMARK 470 LEU C 711 CG CD1 CD2
REMARK 470 ARG C 714 CG CD NE CZ NH1 NH2
REMARK 470 MET C 717 CE
REMARK 470 GLU C 725 CG CD OE1 OE2
REMARK 470 ASP C 726 CG OD1 OD2
REMARK 470 ASP C 727 CG OD1 OD2
REMARK 470 GLU C 741 CG CD OE1 OE2
REMARK 470 ASN C 750 CG OD1 ND2
REMARK 470 GLU D 110 CG CD OE1 OE2
REMARK 470 GLU D 111 CG CD OE1 OE2
REMARK 470 GLN D 112 CG CD OE1 NE2
REMARK 470 ARG D 113 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 114 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 115 CG CD CE NZ
REMARK 470 LYS D 116 CG CD CE NZ
REMARK 470 ARG D 117 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 118 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 119 CG CD1 CD2
REMARK 470 LYS D 120 CG CD CE NZ
REMARK 470 LYS D 121 CG CD CE NZ
REMARK 470 ARG D 122 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 123 CG1 CG2 CD1
REMARK 470 VAL D 127 CG1 CG2
REMARK 470 SER D 128 OG
REMARK 470 GLU D 129 CG CD OE1 OE2
REMARK 470 CYS D 131 SG
REMARK 470 VAL D 132 CG1 CG2
REMARK 470 GLU D 133 CG CD OE1 OE2
REMARK 470 GLU D 134 CG CD OE1 OE2
REMARK 470 LEU D 135 CG CD1 CD2
REMARK 470 VAL D 136 CG1 CG2
REMARK 470 GLU D 137 CG CD OE1 OE2
REMARK 470 LEU D 138 CG CD1 CD2
REMARK 470 LEU D 139 CG CD1 CD2
REMARK 470 VAL D 140 CG1 CG2
REMARK 470 GLU D 141 CG CD OE1 OE2
REMARK 470 LEU D 142 CG CD1 CD2
REMARK 470 GLN D 143 CG CD OE1 NE2
REMARK 470 GLU D 144 CG CD OE1 OE2
REMARK 470 LEU D 145 CG CD1 CD2
REMARK 470 CYS D 146 SG
REMARK 470 ARG D 147 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 148 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 149 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 156 CG OD1 OD2
REMARK 470 PHE D 157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET D 159 CG SD CE
REMARK 470 LYS D 161 CG CD CE NZ
REMARK 470 THR D 163 OG1 CG2
REMARK 470 SER D 165 OG
REMARK 470 ASP D 166 CG OD1 OD2
REMARK 470 THR D 167 OG1 CG2
REMARK 470 CYS D 171 SG
REMARK 470 LYS D 174 CG CD CE NZ
REMARK 470 ASN D 178 CG OD1 ND2
REMARK 470 ILE D 179 CG1 CG2 CD1
REMARK 470 ASN D 182 CG OD1 ND2
REMARK 470 THR D 183 OG1 CG2
REMARK 470 LYS D 184 CG CD CE NZ
REMARK 470 GLU D 185 CG CD OE1 OE2
REMARK 470 VAL D 187 CG1 CG2
REMARK 470 ARG D 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 195 CG CD OE1 OE2
REMARK 470 GLU D 196 CG CD OE1 OE2
REMARK 470 ASN D 197 CG OD1 ND2
REMARK 470 ASP D 198 CG OD1 OD2
REMARK 470 ILE D 199 CG1 CG2 CD1
REMARK 470 ARG D 202 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 205 CG OD1 ND2
REMARK 470 GLU D 207 CG CD OE1 OE2
REMARK 470 THR D 209 OG1 CG2
REMARK 470 GLU D 210 CG CD OE1 OE2
REMARK 470 GLU D 211 CG CD OE1 OE2
REMARK 470 GLU D 214 CG CD OE1 OE2
REMARK 470 THR D 217 OG1 CG2
REMARK 470 GLU D 224 CG CD OE1 OE2
REMARK 470 ASP D 229 CG OD1 OD2
REMARK 470 LEU D 234 CG CD1 CD2
REMARK 470 ILE D 235 CG1 CG2 CD1
REMARK 470 ASP D 240 CG OD1 OD2
REMARK 470 LYS D 246 CG CD CE NZ
REMARK 470 LYS D 253 CG CD CE NZ
REMARK 470 TYR D 254 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS D 256 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 257 CG CD OE1 OE2
REMARK 470 CYS D 271 SG
REMARK 470 GLU D 276 CG CD OE1 OE2
REMARK 470 GLU D 283 CG CD OE1 OE2
REMARK 470 GLU D 285 CG CD OE1 OE2
REMARK 470 GLN D 286 CG CD OE1 NE2
REMARK 470 ASN D 297 CG OD1 ND2
REMARK 470 GLU D 308 CG CD OE1 OE2
REMARK 470 PHE D 310 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 311 CG CD CE NZ
REMARK 470 GLN D 313 CG CD OE1 NE2
REMARK 470 LYS D 318 CE NZ
REMARK 470 MET D 320 CE
REMARK 470 MET D 323 CE
REMARK 470 ARG D 327 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 330 CG OD1 ND2
REMARK 470 GLU D 332 CG CD OE1 OE2
REMARK 470 THR D 335 OG1 CG2
REMARK 470 GLN D 346 CG CD OE1 NE2
REMARK 470 GLU D 355 CG CD OE1 OE2
REMARK 470 GLU D 364 CG CD OE1 OE2
REMARK 470 LYS D 366 CG CD CE NZ
REMARK 470 GLU D 367 CG CD OE1 OE2
REMARK 470 LYS D 368 CG CD CE NZ
REMARK 470 SER D 374 OG
REMARK 470 THR D 399 OG1 CG2
REMARK 470 GLU D 405 CG CD OE1 OE2
REMARK 470 THR D 411 OG1 CG2
REMARK 470 ASN D 412 CG OD1 ND2
REMARK 470 ASP D 414 CG OD1 OD2
REMARK 470 GLU D 418 CG CD OE1 OE2
REMARK 470 GLU D 423 CG CD OE1 OE2
REMARK 470 PHE D 442 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 462 CG CD NE CZ NH1 NH2
REMARK 470 TRP D 481 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 481 CZ3 CH2
REMARK 470 LEU D 482 CG CD1 CD2
REMARK 470 GLN D 483 CG CD OE1 NE2
REMARK 470 LEU D 484 CG CD1 CD2
REMARK 470 LEU D 485 CG CD1 CD2
REMARK 470 ARG D 487 CG CD NE CZ NH1 NH2
REMARK 470 MET D 488 CG SD CE
REMARK 470 LEU D 491 CG CD1 CD2
REMARK 470 ILE D 492 CG1 CG2 CD1
REMARK 470 MET D 495 CG SD CE
REMARK 470 SER D 498 OG
REMARK 470 VAL D 499 CG1 CG2
REMARK 470 GLU D 501 CG CD OE1 OE2
REMARK 470 ILE D 503 CG1 CG2 CD1
REMARK 470 ILE D 505 CG1 CG2 CD1
REMARK 470 PHE D 506 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D 507 CG CD1 CD2
REMARK 470 LEU D 508 CG CD1 CD2
REMARK 470 SER D 518 OG
REMARK 470 ASP D 519 CG OD1 OD2
REMARK 470 PHE D 524 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE D 528 CG1 CG2 CD1
REMARK 470 ILE D 534 CD1
REMARK 470 SER D 536 OG
REMARK 470 VAL D 537 CG1 CG2
REMARK 470 PHE D 538 CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D 541 CG CD1 CD2
REMARK 470 TYR D 544 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 545 CG CD CE NZ
REMARK 470 MET D 574 CG SD CE
REMARK 470 MET D 578 CG SD CE
REMARK 470 ASP D 586 CG OD1 OD2
REMARK 470 ILE D 609 CG1 CG2 CD1
REMARK 470 GLU D 610 CG CD OE1 OE2
REMARK 470 LYS D 611 CG CD CE NZ
REMARK 470 CYS D 612 SG
REMARK 470 LYS D 614 CG CD CE NZ
REMARK 470 ASP D 615 CG OD1 OD2
REMARK 470 ASN D 616 CG OD1 ND2
REMARK 470 LYS D 617 CG CD CE NZ
REMARK 470 ASP D 618 CG OD1 OD2
REMARK 470 CYS D 619 SG
REMARK 470 SER D 624 OG
REMARK 470 ASP D 627 OD1 OD2
REMARK 470 ASP D 641 CG OD1 OD2
REMARK 470 GLN D 645 CG CD OE1 NE2
REMARK 470 ASN D 647 CG OD1 ND2
REMARK 470 SER D 648 OG
REMARK 470 LYS D 649 CG CD CE NZ
REMARK 470 GLU D 682 CG CD OE1 OE2
REMARK 470 ASN D 683 CG OD1 ND2
REMARK 470 LYS D 686 CG CD CE NZ
REMARK 470 GLU D 687 CG CD OE1 OE2
REMARK 470 GLU D 689 CG CD OE1 OE2
REMARK 470 ILE D 700 CD1
REMARK 470 GLU D 702 CG CD OE1 OE2
REMARK 470 GLU D 704 CG CD OE1 OE2
REMARK 470 LYS D 705 CD CE NZ
REMARK 470 GLU D 709 CG CD OE1 OE2
REMARK 470 LEU D 711 CG CD1 CD2
REMARK 470 ARG D 714 CG CD NE CZ NH1 NH2
REMARK 470 MET D 717 CE
REMARK 470 GLU D 725 CG CD OE1 OE2
REMARK 470 ASP D 726 CG OD1 OD2
REMARK 470 ASP D 727 CG OD1 OD2
REMARK 470 GLU D 741 CG CD OE1 OE2
REMARK 470 ASN D 750 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HB2 HIS A 426 H15 FZ4 A 1001 0.75
REMARK 500 HB2 HIS D 426 H15 FZ4 D 1001 0.75
REMARK 500 HB2 HIS B 426 H15 FZ4 B 1001 0.75
REMARK 500 HB2 HIS C 426 H15 FZ4 C 1001 0.75
REMARK 500 HB2 HIS A 426 N17 FZ4 A 1001 0.93
REMARK 500 HB2 HIS D 426 N17 FZ4 D 1001 0.93
REMARK 500 HB2 HIS B 426 N17 FZ4 B 1001 0.93
REMARK 500 HB2 HIS C 426 N17 FZ4 C 1001 0.93
REMARK 500 HB2 HIS A 426 H16 FZ4 A 1001 0.99
REMARK 500 HB2 HIS C 426 H16 FZ4 C 1001 0.99
REMARK 500 HB2 HIS D 426 H16 FZ4 D 1001 0.99
REMARK 500 HB2 HIS B 426 H16 FZ4 B 1001 0.99
REMARK 500 ND1 HIS B 426 H14 FZ4 B 1001 1.16
REMARK 500 ND1 HIS C 426 H14 FZ4 C 1001 1.16
REMARK 500 ND1 HIS D 426 H14 FZ4 D 1001 1.16
REMARK 500 ND1 HIS A 426 H14 FZ4 A 1001 1.16
REMARK 500 HD13 LEU A 420 H2 FZ4 A 1001 1.25
REMARK 500 HD13 LEU D 420 H2 FZ4 D 1001 1.25
REMARK 500 HD13 LEU C 420 H2 FZ4 C 1001 1.25
REMARK 500 HD13 LEU B 420 H2 FZ4 B 1001 1.25
REMARK 500 CB HIS C 426 H15 FZ4 C 1001 1.31
REMARK 500 CB HIS D 426 H15 FZ4 D 1001 1.31
REMARK 500 CB HIS A 426 H15 FZ4 A 1001 1.31
REMARK 500 CB HIS B 426 H15 FZ4 B 1001 1.31
REMARK 500 CB HIS B 426 H16 FZ4 B 1001 1.35
REMARK 500 CB HIS C 426 H16 FZ4 C 1001 1.35
REMARK 500 CB HIS D 426 H16 FZ4 D 1001 1.35
REMARK 500 CB HIS A 426 H16 FZ4 A 1001 1.35
REMARK 500 CG HIS A 426 H14 FZ4 A 1001 1.42
REMARK 500 CG HIS B 426 H14 FZ4 B 1001 1.42
REMARK 500 CG HIS C 426 H14 FZ4 C 1001 1.42
REMARK 500 CG HIS D 426 H14 FZ4 D 1001 1.42
REMARK 500 CB HIS A 426 N17 FZ4 A 1001 1.62
REMARK 500 CB HIS D 426 N17 FZ4 D 1001 1.62
REMARK 500 CB HIS B 426 N17 FZ4 B 1001 1.62
REMARK 500 CB HIS C 426 N17 FZ4 C 1001 1.62
REMARK 500 ND1 HIS B 426 C16 FZ4 B 1001 1.76
REMARK 500 ND1 HIS C 426 C16 FZ4 C 1001 1.76
REMARK 500 ND1 HIS D 426 C16 FZ4 D 1001 1.76
REMARK 500 ND1 HIS A 426 C16 FZ4 A 1001 1.76
REMARK 500 ND2 ASN A 273 CB ASN D 750 1.92
REMARK 500 CB ASN B 750 ND2 ASN C 273 1.92
REMARK 500 CB ASN C 750 ND2 ASN D 273 1.92
REMARK 500 CB ASN A 750 ND2 ASN B 273 1.93
REMARK 500 CG HIS A 426 N17 FZ4 A 1001 1.96
REMARK 500 CG HIS B 426 N17 FZ4 B 1001 1.96
REMARK 500 CG HIS C 426 N17 FZ4 C 1001 1.96
REMARK 500 CG HIS D 426 N17 FZ4 D 1001 1.96
REMARK 500 CG HIS B 426 C16 FZ4 B 1001 1.97
REMARK 500 CG HIS C 426 C16 FZ4 C 1001 1.97
REMARK 500
REMARK 500 THIS ENTRY HAS 60 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 216 147.99 -173.49
REMARK 500 ASN A 251 70.26 -150.05
REMARK 500 GLN A 274 109.56 -56.30
REMARK 500 LYS A 376 75.10 60.93
REMARK 500 ASN A 415 24.11 -140.38
REMARK 500 ALA A 520 30.37 -97.60
REMARK 500 PRO A 708 -177.92 -69.74
REMARK 500 GLN B 216 147.99 -173.50
REMARK 500 ASN B 251 70.32 -150.01
REMARK 500 GLN B 274 109.50 -56.30
REMARK 500 LYS B 376 75.11 60.92
REMARK 500 ASN B 415 24.14 -140.38
REMARK 500 ALA B 520 30.38 -97.59
REMARK 500 PRO B 708 -177.92 -69.78
REMARK 500 GLN C 216 147.99 -173.50
REMARK 500 ASN C 251 70.32 -150.01
REMARK 500 GLN C 274 109.50 -56.30
REMARK 500 LYS C 376 75.11 60.92
REMARK 500 ASN C 415 24.14 -140.38
REMARK 500 ALA C 520 30.38 -97.59
REMARK 500 PRO C 708 -177.92 -69.73
REMARK 500 GLN D 216 147.99 -173.50
REMARK 500 ASN D 251 70.32 -150.01
REMARK 500 GLN D 274 109.50 -56.30
REMARK 500 LYS D 376 75.11 60.92
REMARK 500 ASN D 415 24.14 -140.38
REMARK 500 ALA D 520 30.38 -97.59
REMARK 500 PRO D 708 -177.92 -69.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FZ4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FZ4 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FZ4 C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FZ4 D 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-20194 RELATED DB: EMDB
REMARK 900 STRUCTURE OF THE TRPV3 K169A SENSITIZED MUTANT IN THE PRESENCE OF 2-
REMARK 900 APB AT 3.6 A RESOLUTION
REMARK 900 RELATED ID: EMD-20192 RELATED DB: EMDB
REMARK 900 STRUCTURE OF THE TRPV3 K169A SENSITIZED MUTANT IN APO FORM AT 4.1 A
REMARK 900 RESOLUTION
DBREF 6OT5 A 1 12 PDB 6OT5 6OT5 1 12
DBREF 6OT5 A 110 790 UNP Q8NET8 TRPV3_HUMAN 110 790
DBREF 6OT5 B 1 12 PDB 6OT5 6OT5 1 12
DBREF 6OT5 B 110 790 UNP Q8NET8 TRPV3_HUMAN 110 790
DBREF 6OT5 C 1 12 PDB 6OT5 6OT5 1 12
DBREF 6OT5 C 110 790 UNP Q8NET8 TRPV3_HUMAN 110 790
DBREF 6OT5 D 1 12 PDB 6OT5 6OT5 1 12
DBREF 6OT5 D 110 790 UNP Q8NET8 TRPV3_HUMAN 110 790
SEQADV 6OT5 ALA A 169 UNP Q8NET8 LYS 169 ENGINEERED MUTATION
SEQADV 6OT5 VAL A 791 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 792 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA A 793 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY A 794 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU A 795 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLU A 796 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 VAL A 797 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU A 798 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 PHE A 799 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLN A 800 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY A 801 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 802 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 TYR A 803 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS A 804 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 805 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 806 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 807 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP A 808 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS A 809 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA A 810 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 811 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 812 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 813 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 814 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 815 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS A 816 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA B 169 UNP Q8NET8 LYS 169 ENGINEERED MUTATION
SEQADV 6OT5 VAL B 791 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 792 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA B 793 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY B 794 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU B 795 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLU B 796 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 VAL B 797 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU B 798 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 PHE B 799 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLN B 800 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY B 801 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 802 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 TYR B 803 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS B 804 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 805 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 806 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 807 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP B 808 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS B 809 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA B 810 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 811 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 812 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 813 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 814 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 815 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS B 816 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA C 169 UNP Q8NET8 LYS 169 ENGINEERED MUTATION
SEQADV 6OT5 VAL C 791 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 792 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA C 793 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY C 794 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU C 795 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLU C 796 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 VAL C 797 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU C 798 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 PHE C 799 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLN C 800 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY C 801 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 802 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 TYR C 803 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS C 804 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 805 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 806 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 807 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP C 808 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS C 809 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA C 810 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 811 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 812 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 813 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 814 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 815 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS C 816 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA D 169 UNP Q8NET8 LYS 169 ENGINEERED MUTATION
SEQADV 6OT5 VAL D 791 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 792 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA D 793 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY D 794 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU D 795 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLU D 796 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 VAL D 797 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LEU D 798 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 PHE D 799 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLN D 800 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 GLY D 801 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 802 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 TYR D 803 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS D 804 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 805 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 806 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 807 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ASP D 808 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 LYS D 809 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 ALA D 810 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 811 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 812 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 813 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 814 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 815 UNP Q8NET8 EXPRESSION TAG
SEQADV 6OT5 HIS D 816 UNP Q8NET8 EXPRESSION TAG
SEQRES 1 A 719 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK GLU
SEQRES 2 A 719 GLU GLN ARG ARG LYS LYS ARG ARG LEU LYS LYS ARG ILE
SEQRES 3 A 719 PHE ALA ALA VAL SER GLU GLY CYS VAL GLU GLU LEU VAL
SEQRES 4 A 719 GLU LEU LEU VAL GLU LEU GLN GLU LEU CYS ARG ARG ARG
SEQRES 5 A 719 HIS ASP GLU ASP VAL PRO ASP PHE LEU MET HIS LYS LEU
SEQRES 6 A 719 THR ALA SER ASP THR GLY ALA THR CYS LEU MET LYS ALA
SEQRES 7 A 719 LEU LEU ASN ILE ASN PRO ASN THR LYS GLU ILE VAL ARG
SEQRES 8 A 719 ILE LEU LEU ALA PHE ALA GLU GLU ASN ASP ILE LEU GLY
SEQRES 9 A 719 ARG PHE ILE ASN ALA GLU TYR THR GLU GLU ALA TYR GLU
SEQRES 10 A 719 GLY GLN THR ALA LEU ASN ILE ALA ILE GLU ARG ARG GLN
SEQRES 11 A 719 GLY ASP ILE ALA ALA LEU LEU ILE ALA ALA GLY ALA ASP
SEQRES 12 A 719 VAL ASN ALA HIS ALA LYS GLY ALA PHE PHE ASN PRO LYS
SEQRES 13 A 719 TYR GLN HIS GLU GLY PHE TYR PHE GLY GLU THR PRO LEU
SEQRES 14 A 719 ALA LEU ALA ALA CYS THR ASN GLN PRO GLU ILE VAL GLN
SEQRES 15 A 719 LEU LEU MET GLU HIS GLU GLN THR ASP ILE THR SER ARG
SEQRES 16 A 719 ASP SER ARG GLY ASN ASN ILE LEU HIS ALA LEU VAL THR
SEQRES 17 A 719 VAL ALA GLU ASP PHE LYS THR GLN ASN ASP PHE VAL LYS
SEQRES 18 A 719 ARG MET TYR ASP MET ILE LEU LEU ARG SER GLY ASN TRP
SEQRES 19 A 719 GLU LEU GLU THR THR ARG ASN ASN ASP GLY LEU THR PRO
SEQRES 20 A 719 LEU GLN LEU ALA ALA LYS MET GLY LYS ALA GLU ILE LEU
SEQRES 21 A 719 LYS TYR ILE LEU SER ARG GLU ILE LYS GLU LYS ARG LEU
SEQRES 22 A 719 ARG SER LEU SER ARG LYS PHE THR ASP TRP ALA TYR GLY
SEQRES 23 A 719 PRO VAL SER SER SER LEU TYR ASP LEU THR ASN VAL ASP
SEQRES 24 A 719 THR THR THR ASP ASN SER VAL LEU GLU ILE THR VAL TYR
SEQRES 25 A 719 ASN THR ASN ILE ASP ASN ARG HIS GLU MET LEU THR LEU
SEQRES 26 A 719 GLU PRO LEU HIS THR LEU LEU HIS MET LYS TRP LYS LYS
SEQRES 27 A 719 PHE ALA LYS HIS MET PHE PHE LEU SER PHE CYS PHE TYR
SEQRES 28 A 719 PHE PHE TYR ASN ILE THR LEU THR LEU VAL SER TYR TYR
SEQRES 29 A 719 ARG PRO ARG GLU GLU GLU ALA ILE PRO HIS PRO LEU ALA
SEQRES 30 A 719 LEU THR HIS LYS MET GLY TRP LEU GLN LEU LEU GLY ARG
SEQRES 31 A 719 MET PHE VAL LEU ILE TRP ALA MET CYS ILE SER VAL LYS
SEQRES 32 A 719 GLU GLY ILE ALA ILE PHE LEU LEU ARG PRO SER ASP LEU
SEQRES 33 A 719 GLN SER ILE LEU SER ASP ALA TRP PHE HIS PHE VAL PHE
SEQRES 34 A 719 PHE ILE GLN ALA VAL LEU VAL ILE LEU SER VAL PHE LEU
SEQRES 35 A 719 TYR LEU PHE ALA TYR LYS GLU TYR LEU ALA CYS LEU VAL
SEQRES 36 A 719 LEU ALA MET ALA LEU GLY TRP ALA ASN MET LEU TYR TYR
SEQRES 37 A 719 THR ARG GLY PHE GLN SER MET GLY MET TYR SER VAL MET
SEQRES 38 A 719 ILE GLN LYS VAL ILE LEU HIS ASP VAL LEU LYS PHE LEU
SEQRES 39 A 719 PHE VAL TYR ILE VAL PHE LEU LEU GLY PHE GLY VAL ALA
SEQRES 40 A 719 LEU ALA SER LEU ILE GLU LYS CYS PRO LYS ASP ASN LYS
SEQRES 41 A 719 ASP CYS SER SER TYR GLY SER PHE SER ASP ALA VAL LEU
SEQRES 42 A 719 GLU LEU PHE LYS LEU THR ILE GLY LEU GLY ASP LEU ASN
SEQRES 43 A 719 ILE GLN GLN ASN SER LYS TYR PRO ILE LEU PHE LEU PHE
SEQRES 44 A 719 LEU LEU ILE THR TYR VAL ILE LEU THR PHE VAL LEU LEU
SEQRES 45 A 719 LEU ASN MET LEU ILE ALA LEU MET GLY GLU THR VAL GLU
SEQRES 46 A 719 ASN VAL SER LYS GLU SER GLU ARG ILE TRP ARG LEU GLN
SEQRES 47 A 719 ARG ALA ARG THR ILE LEU GLU PHE GLU LYS MET LEU PRO
SEQRES 48 A 719 GLU TRP LEU ARG SER ARG PHE ARG MET GLY GLU LEU CYS
SEQRES 49 A 719 LYS VAL ALA GLU ASP ASP PHE ARG LEU CYS LEU ARG ILE
SEQRES 50 A 719 ASN GLU VAL LYS TRP THR GLU TRP LYS THR HIS VAL SER
SEQRES 51 A 719 PHE LEU ASN GLU ASP PRO GLY PRO VAL ARG ARG THR ASP
SEQRES 52 A 719 PHE ASN LYS ILE GLN ASP SER SER ARG ASN ASN SER LYS
SEQRES 53 A 719 THR THR LEU ASN ALA PHE GLU GLU VAL GLU GLU PHE PRO
SEQRES 54 A 719 GLU THR SER VAL VAL ASP ALA GLY LEU GLU VAL LEU PHE
SEQRES 55 A 719 GLN GLY ASP TYR LYS ASP ASP ASP ASP LYS ALA HIS HIS
SEQRES 56 A 719 HIS HIS HIS HIS
SEQRES 1 B 719 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK GLU
SEQRES 2 B 719 GLU GLN ARG ARG LYS LYS ARG ARG LEU LYS LYS ARG ILE
SEQRES 3 B 719 PHE ALA ALA VAL SER GLU GLY CYS VAL GLU GLU LEU VAL
SEQRES 4 B 719 GLU LEU LEU VAL GLU LEU GLN GLU LEU CYS ARG ARG ARG
SEQRES 5 B 719 HIS ASP GLU ASP VAL PRO ASP PHE LEU MET HIS LYS LEU
SEQRES 6 B 719 THR ALA SER ASP THR GLY ALA THR CYS LEU MET LYS ALA
SEQRES 7 B 719 LEU LEU ASN ILE ASN PRO ASN THR LYS GLU ILE VAL ARG
SEQRES 8 B 719 ILE LEU LEU ALA PHE ALA GLU GLU ASN ASP ILE LEU GLY
SEQRES 9 B 719 ARG PHE ILE ASN ALA GLU TYR THR GLU GLU ALA TYR GLU
SEQRES 10 B 719 GLY GLN THR ALA LEU ASN ILE ALA ILE GLU ARG ARG GLN
SEQRES 11 B 719 GLY ASP ILE ALA ALA LEU LEU ILE ALA ALA GLY ALA ASP
SEQRES 12 B 719 VAL ASN ALA HIS ALA LYS GLY ALA PHE PHE ASN PRO LYS
SEQRES 13 B 719 TYR GLN HIS GLU GLY PHE TYR PHE GLY GLU THR PRO LEU
SEQRES 14 B 719 ALA LEU ALA ALA CYS THR ASN GLN PRO GLU ILE VAL GLN
SEQRES 15 B 719 LEU LEU MET GLU HIS GLU GLN THR ASP ILE THR SER ARG
SEQRES 16 B 719 ASP SER ARG GLY ASN ASN ILE LEU HIS ALA LEU VAL THR
SEQRES 17 B 719 VAL ALA GLU ASP PHE LYS THR GLN ASN ASP PHE VAL LYS
SEQRES 18 B 719 ARG MET TYR ASP MET ILE LEU LEU ARG SER GLY ASN TRP
SEQRES 19 B 719 GLU LEU GLU THR THR ARG ASN ASN ASP GLY LEU THR PRO
SEQRES 20 B 719 LEU GLN LEU ALA ALA LYS MET GLY LYS ALA GLU ILE LEU
SEQRES 21 B 719 LYS TYR ILE LEU SER ARG GLU ILE LYS GLU LYS ARG LEU
SEQRES 22 B 719 ARG SER LEU SER ARG LYS PHE THR ASP TRP ALA TYR GLY
SEQRES 23 B 719 PRO VAL SER SER SER LEU TYR ASP LEU THR ASN VAL ASP
SEQRES 24 B 719 THR THR THR ASP ASN SER VAL LEU GLU ILE THR VAL TYR
SEQRES 25 B 719 ASN THR ASN ILE ASP ASN ARG HIS GLU MET LEU THR LEU
SEQRES 26 B 719 GLU PRO LEU HIS THR LEU LEU HIS MET LYS TRP LYS LYS
SEQRES 27 B 719 PHE ALA LYS HIS MET PHE PHE LEU SER PHE CYS PHE TYR
SEQRES 28 B 719 PHE PHE TYR ASN ILE THR LEU THR LEU VAL SER TYR TYR
SEQRES 29 B 719 ARG PRO ARG GLU GLU GLU ALA ILE PRO HIS PRO LEU ALA
SEQRES 30 B 719 LEU THR HIS LYS MET GLY TRP LEU GLN LEU LEU GLY ARG
SEQRES 31 B 719 MET PHE VAL LEU ILE TRP ALA MET CYS ILE SER VAL LYS
SEQRES 32 B 719 GLU GLY ILE ALA ILE PHE LEU LEU ARG PRO SER ASP LEU
SEQRES 33 B 719 GLN SER ILE LEU SER ASP ALA TRP PHE HIS PHE VAL PHE
SEQRES 34 B 719 PHE ILE GLN ALA VAL LEU VAL ILE LEU SER VAL PHE LEU
SEQRES 35 B 719 TYR LEU PHE ALA TYR LYS GLU TYR LEU ALA CYS LEU VAL
SEQRES 36 B 719 LEU ALA MET ALA LEU GLY TRP ALA ASN MET LEU TYR TYR
SEQRES 37 B 719 THR ARG GLY PHE GLN SER MET GLY MET TYR SER VAL MET
SEQRES 38 B 719 ILE GLN LYS VAL ILE LEU HIS ASP VAL LEU LYS PHE LEU
SEQRES 39 B 719 PHE VAL TYR ILE VAL PHE LEU LEU GLY PHE GLY VAL ALA
SEQRES 40 B 719 LEU ALA SER LEU ILE GLU LYS CYS PRO LYS ASP ASN LYS
SEQRES 41 B 719 ASP CYS SER SER TYR GLY SER PHE SER ASP ALA VAL LEU
SEQRES 42 B 719 GLU LEU PHE LYS LEU THR ILE GLY LEU GLY ASP LEU ASN
SEQRES 43 B 719 ILE GLN GLN ASN SER LYS TYR PRO ILE LEU PHE LEU PHE
SEQRES 44 B 719 LEU LEU ILE THR TYR VAL ILE LEU THR PHE VAL LEU LEU
SEQRES 45 B 719 LEU ASN MET LEU ILE ALA LEU MET GLY GLU THR VAL GLU
SEQRES 46 B 719 ASN VAL SER LYS GLU SER GLU ARG ILE TRP ARG LEU GLN
SEQRES 47 B 719 ARG ALA ARG THR ILE LEU GLU PHE GLU LYS MET LEU PRO
SEQRES 48 B 719 GLU TRP LEU ARG SER ARG PHE ARG MET GLY GLU LEU CYS
SEQRES 49 B 719 LYS VAL ALA GLU ASP ASP PHE ARG LEU CYS LEU ARG ILE
SEQRES 50 B 719 ASN GLU VAL LYS TRP THR GLU TRP LYS THR HIS VAL SER
SEQRES 51 B 719 PHE LEU ASN GLU ASP PRO GLY PRO VAL ARG ARG THR ASP
SEQRES 52 B 719 PHE ASN LYS ILE GLN ASP SER SER ARG ASN ASN SER LYS
SEQRES 53 B 719 THR THR LEU ASN ALA PHE GLU GLU VAL GLU GLU PHE PRO
SEQRES 54 B 719 GLU THR SER VAL VAL ASP ALA GLY LEU GLU VAL LEU PHE
SEQRES 55 B 719 GLN GLY ASP TYR LYS ASP ASP ASP ASP LYS ALA HIS HIS
SEQRES 56 B 719 HIS HIS HIS HIS
SEQRES 1 C 719 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK GLU
SEQRES 2 C 719 GLU GLN ARG ARG LYS LYS ARG ARG LEU LYS LYS ARG ILE
SEQRES 3 C 719 PHE ALA ALA VAL SER GLU GLY CYS VAL GLU GLU LEU VAL
SEQRES 4 C 719 GLU LEU LEU VAL GLU LEU GLN GLU LEU CYS ARG ARG ARG
SEQRES 5 C 719 HIS ASP GLU ASP VAL PRO ASP PHE LEU MET HIS LYS LEU
SEQRES 6 C 719 THR ALA SER ASP THR GLY ALA THR CYS LEU MET LYS ALA
SEQRES 7 C 719 LEU LEU ASN ILE ASN PRO ASN THR LYS GLU ILE VAL ARG
SEQRES 8 C 719 ILE LEU LEU ALA PHE ALA GLU GLU ASN ASP ILE LEU GLY
SEQRES 9 C 719 ARG PHE ILE ASN ALA GLU TYR THR GLU GLU ALA TYR GLU
SEQRES 10 C 719 GLY GLN THR ALA LEU ASN ILE ALA ILE GLU ARG ARG GLN
SEQRES 11 C 719 GLY ASP ILE ALA ALA LEU LEU ILE ALA ALA GLY ALA ASP
SEQRES 12 C 719 VAL ASN ALA HIS ALA LYS GLY ALA PHE PHE ASN PRO LYS
SEQRES 13 C 719 TYR GLN HIS GLU GLY PHE TYR PHE GLY GLU THR PRO LEU
SEQRES 14 C 719 ALA LEU ALA ALA CYS THR ASN GLN PRO GLU ILE VAL GLN
SEQRES 15 C 719 LEU LEU MET GLU HIS GLU GLN THR ASP ILE THR SER ARG
SEQRES 16 C 719 ASP SER ARG GLY ASN ASN ILE LEU HIS ALA LEU VAL THR
SEQRES 17 C 719 VAL ALA GLU ASP PHE LYS THR GLN ASN ASP PHE VAL LYS
SEQRES 18 C 719 ARG MET TYR ASP MET ILE LEU LEU ARG SER GLY ASN TRP
SEQRES 19 C 719 GLU LEU GLU THR THR ARG ASN ASN ASP GLY LEU THR PRO
SEQRES 20 C 719 LEU GLN LEU ALA ALA LYS MET GLY LYS ALA GLU ILE LEU
SEQRES 21 C 719 LYS TYR ILE LEU SER ARG GLU ILE LYS GLU LYS ARG LEU
SEQRES 22 C 719 ARG SER LEU SER ARG LYS PHE THR ASP TRP ALA TYR GLY
SEQRES 23 C 719 PRO VAL SER SER SER LEU TYR ASP LEU THR ASN VAL ASP
SEQRES 24 C 719 THR THR THR ASP ASN SER VAL LEU GLU ILE THR VAL TYR
SEQRES 25 C 719 ASN THR ASN ILE ASP ASN ARG HIS GLU MET LEU THR LEU
SEQRES 26 C 719 GLU PRO LEU HIS THR LEU LEU HIS MET LYS TRP LYS LYS
SEQRES 27 C 719 PHE ALA LYS HIS MET PHE PHE LEU SER PHE CYS PHE TYR
SEQRES 28 C 719 PHE PHE TYR ASN ILE THR LEU THR LEU VAL SER TYR TYR
SEQRES 29 C 719 ARG PRO ARG GLU GLU GLU ALA ILE PRO HIS PRO LEU ALA
SEQRES 30 C 719 LEU THR HIS LYS MET GLY TRP LEU GLN LEU LEU GLY ARG
SEQRES 31 C 719 MET PHE VAL LEU ILE TRP ALA MET CYS ILE SER VAL LYS
SEQRES 32 C 719 GLU GLY ILE ALA ILE PHE LEU LEU ARG PRO SER ASP LEU
SEQRES 33 C 719 GLN SER ILE LEU SER ASP ALA TRP PHE HIS PHE VAL PHE
SEQRES 34 C 719 PHE ILE GLN ALA VAL LEU VAL ILE LEU SER VAL PHE LEU
SEQRES 35 C 719 TYR LEU PHE ALA TYR LYS GLU TYR LEU ALA CYS LEU VAL
SEQRES 36 C 719 LEU ALA MET ALA LEU GLY TRP ALA ASN MET LEU TYR TYR
SEQRES 37 C 719 THR ARG GLY PHE GLN SER MET GLY MET TYR SER VAL MET
SEQRES 38 C 719 ILE GLN LYS VAL ILE LEU HIS ASP VAL LEU LYS PHE LEU
SEQRES 39 C 719 PHE VAL TYR ILE VAL PHE LEU LEU GLY PHE GLY VAL ALA
SEQRES 40 C 719 LEU ALA SER LEU ILE GLU LYS CYS PRO LYS ASP ASN LYS
SEQRES 41 C 719 ASP CYS SER SER TYR GLY SER PHE SER ASP ALA VAL LEU
SEQRES 42 C 719 GLU LEU PHE LYS LEU THR ILE GLY LEU GLY ASP LEU ASN
SEQRES 43 C 719 ILE GLN GLN ASN SER LYS TYR PRO ILE LEU PHE LEU PHE
SEQRES 44 C 719 LEU LEU ILE THR TYR VAL ILE LEU THR PHE VAL LEU LEU
SEQRES 45 C 719 LEU ASN MET LEU ILE ALA LEU MET GLY GLU THR VAL GLU
SEQRES 46 C 719 ASN VAL SER LYS GLU SER GLU ARG ILE TRP ARG LEU GLN
SEQRES 47 C 719 ARG ALA ARG THR ILE LEU GLU PHE GLU LYS MET LEU PRO
SEQRES 48 C 719 GLU TRP LEU ARG SER ARG PHE ARG MET GLY GLU LEU CYS
SEQRES 49 C 719 LYS VAL ALA GLU ASP ASP PHE ARG LEU CYS LEU ARG ILE
SEQRES 50 C 719 ASN GLU VAL LYS TRP THR GLU TRP LYS THR HIS VAL SER
SEQRES 51 C 719 PHE LEU ASN GLU ASP PRO GLY PRO VAL ARG ARG THR ASP
SEQRES 52 C 719 PHE ASN LYS ILE GLN ASP SER SER ARG ASN ASN SER LYS
SEQRES 53 C 719 THR THR LEU ASN ALA PHE GLU GLU VAL GLU GLU PHE PRO
SEQRES 54 C 719 GLU THR SER VAL VAL ASP ALA GLY LEU GLU VAL LEU PHE
SEQRES 55 C 719 GLN GLY ASP TYR LYS ASP ASP ASP ASP LYS ALA HIS HIS
SEQRES 56 C 719 HIS HIS HIS HIS
SEQRES 1 D 719 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK GLU
SEQRES 2 D 719 GLU GLN ARG ARG LYS LYS ARG ARG LEU LYS LYS ARG ILE
SEQRES 3 D 719 PHE ALA ALA VAL SER GLU GLY CYS VAL GLU GLU LEU VAL
SEQRES 4 D 719 GLU LEU LEU VAL GLU LEU GLN GLU LEU CYS ARG ARG ARG
SEQRES 5 D 719 HIS ASP GLU ASP VAL PRO ASP PHE LEU MET HIS LYS LEU
SEQRES 6 D 719 THR ALA SER ASP THR GLY ALA THR CYS LEU MET LYS ALA
SEQRES 7 D 719 LEU LEU ASN ILE ASN PRO ASN THR LYS GLU ILE VAL ARG
SEQRES 8 D 719 ILE LEU LEU ALA PHE ALA GLU GLU ASN ASP ILE LEU GLY
SEQRES 9 D 719 ARG PHE ILE ASN ALA GLU TYR THR GLU GLU ALA TYR GLU
SEQRES 10 D 719 GLY GLN THR ALA LEU ASN ILE ALA ILE GLU ARG ARG GLN
SEQRES 11 D 719 GLY ASP ILE ALA ALA LEU LEU ILE ALA ALA GLY ALA ASP
SEQRES 12 D 719 VAL ASN ALA HIS ALA LYS GLY ALA PHE PHE ASN PRO LYS
SEQRES 13 D 719 TYR GLN HIS GLU GLY PHE TYR PHE GLY GLU THR PRO LEU
SEQRES 14 D 719 ALA LEU ALA ALA CYS THR ASN GLN PRO GLU ILE VAL GLN
SEQRES 15 D 719 LEU LEU MET GLU HIS GLU GLN THR ASP ILE THR SER ARG
SEQRES 16 D 719 ASP SER ARG GLY ASN ASN ILE LEU HIS ALA LEU VAL THR
SEQRES 17 D 719 VAL ALA GLU ASP PHE LYS THR GLN ASN ASP PHE VAL LYS
SEQRES 18 D 719 ARG MET TYR ASP MET ILE LEU LEU ARG SER GLY ASN TRP
SEQRES 19 D 719 GLU LEU GLU THR THR ARG ASN ASN ASP GLY LEU THR PRO
SEQRES 20 D 719 LEU GLN LEU ALA ALA LYS MET GLY LYS ALA GLU ILE LEU
SEQRES 21 D 719 LYS TYR ILE LEU SER ARG GLU ILE LYS GLU LYS ARG LEU
SEQRES 22 D 719 ARG SER LEU SER ARG LYS PHE THR ASP TRP ALA TYR GLY
SEQRES 23 D 719 PRO VAL SER SER SER LEU TYR ASP LEU THR ASN VAL ASP
SEQRES 24 D 719 THR THR THR ASP ASN SER VAL LEU GLU ILE THR VAL TYR
SEQRES 25 D 719 ASN THR ASN ILE ASP ASN ARG HIS GLU MET LEU THR LEU
SEQRES 26 D 719 GLU PRO LEU HIS THR LEU LEU HIS MET LYS TRP LYS LYS
SEQRES 27 D 719 PHE ALA LYS HIS MET PHE PHE LEU SER PHE CYS PHE TYR
SEQRES 28 D 719 PHE PHE TYR ASN ILE THR LEU THR LEU VAL SER TYR TYR
SEQRES 29 D 719 ARG PRO ARG GLU GLU GLU ALA ILE PRO HIS PRO LEU ALA
SEQRES 30 D 719 LEU THR HIS LYS MET GLY TRP LEU GLN LEU LEU GLY ARG
SEQRES 31 D 719 MET PHE VAL LEU ILE TRP ALA MET CYS ILE SER VAL LYS
SEQRES 32 D 719 GLU GLY ILE ALA ILE PHE LEU LEU ARG PRO SER ASP LEU
SEQRES 33 D 719 GLN SER ILE LEU SER ASP ALA TRP PHE HIS PHE VAL PHE
SEQRES 34 D 719 PHE ILE GLN ALA VAL LEU VAL ILE LEU SER VAL PHE LEU
SEQRES 35 D 719 TYR LEU PHE ALA TYR LYS GLU TYR LEU ALA CYS LEU VAL
SEQRES 36 D 719 LEU ALA MET ALA LEU GLY TRP ALA ASN MET LEU TYR TYR
SEQRES 37 D 719 THR ARG GLY PHE GLN SER MET GLY MET TYR SER VAL MET
SEQRES 38 D 719 ILE GLN LYS VAL ILE LEU HIS ASP VAL LEU LYS PHE LEU
SEQRES 39 D 719 PHE VAL TYR ILE VAL PHE LEU LEU GLY PHE GLY VAL ALA
SEQRES 40 D 719 LEU ALA SER LEU ILE GLU LYS CYS PRO LYS ASP ASN LYS
SEQRES 41 D 719 ASP CYS SER SER TYR GLY SER PHE SER ASP ALA VAL LEU
SEQRES 42 D 719 GLU LEU PHE LYS LEU THR ILE GLY LEU GLY ASP LEU ASN
SEQRES 43 D 719 ILE GLN GLN ASN SER LYS TYR PRO ILE LEU PHE LEU PHE
SEQRES 44 D 719 LEU LEU ILE THR TYR VAL ILE LEU THR PHE VAL LEU LEU
SEQRES 45 D 719 LEU ASN MET LEU ILE ALA LEU MET GLY GLU THR VAL GLU
SEQRES 46 D 719 ASN VAL SER LYS GLU SER GLU ARG ILE TRP ARG LEU GLN
SEQRES 47 D 719 ARG ALA ARG THR ILE LEU GLU PHE GLU LYS MET LEU PRO
SEQRES 48 D 719 GLU TRP LEU ARG SER ARG PHE ARG MET GLY GLU LEU CYS
SEQRES 49 D 719 LYS VAL ALA GLU ASP ASP PHE ARG LEU CYS LEU ARG ILE
SEQRES 50 D 719 ASN GLU VAL LYS TRP THR GLU TRP LYS THR HIS VAL SER
SEQRES 51 D 719 PHE LEU ASN GLU ASP PRO GLY PRO VAL ARG ARG THR ASP
SEQRES 52 D 719 PHE ASN LYS ILE GLN ASP SER SER ARG ASN ASN SER LYS
SEQRES 53 D 719 THR THR LEU ASN ALA PHE GLU GLU VAL GLU GLU PHE PRO
SEQRES 54 D 719 GLU THR SER VAL VAL ASP ALA GLY LEU GLU VAL LEU PHE
SEQRES 55 D 719 GLN GLY ASP TYR LYS ASP ASP ASP ASP LYS ALA HIS HIS
SEQRES 56 D 719 HIS HIS HIS HIS
HET FZ4 A1001 33
HET FZ4 B1001 33
HET FZ4 C1001 33
HET FZ4 D1001 33
HETNAM FZ4 2-AMINOETHYL DIPHENYLBORINATE
FORMUL 5 FZ4 4(C14 H16 B N O)
HELIX 1 AA1 GLU A 111 GLY A 130 1 20
HELIX 2 AA2 VAL A 132 ARG A 149 1 18
HELIX 3 AA3 PRO A 155 THR A 163 1 9
HELIX 4 AA4 THR A 170 ASN A 178 1 9
HELIX 5 AA5 ASN A 182 ASP A 198 1 17
HELIX 6 AA6 ILE A 199 ASN A 205 1 7
HELIX 7 AA7 THR A 217 ARG A 225 1 9
HELIX 8 AA8 GLY A 228 GLY A 238 1 11
HELIX 9 AA9 GLY A 247 ASN A 251 5 5
HELIX 10 AB1 THR A 264 THR A 272 1 9
HELIX 11 AB2 PRO A 275 GLU A 283 1 9
HELIX 12 AB3 ASN A 298 ALA A 307 1 10
HELIX 13 AB4 PHE A 316 SER A 328 1 13
HELIX 14 AB5 TRP A 331 THR A 336 1 6
HELIX 15 AB6 THR A 343 MET A 351 1 9
HELIX 16 AB7 ALA A 354 SER A 362 1 9
HELIX 17 AB8 LEU A 370 SER A 374 5 5
HELIX 18 AB9 SER A 402 TYR A 409 1 8
HELIX 19 AC1 ASN A 415 THR A 421 1 7
HELIX 20 AC2 LEU A 422 PHE A 436 1 15
HELIX 21 AC3 PHE A 436 TYR A 461 1 26
HELIX 22 AC4 TRP A 481 LEU A 507 1 27
HELIX 23 AC5 TRP A 521 PHE A 542 1 22
HELIX 24 AC6 GLU A 546 ASN A 561 1 16
HELIX 25 AC7 MET A 562 ARG A 567 5 6
HELIX 26 AC8 MET A 572 ILE A 583 1 12
HELIX 27 AC9 HIS A 585 ILE A 609 1 25
HELIX 28 AD1 SER A 624 THR A 636 1 13
HELIX 29 AD2 TYR A 650 VAL A 667 1 18
HELIX 30 AD3 LEU A 668 LEU A 707 1 40
HELIX 31 AD4 PRO A 708 PHE A 715 1 8
HELIX 32 AD5 LYS A 738 ASN A 750 1 13
HELIX 33 AD6 GLU B 111 GLY B 130 1 20
HELIX 34 AD7 VAL B 132 ARG B 149 1 18
HELIX 35 AD8 PRO B 155 THR B 163 1 9
HELIX 36 AD9 THR B 170 ASN B 178 1 9
HELIX 37 AE1 ASN B 182 ASP B 198 1 17
HELIX 38 AE2 ILE B 199 ASN B 205 1 7
HELIX 39 AE3 THR B 217 ARG B 225 1 9
HELIX 40 AE4 GLY B 228 GLY B 238 1 11
HELIX 41 AE5 GLY B 247 ASN B 251 5 5
HELIX 42 AE6 THR B 264 THR B 272 1 9
HELIX 43 AE7 PRO B 275 GLU B 283 1 9
HELIX 44 AE8 ASN B 298 ALA B 307 1 10
HELIX 45 AE9 PHE B 316 SER B 328 1 13
HELIX 46 AF1 TRP B 331 THR B 336 1 6
HELIX 47 AF2 THR B 343 MET B 351 1 9
HELIX 48 AF3 ALA B 354 SER B 362 1 9
HELIX 49 AF4 LEU B 370 SER B 374 5 5
HELIX 50 AF5 SER B 402 TYR B 409 1 8
HELIX 51 AF6 ASN B 415 THR B 421 1 7
HELIX 52 AF7 LEU B 422 PHE B 436 1 15
HELIX 53 AF8 PHE B 436 TYR B 461 1 26
HELIX 54 AF9 TRP B 481 LEU B 507 1 27
HELIX 55 AG1 TRP B 521 PHE B 542 1 22
HELIX 56 AG2 GLU B 546 ASN B 561 1 16
HELIX 57 AG3 MET B 562 ARG B 567 5 6
HELIX 58 AG4 MET B 572 ILE B 583 1 12
HELIX 59 AG5 HIS B 585 ILE B 609 1 25
HELIX 60 AG6 SER B 624 THR B 636 1 13
HELIX 61 AG7 TYR B 650 VAL B 667 1 18
HELIX 62 AG8 LEU B 668 LEU B 707 1 40
HELIX 63 AG9 PRO B 708 PHE B 715 1 8
HELIX 64 AH1 LYS B 738 ASN B 750 1 13
HELIX 65 AH2 GLU C 111 GLY C 130 1 20
HELIX 66 AH3 VAL C 132 ARG C 149 1 18
HELIX 67 AH4 PRO C 155 THR C 163 1 9
HELIX 68 AH5 THR C 170 ASN C 178 1 9
HELIX 69 AH6 ASN C 182 ASP C 198 1 17
HELIX 70 AH7 ILE C 199 ASN C 205 1 7
HELIX 71 AH8 THR C 217 ARG C 225 1 9
HELIX 72 AH9 GLY C 228 GLY C 238 1 11
HELIX 73 AI1 GLY C 247 ASN C 251 5 5
HELIX 74 AI2 THR C 264 THR C 272 1 9
HELIX 75 AI3 PRO C 275 GLU C 283 1 9
HELIX 76 AI4 ASN C 298 ALA C 307 1 10
HELIX 77 AI5 PHE C 316 SER C 328 1 13
HELIX 78 AI6 TRP C 331 THR C 336 1 6
HELIX 79 AI7 THR C 343 MET C 351 1 9
HELIX 80 AI8 ALA C 354 SER C 362 1 9
HELIX 81 AI9 LEU C 370 SER C 374 5 5
HELIX 82 AJ1 SER C 402 TYR C 409 1 8
HELIX 83 AJ2 ASN C 415 THR C 421 1 7
HELIX 84 AJ3 LEU C 422 PHE C 436 1 15
HELIX 85 AJ4 PHE C 436 TYR C 461 1 26
HELIX 86 AJ5 TRP C 481 LEU C 507 1 27
HELIX 87 AJ6 TRP C 521 PHE C 542 1 22
HELIX 88 AJ7 GLU C 546 ASN C 561 1 16
HELIX 89 AJ8 MET C 562 ARG C 567 5 6
HELIX 90 AJ9 MET C 572 ILE C 583 1 12
HELIX 91 AK1 HIS C 585 ILE C 609 1 25
HELIX 92 AK2 SER C 624 THR C 636 1 13
HELIX 93 AK3 TYR C 650 VAL C 667 1 18
HELIX 94 AK4 LEU C 668 LEU C 707 1 40
HELIX 95 AK5 PRO C 708 PHE C 715 1 8
HELIX 96 AK6 LYS C 738 ASN C 750 1 13
HELIX 97 AK7 GLU D 111 GLY D 130 1 20
HELIX 98 AK8 VAL D 132 ARG D 149 1 18
HELIX 99 AK9 PRO D 155 THR D 163 1 9
HELIX 100 AL1 THR D 170 ASN D 178 1 9
HELIX 101 AL2 ASN D 182 ASP D 198 1 17
HELIX 102 AL3 ILE D 199 ASN D 205 1 7
HELIX 103 AL4 THR D 217 ARG D 225 1 9
HELIX 104 AL5 GLY D 228 GLY D 238 1 11
HELIX 105 AL6 GLY D 247 ASN D 251 5 5
HELIX 106 AL7 THR D 264 THR D 272 1 9
HELIX 107 AL8 PRO D 275 GLU D 283 1 9
HELIX 108 AL9 ASN D 298 ALA D 307 1 10
HELIX 109 AM1 PHE D 316 SER D 328 1 13
HELIX 110 AM2 TRP D 331 THR D 336 1 6
HELIX 111 AM3 THR D 343 MET D 351 1 9
HELIX 112 AM4 ALA D 354 SER D 362 1 9
HELIX 113 AM5 LEU D 370 SER D 374 5 5
HELIX 114 AM6 SER D 402 TYR D 409 1 8
HELIX 115 AM7 ASN D 415 THR D 421 1 7
HELIX 116 AM8 LEU D 422 PHE D 436 1 15
HELIX 117 AM9 PHE D 436 TYR D 461 1 26
HELIX 118 AN1 TRP D 481 LEU D 507 1 27
HELIX 119 AN2 TRP D 521 PHE D 542 1 22
HELIX 120 AN3 GLU D 546 ASN D 561 1 16
HELIX 121 AN4 MET D 562 ARG D 567 5 6
HELIX 122 AN5 MET D 572 ILE D 583 1 12
HELIX 123 AN6 HIS D 585 ILE D 609 1 25
HELIX 124 AN7 SER D 624 THR D 636 1 13
HELIX 125 AN8 TYR D 650 VAL D 667 1 18
HELIX 126 AN9 LEU D 668 LEU D 707 1 40
HELIX 127 AO1 PRO D 708 PHE D 715 1 8
HELIX 128 AO2 LYS D 738 ASN D 750 1 13
SHEET 1 AA1 4 PHE A 377 TYR A 382 0
SHEET 2 AA1 4 VAL A 385 TYR A 390 -1 O LEU A 389 N PHE A 377
SHEET 3 AA1 4 PHE A 728 GLU A 736 -1 O ILE A 734 N SER A 388
SHEET 4 AA1 4 GLU A 719 LYS A 722 -1 N GLU A 719 O CYS A 731
SHEET 1 AA2 4 PHE B 377 TYR B 382 0
SHEET 2 AA2 4 VAL B 385 TYR B 390 -1 O LEU B 389 N PHE B 377
SHEET 3 AA2 4 PHE B 728 GLU B 736 -1 O ILE B 734 N SER B 388
SHEET 4 AA2 4 GLU B 719 LYS B 722 -1 N GLU B 719 O CYS B 731
SHEET 1 AA3 4 PHE C 377 TYR C 382 0
SHEET 2 AA3 4 VAL C 385 TYR C 390 -1 O LEU C 389 N PHE C 377
SHEET 3 AA3 4 PHE C 728 GLU C 736 -1 O ILE C 734 N SER C 388
SHEET 4 AA3 4 GLU C 719 LYS C 722 -1 N GLU C 719 O CYS C 731
SHEET 1 AA4 4 PHE D 377 TYR D 382 0
SHEET 2 AA4 4 VAL D 385 TYR D 390 -1 O LEU D 389 N PHE D 377
SHEET 3 AA4 4 PHE D 728 GLU D 736 -1 O ILE D 734 N SER D 388
SHEET 4 AA4 4 GLU D 719 LYS D 722 -1 N GLU D 719 O CYS D 731
SSBOND 1 CYS A 721 CYS A 731 1555 1555 2.04
SSBOND 2 CYS B 721 CYS B 731 1555 1555 2.04
SSBOND 3 CYS C 721 CYS C 731 1555 1555 2.04
SSBOND 4 CYS D 721 CYS D 731 1555 1555 2.04
SITE 1 AC1 7 HIS A 417 LEU A 420 THR A 421 LEU A 422
SITE 2 AC1 7 HIS A 426 LEU A 429 ARG A 693
SITE 1 AC2 7 HIS B 417 LEU B 420 THR B 421 LEU B 422
SITE 2 AC2 7 HIS B 426 LEU B 429 ARG B 693
SITE 1 AC3 7 HIS C 417 LEU C 420 THR C 421 LEU C 422
SITE 2 AC3 7 HIS C 426 LEU C 429 ARG C 693
SITE 1 AC4 7 HIS D 417 LEU D 420 THR D 421 LEU D 422
SITE 2 AC4 7 HIS D 426 LEU D 429 ARG D 693
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
