HEADER VIRAL PROTEIN/IMMUNE SYSTEM 30-DEC-23 8VH1 TITLE CH235.12 FAB BOUND TO THE HIV-1 CH505.M5 SOSIP COMPND MOL_ID: 1; COMPND 2 MOLECULE: CH505.M5 SOSIP GP120; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CH505.M5 SOSIP GP41; COMPND 8 CHAIN: B, F, J; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: CH235.I60 FAB HEAVY CHAIN; COMPND 13 CHAIN: C, G, K; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: CH235.I60 FAB LIGHT CHAIN; COMPND 17 CHAIN: D, H, L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNOGEN, VACCINE, ANTIBODY, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.HENDERSON,P.ACHARYA REVDAT 1 02-OCT-24 8VH1 0 JRNL AUTH R.HENDERSON,B.F.HAYNES JRNL TITL ENGINEERING IMMUNOGENS THAT SELECT FOR SPECIFIC MUTATIONS IN JRNL TITL 2 HIV BROADLY NEUTRALIZING ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.08 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) : 4.080 REMARK 3 NUMBER OF PARTICLES : 21982 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 8VH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000280228. 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 : ANTIBODY FAB BOUND HIV-1 REMARK 245 ECTODOMAIN REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.10 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 : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 230.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4540.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5970.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L 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 ALA A 31 REMARK 465 LYS A 63 REMARK 465 LYS A 64 REMARK 465 VAL A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 VAL A 68 REMARK 465 TRP A 69 REMARK 465 ALA A 70 REMARK 465 SER A 399 REMARK 465 THR A 400 REMARK 465 ASP A 401 REMARK 465 MET A 402 REMARK 465 ALA A 403 REMARK 465 ASN A 404 REMARK 465 SER A 405 REMARK 465 THR A 406 REMARK 465 GLU A 407 REMARK 465 THR A 408 REMARK 465 VAL A 504 REMARK 465 GLY A 505 REMARK 465 ARG B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 THR B 569 REMARK 465 VAL B 570 REMARK 465 TRP B 571 REMARK 465 ALA E 31 REMARK 465 LYS E 63 REMARK 465 LYS E 64 REMARK 465 VAL E 65 REMARK 465 HIS E 66 REMARK 465 ASN E 67 REMARK 465 VAL E 68 REMARK 465 TRP E 69 REMARK 465 ALA E 70 REMARK 465 SER E 399 REMARK 465 THR E 400 REMARK 465 ASP E 401 REMARK 465 MET E 402 REMARK 465 ALA E 403 REMARK 465 ASN E 404 REMARK 465 SER E 405 REMARK 465 THR E 406 REMARK 465 GLU E 407 REMARK 465 THR E 408 REMARK 465 VAL E 504 REMARK 465 GLY E 505 REMARK 465 ARG F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 THR F 569 REMARK 465 VAL F 570 REMARK 465 TRP F 571 REMARK 465 ALA I 31 REMARK 465 LYS I 63 REMARK 465 LYS I 64 REMARK 465 VAL I 65 REMARK 465 HIS I 66 REMARK 465 ASN I 67 REMARK 465 VAL I 68 REMARK 465 TRP I 69 REMARK 465 ALA I 70 REMARK 465 SER I 399 REMARK 465 THR I 400 REMARK 465 ASP I 401 REMARK 465 MET I 402 REMARK 465 ALA I 403 REMARK 465 ASN I 404 REMARK 465 SER I 405 REMARK 465 THR I 406 REMARK 465 GLU I 407 REMARK 465 THR I 408 REMARK 465 VAL I 504 REMARK 465 GLY I 505 REMARK 465 ARG J 507 REMARK 465 ARG J 508 REMARK 465 ARG J 509 REMARK 465 ARG J 510 REMARK 465 ARG J 511 REMARK 465 ALA J 512 REMARK 465 VAL J 513 REMARK 465 GLY J 514 REMARK 465 ILE J 515 REMARK 465 GLY J 516 REMARK 465 ALA J 517 REMARK 465 GLY J 547 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 PRO J 559 REMARK 465 GLU J 560 REMARK 465 ALA J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 LEU J 566 REMARK 465 LYS J 567 REMARK 465 LEU J 568 REMARK 465 THR J 569 REMARK 465 VAL J 570 REMARK 465 TRP J 571 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 H ARG G 3 OG SER G 25 1.48 REMARK 500 H ARG C 3 OG SER C 25 1.51 REMARK 500 H ARG K 3 OG SER K 25 1.54 REMARK 500 OE1 GLU F 648 HD21 ASN F 651 1.54 REMARK 500 O SER F 612 HD21 ASN F 616 1.55 REMARK 500 HG SER A 199 O GLY A 431 1.55 REMARK 500 HG SER E 199 O GLY E 431 1.55 REMARK 500 HG SER I 199 O GLY I 431 1.55 REMARK 500 O PHE G 100E HH TYR H 36 1.55 REMARK 500 H ASN G 155 O ILE G 195 1.56 REMARK 500 OE1 GLN H 155 HD22 ASN H 158 1.56 REMARK 500 H ASN K 155 O ILE K 195 1.56 REMARK 500 H SER C 156 OD1 ASN C 197 1.56 REMARK 500 O PHE C 100E HH TYR D 36 1.56 REMARK 500 O GLY B 521 HE21 GLN B 540 1.57 REMARK 500 H ASN C 155 O ILE C 195 1.57 REMARK 500 HH12 ARG G 38 OD1 ASP G 86 1.57 REMARK 500 HD1 HIS E 249 OH TYR E 484 1.57 REMARK 500 HD1 HIS A 249 OH TYR A 484 1.57 REMARK 500 HD1 HIS I 249 OH TYR I 484 1.57 REMARK 500 OD1 ASP C 101 H TYR C 102 1.58 REMARK 500 O PHE K 100E HH TYR L 36 1.58 REMARK 500 OE1 GLU I 335 HE ARG I 412 1.58 REMARK 500 HG SER H 14 OE1 GLU H 17 1.58 REMARK 500 HD21 ASN C 197 OD1 ASP C 208 1.59 REMARK 500 OE1 GLU A 335 HE ARG A 412 1.59 REMARK 500 HZ1 LYS C 209 OE1 GLU D 123 1.59 REMARK 500 HD21 ASN G 197 OD1 ASP G 208 1.59 REMARK 500 OD1 ASP G 101 H TYR G 102 1.59 REMARK 500 HG SER L 14 OE1 GLU L 17 1.60 REMARK 500 OE1 GLN D 155 HD22 ASN D 158 1.60 REMARK 500 OD1 ASP K 101 H TYR K 102 1.60 REMARK 500 O HIS H 198 H LEU H 201 1.60 REMARK 500 O THR J 536 NE2 GLN J 540 2.00 REMARK 500 OG SER A 199 O GLY A 431 2.02 REMARK 500 O GLN H 124 OG SER H 127 2.05 REMARK 500 O SER G 188 OH TYR G 194 2.08 REMARK 500 OD1 ASP E 368 NH2 ARG G 71 2.09 REMARK 500 O ALA E 136 OG SER E 139 2.12 REMARK 500 OE2 GLU E 335 ND2 ASN E 339 2.13 REMARK 500 O ALA I 136 OG SER I 139 2.13 REMARK 500 OE1 GLU D 105 OH TYR D 173 2.15 REMARK 500 OE1 GLU H 105 OH TYR H 173 2.15 REMARK 500 O PHE G 100E OH TYR H 36 2.17 REMARK 500 OG SER I 199 O GLY I 431 2.17 REMARK 500 OG SER E 199 O GLY E 431 2.17 REMARK 500 N ARG G 3 OG SER G 25 2.18 REMARK 500 O PHE C 100E OH TYR D 36 2.19 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 ASP A 57 -179.08 -66.75 REMARK 500 CYS A 74 167.72 59.67 REMARK 500 PRO A 76 -164.36 -77.98 REMARK 500 ASP A 78 108.82 -48.07 REMARK 500 LYS A 87 -104.37 47.40 REMARK 500 ASN A 98 170.16 -58.30 REMARK 500 ALA A 134 10.68 -140.17 REMARK 500 GLU A 143 -109.89 45.90 REMARK 500 THR A 198 28.53 -141.44 REMARK 500 PRO A 212 69.59 -68.93 REMARK 500 GLN A 258 -17.80 72.10 REMARK 500 LEU A 259 137.68 -179.55 REMARK 500 HIS A 355 11.98 -144.82 REMARK 500 SER A 410 35.09 -143.81 REMARK 500 ARG A 412 131.13 66.22 REMARK 500 MET A 426 129.16 -37.83 REMARK 500 ALA A 433 139.91 -173.26 REMARK 500 MET A 473 -15.29 -49.91 REMARK 500 PRO A 491 2.80 -68.94 REMARK 500 LEU B 523 32.96 -140.83 REMARK 500 SER B 599 -143.64 58.29 REMARK 500 VAL B 608 137.12 61.39 REMARK 500 SER B 613 -164.78 -75.97 REMARK 500 TRP B 614 -110.71 66.54 REMARK 500 ALA C 9 -72.07 69.44 REMARK 500 GLU C 10 -144.61 31.37 REMARK 500 TYR C 27 164.64 179.57 REMARK 500 MET C 48 -64.30 -98.91 REMARK 500 ALA C 88 -177.74 -176.22 REMARK 500 PRO C 185 171.73 -53.33 REMARK 500 ASN C 204 14.23 59.75 REMARK 500 LYS C 214 69.11 60.50 REMARK 500 SER C 215 151.68 -48.47 REMARK 500 SER D 30 -99.98 50.81 REMARK 500 PRO D 44 156.46 -47.24 REMARK 500 SER D 63 142.57 -170.31 REMARK 500 ALA D 84 -164.49 -163.92 REMARK 500 TYR D 91 31.49 -140.18 REMARK 500 ASN D 93 -157.80 -151.42 REMARK 500 PRO D 141 -165.69 -78.72 REMARK 500 HIS D 198 143.76 -171.17 REMARK 500 ASP E 57 -169.89 -75.09 REMARK 500 CYS E 74 174.52 56.28 REMARK 500 LYS E 87 -105.60 46.72 REMARK 500 ASN E 98 170.27 -58.48 REMARK 500 ASN E 133 -4.51 74.90 REMARK 500 GLU E 143 -105.96 42.69 REMARK 500 THR E 198 24.60 -141.80 REMARK 500 PRO E 212 71.38 -69.04 REMARK 500 GLN E 258 -17.02 72.42 REMARK 500 REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43231 RELATED DB: EMDB REMARK 900 CH235.12 FAB BOUND TO THE HIV-1 CH505.M5 SOSIP DBREF 8VH1 A 34 504 UNP M4M0W3 M4M0W3_9HIV1 30 489 DBREF 8VH1 B 507 664 UNP M4M0W3 M4M0W3_9HIV1 490 647 DBREF 8VH1 C 1 216 PDB 8VH1 8VH1 1 216 DBREF 8VH1 D 1 212 PDB 8VH1 8VH1 1 212 DBREF 8VH1 E 34 504 UNP M4M0W3 M4M0W3_9HIV1 30 489 DBREF 8VH1 F 507 664 UNP M4M0W3 M4M0W3_9HIV1 490 647 DBREF 8VH1 G 1 216 PDB 8VH1 8VH1 1 216 DBREF 8VH1 H 1 212 PDB 8VH1 8VH1 1 212 DBREF 8VH1 I 34 504 UNP M4M0W3 M4M0W3_9HIV1 30 489 DBREF 8VH1 J 507 664 UNP M4M0W3 M4M0W3_9HIV1 490 647 DBREF 8VH1 K 1 216 PDB 8VH1 8VH1 1 216 DBREF 8VH1 L 1 212 PDB 8VH1 8VH1 1 212 SEQADV 8VH1 ALA A 31 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 GLU A 32 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ASN A 33 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 LEU A 34 UNP M4M0W3 MET 30 CONFLICT SEQADV 8VH1 LYS A 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 8VH1 LYS A 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 8VH1 ILE A 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 8VH1 GLU A 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 8VH1 ARG A 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 8VH1 CYS A 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 8VH1 LYS A 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 8VH1 GLY A 505 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ARG B 507 UNP M4M0W3 GLU 490 CONFLICT SEQADV 8VH1 ARG B 509 UNP M4M0W3 GLU 492 CONFLICT SEQADV 8VH1 ARG B 510 UNP M4M0W3 LYS 493 CONFLICT SEQADV 8VH1 ILE B 515 UNP M4M0W3 MET 498 CONFLICT SEQADV 8VH1 MET B 535 UNP M4M0W3 ILE 518 CONFLICT SEQADV 8VH1 ASN B 543 UNP M4M0W3 GLN 526 CONFLICT SEQADV 8VH1 ARG B 557 UNP M4M0W3 LYS 540 CONFLICT SEQADV 8VH1 PRO B 559 UNP M4M0W3 ILE 542 CONFLICT SEQADV 8VH1 LEU B 565 UNP M4M0W3 MET 548 CONFLICT SEQADV 8VH1 VAL B 583 UNP M4M0W3 LEU 566 CONFLICT SEQADV 8VH1 ARG B 588 UNP M4M0W3 LYS 571 CONFLICT SEQADV 8VH1 ILE B 595 UNP M4M0W3 MET 578 CONFLICT SEQADV 8VH1 CYS B 605 UNP M4M0W3 THR 588 CONFLICT SEQADV 8VH1 PRO B 609 UNP M4M0W3 TYR 592 CONFLICT SEQADV 8VH1 ARG B 617 UNP M4M0W3 LYS 600 CONFLICT SEQADV 8VH1 ASN B 618 UNP M4M0W3 THR 601 CONFLICT SEQADV 8VH1 LEU B 619 UNP M4M0W3 TYR 602 CONFLICT SEQADV 8VH1 SER B 620 UNP M4M0W3 GLY 603 CONFLICT SEQADV 8VH1 GLU B 621 UNP M4M0W3 ASP 604 CONFLICT SEQADV 8VH1 LEU B 629 UNP M4M0W3 MET 612 CONFLICT SEQADV 8VH1 ASP B 632 UNP M4M0W3 GLU 615 CONFLICT SEQADV 8VH1 LYS B 633 UNP M4M0W3 ARG 616 CONFLICT SEQADV 8VH1 GLN B 640 UNP M4M0W3 GLU 623 CONFLICT SEQADV 8VH1 GLY B 644 UNP M4M0W3 GLU 627 CONFLICT SEQADV 8VH1 ALA E 31 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 GLU E 32 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ASN E 33 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 LEU E 34 UNP M4M0W3 MET 30 CONFLICT SEQADV 8VH1 LYS E 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 8VH1 LYS E 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 8VH1 ILE E 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 8VH1 GLU E 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 8VH1 ARG E 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 8VH1 CYS E 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 8VH1 LYS E 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 8VH1 GLY E 505 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ARG F 507 UNP M4M0W3 GLU 490 CONFLICT SEQADV 8VH1 ARG F 509 UNP M4M0W3 GLU 492 CONFLICT SEQADV 8VH1 ARG F 510 UNP M4M0W3 LYS 493 CONFLICT SEQADV 8VH1 ILE F 515 UNP M4M0W3 MET 498 CONFLICT SEQADV 8VH1 MET F 535 UNP M4M0W3 ILE 518 CONFLICT SEQADV 8VH1 ASN F 543 UNP M4M0W3 GLN 526 CONFLICT SEQADV 8VH1 ARG F 557 UNP M4M0W3 LYS 540 CONFLICT SEQADV 8VH1 PRO F 559 UNP M4M0W3 ILE 542 CONFLICT SEQADV 8VH1 LEU F 565 UNP M4M0W3 MET 548 CONFLICT SEQADV 8VH1 VAL F 583 UNP M4M0W3 LEU 566 CONFLICT SEQADV 8VH1 ARG F 588 UNP M4M0W3 LYS 571 CONFLICT SEQADV 8VH1 ILE F 595 UNP M4M0W3 MET 578 CONFLICT SEQADV 8VH1 CYS F 605 UNP M4M0W3 THR 588 CONFLICT SEQADV 8VH1 PRO F 609 UNP M4M0W3 TYR 592 CONFLICT SEQADV 8VH1 ARG F 617 UNP M4M0W3 LYS 600 CONFLICT SEQADV 8VH1 ASN F 618 UNP M4M0W3 THR 601 CONFLICT SEQADV 8VH1 LEU F 619 UNP M4M0W3 TYR 602 CONFLICT SEQADV 8VH1 SER F 620 UNP M4M0W3 GLY 603 CONFLICT SEQADV 8VH1 GLU F 621 UNP M4M0W3 ASP 604 CONFLICT SEQADV 8VH1 LEU F 629 UNP M4M0W3 MET 612 CONFLICT SEQADV 8VH1 ASP F 632 UNP M4M0W3 GLU 615 CONFLICT SEQADV 8VH1 LYS F 633 UNP M4M0W3 ARG 616 CONFLICT SEQADV 8VH1 GLN F 640 UNP M4M0W3 GLU 623 CONFLICT SEQADV 8VH1 GLY F 644 UNP M4M0W3 GLU 627 CONFLICT SEQADV 8VH1 ALA I 31 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 GLU I 32 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ASN I 33 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 LEU I 34 UNP M4M0W3 MET 30 CONFLICT SEQADV 8VH1 LYS I 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 8VH1 LYS I 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 8VH1 ILE I 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 8VH1 GLU I 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 8VH1 ARG I 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 8VH1 CYS I 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 8VH1 LYS I 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 8VH1 GLY I 505 UNP M4M0W3 EXPRESSION TAG SEQADV 8VH1 ARG J 507 UNP M4M0W3 GLU 490 CONFLICT SEQADV 8VH1 ARG J 509 UNP M4M0W3 GLU 492 CONFLICT SEQADV 8VH1 ARG J 510 UNP M4M0W3 LYS 493 CONFLICT SEQADV 8VH1 ILE J 515 UNP M4M0W3 MET 498 CONFLICT SEQADV 8VH1 MET J 535 UNP M4M0W3 ILE 518 CONFLICT SEQADV 8VH1 ASN J 543 UNP M4M0W3 GLN 526 CONFLICT SEQADV 8VH1 ARG J 557 UNP M4M0W3 LYS 540 CONFLICT SEQADV 8VH1 PRO J 559 UNP M4M0W3 ILE 542 CONFLICT SEQADV 8VH1 LEU J 565 UNP M4M0W3 MET 548 CONFLICT SEQADV 8VH1 VAL J 583 UNP M4M0W3 LEU 566 CONFLICT SEQADV 8VH1 ARG J 588 UNP M4M0W3 LYS 571 CONFLICT SEQADV 8VH1 ILE J 595 UNP M4M0W3 MET 578 CONFLICT SEQADV 8VH1 CYS J 605 UNP M4M0W3 THR 588 CONFLICT SEQADV 8VH1 PRO J 609 UNP M4M0W3 TYR 592 CONFLICT SEQADV 8VH1 ARG J 617 UNP M4M0W3 LYS 600 CONFLICT SEQADV 8VH1 ASN J 618 UNP M4M0W3 THR 601 CONFLICT SEQADV 8VH1 LEU J 619 UNP M4M0W3 TYR 602 CONFLICT SEQADV 8VH1 SER J 620 UNP M4M0W3 GLY 603 CONFLICT SEQADV 8VH1 GLU J 621 UNP M4M0W3 ASP 604 CONFLICT SEQADV 8VH1 LEU J 629 UNP M4M0W3 MET 612 CONFLICT SEQADV 8VH1 ASP J 632 UNP M4M0W3 GLU 615 CONFLICT SEQADV 8VH1 LYS J 633 UNP M4M0W3 ARG 616 CONFLICT SEQADV 8VH1 GLN J 640 UNP M4M0W3 GLU 623 CONFLICT SEQADV 8VH1 GLY J 644 UNP M4M0W3 GLU 627 CONFLICT SEQRES 1 A 464 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 464 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 A 464 ASP ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP SEQRES 4 A 464 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 464 GLU MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 A 464 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL SEQRES 7 A 464 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 464 LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA SEQRES 9 A 464 THR ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN SEQRES 10 A 464 CYS SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG SEQRES 11 A 464 GLU LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL SEQRES 12 A 464 GLN LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN SEQRES 13 A 464 CYS ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 A 464 SER PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 A 464 GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR SEQRES 16 A 464 GLY THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS SEQRES 17 A 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 A 464 LEU ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SEQRES 19 A 464 SER GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL SEQRES 20 A 464 HIS LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO SEQRES 21 A 464 ASN ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY SEQRES 22 A 464 GLN ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE SEQRES 23 A 464 ARG GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN SEQRES 24 A 464 GLU THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR SEQRES 25 A 464 PHE PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY SEQRES 26 A 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 A 464 GLY GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN SEQRES 28 A 464 ARG THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER SEQRES 29 A 464 THR GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS SEQRES 30 A 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY SEQRES 31 A 464 ARG ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR SEQRES 32 A 464 CYS ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 A 464 GLY GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY SEQRES 34 A 464 GLY ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 A 464 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 A 464 THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 1 B 158 ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA VAL PHE SEQRES 2 B 158 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 3 B 158 ALA SER MET THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 4 B 158 SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU ARG ALA SEQRES 5 B 158 PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR VAL TRP SEQRES 6 B 158 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 7 B 158 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 8 B 158 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 9 B 158 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 10 B 158 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 11 B 158 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 12 B 158 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 13 B 158 LEU ASP SEQRES 1 C 220 GLN VAL ARG LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 C 220 PRO GLY ALA SER VAL THR VAL SER CYS LYS ALA SER GLY SEQRES 3 C 220 TYR THR PHE THR ASN TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 C 220 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASP SEQRES 5 C 220 PRO SER VAL GLY SER THR ASN TYR ALA GLN LYS TYR GLN SEQRES 6 C 220 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 C 220 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 C 220 ALA VAL TYR TYR CYS VAL ARG ASP VAL GLY THR GLU GLY SEQRES 9 C 220 SER LEU LEU HIS PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 C 220 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 220 PHE PRO LEU ALA PRO SER SER GLY THR ALA ALA LEU GLY SEQRES 12 C 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 C 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 C 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 C 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 C 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 C 220 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 D 211 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 D 211 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 211 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 211 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 D 211 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 D 211 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER MET SEQRES 7 D 211 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS HIS GLN TYR SEQRES 8 D 211 ASN ASN TRP TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 D 211 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 D 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 D 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 D 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 D 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 D 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 D 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 D 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 D 211 ASN ARG GLY SEQRES 1 E 464 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 464 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 E 464 ASP ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP SEQRES 4 E 464 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 464 GLU MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 E 464 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL SEQRES 7 E 464 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 464 LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA SEQRES 9 E 464 THR ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN SEQRES 10 E 464 CYS SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG SEQRES 11 E 464 GLU LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL SEQRES 12 E 464 GLN LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN SEQRES 13 E 464 CYS ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 E 464 SER PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 E 464 GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR SEQRES 16 E 464 GLY THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS SEQRES 17 E 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 E 464 LEU ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SEQRES 19 E 464 SER GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL SEQRES 20 E 464 HIS LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO SEQRES 21 E 464 ASN ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY SEQRES 22 E 464 GLN ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE SEQRES 23 E 464 ARG GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN SEQRES 24 E 464 GLU THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR SEQRES 25 E 464 PHE PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY SEQRES 26 E 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 E 464 GLY GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN SEQRES 28 E 464 ARG THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER SEQRES 29 E 464 THR GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS SEQRES 30 E 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY SEQRES 31 E 464 ARG ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR SEQRES 32 E 464 CYS ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 E 464 GLY GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY SEQRES 34 E 464 GLY ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 E 464 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 E 464 THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 1 F 158 ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA VAL PHE SEQRES 2 F 158 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 3 F 158 ALA SER MET THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 4 F 158 SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU ARG ALA SEQRES 5 F 158 PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR VAL TRP SEQRES 6 F 158 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 7 F 158 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 8 F 158 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 9 F 158 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 10 F 158 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 11 F 158 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 12 F 158 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 13 F 158 LEU ASP SEQRES 1 G 220 GLN VAL ARG LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 G 220 PRO GLY ALA SER VAL THR VAL SER CYS LYS ALA SER GLY SEQRES 3 G 220 TYR THR PHE THR ASN TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 G 220 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASP SEQRES 5 G 220 PRO SER VAL GLY SER THR ASN TYR ALA GLN LYS TYR GLN SEQRES 6 G 220 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 G 220 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 G 220 ALA VAL TYR TYR CYS VAL ARG ASP VAL GLY THR GLU GLY SEQRES 9 G 220 SER LEU LEU HIS PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 G 220 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 G 220 PHE PRO LEU ALA PRO SER SER GLY THR ALA ALA LEU GLY SEQRES 12 G 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 G 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 G 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 G 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 G 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 G 220 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 H 211 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 H 211 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 H 211 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 H 211 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 H 211 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 H 211 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER MET SEQRES 7 H 211 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS HIS GLN TYR SEQRES 8 H 211 ASN ASN TRP TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 H 211 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 H 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 H 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 H 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 H 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 H 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 H 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 H 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 H 211 ASN ARG GLY SEQRES 1 I 464 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 I 464 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 I 464 ASP ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP SEQRES 4 I 464 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 I 464 GLU MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 I 464 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL SEQRES 7 I 464 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 I 464 LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA SEQRES 9 I 464 THR ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN SEQRES 10 I 464 CYS SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG SEQRES 11 I 464 GLU LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL SEQRES 12 I 464 GLN LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN SEQRES 13 I 464 CYS ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 I 464 SER PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA SEQRES 15 I 464 GLY TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR SEQRES 16 I 464 GLY THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS SEQRES 17 I 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 I 464 LEU ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SEQRES 19 I 464 SER GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL SEQRES 20 I 464 HIS LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO SEQRES 21 I 464 ASN ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY SEQRES 22 I 464 GLN ALA PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE SEQRES 23 I 464 ARG GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN SEQRES 24 I 464 GLU THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR SEQRES 25 I 464 PHE PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY SEQRES 26 I 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 I 464 GLY GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN SEQRES 28 I 464 ARG THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER SEQRES 29 I 464 THR GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS SEQRES 30 I 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY SEQRES 31 I 464 ARG ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR SEQRES 32 I 464 CYS ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 I 464 GLY GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY SEQRES 34 I 464 GLY ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 35 I 464 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 36 I 464 THR ARG CYS LYS ARG ARG VAL VAL GLY SEQRES 1 J 158 ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA VAL PHE SEQRES 2 J 158 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 3 J 158 ALA SER MET THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 4 J 158 SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU ARG ALA SEQRES 5 J 158 PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR VAL TRP SEQRES 6 J 158 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 7 J 158 ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 8 J 158 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 9 J 158 ASN SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP SEQRES 10 J 158 ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER SEQRES 11 J 158 ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER SEQRES 12 J 158 GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA SEQRES 13 J 158 LEU ASP SEQRES 1 K 220 GLN VAL ARG LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 220 PRO GLY ALA SER VAL THR VAL SER CYS LYS ALA SER GLY SEQRES 3 K 220 TYR THR PHE THR ASN TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 K 220 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASP SEQRES 5 K 220 PRO SER VAL GLY SER THR ASN TYR ALA GLN LYS TYR GLN SEQRES 6 K 220 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 K 220 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 K 220 ALA VAL TYR TYR CYS VAL ARG ASP VAL GLY THR GLU GLY SEQRES 9 K 220 SER LEU LEU HIS PHE ASP TYR TRP GLY GLN GLY THR LEU SEQRES 10 K 220 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 K 220 PHE PRO LEU ALA PRO SER SER GLY THR ALA ALA LEU GLY SEQRES 12 K 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 K 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 K 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 K 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 K 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 K 220 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 L 211 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 211 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 211 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 211 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 211 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 211 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER MET SEQRES 7 L 211 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS HIS GLN TYR SEQRES 8 L 211 ASN ASN TRP TRP THR PHE GLY GLN GLY THR LYS VAL GLU SEQRES 9 L 211 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 211 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 211 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 211 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 211 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 211 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 211 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 211 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 211 ASN ARG GLY HELIX 1 AA1 ASP A 99 LYS A 117 1 19 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 ASN A 195 THR A 198 5 4 HELIX 4 AA4 GLU A 335 LYS A 350 1 16 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 MET A 473 SER A 479 1 7 HELIX 7 AA7 GLY B 531 MET B 535 5 5 HELIX 8 AA8 THR B 536 ALA B 541 1 6 HELIX 9 AA9 ILE B 573 GLY B 597 1 25 HELIX 10 AB1 LEU B 619 TRP B 623 5 5 HELIX 11 AB2 TRP B 628 SER B 636 1 9 HELIX 12 AB3 TYR B 638 ALA B 662 1 25 HELIX 13 AB4 THR C 28 TYR C 32 5 5 HELIX 14 AB5 ARG C 83 THR C 87 5 5 HELIX 15 AB6 SER D 121 GLY D 128 1 8 HELIX 16 AB7 ALA D 184 HIS D 189 1 6 HELIX 17 AB8 ASP E 99 LYS E 117 1 19 HELIX 18 AB9 LEU E 122 CYS E 126 5 5 HELIX 19 AC1 ASN E 195 THR E 198 5 4 HELIX 20 AC2 GLU E 335 LYS E 350 1 16 HELIX 21 AC3 ASP E 368 THR E 373 1 6 HELIX 22 AC4 MET E 473 SER E 479 1 7 HELIX 23 AC5 GLY F 531 MET F 535 5 5 HELIX 24 AC6 THR F 536 ALA F 541 1 6 HELIX 25 AC7 ILE F 573 TRP F 596 1 24 HELIX 26 AC8 THR F 627 SER F 636 1 10 HELIX 27 AC9 TYR F 638 ALA F 662 1 25 HELIX 28 AD1 THR G 28 TYR G 32 5 5 HELIX 29 AD2 ARG G 83 THR G 87 5 5 HELIX 30 AD3 SER H 121 LYS H 126 1 6 HELIX 31 AD4 ALA H 184 HIS H 189 1 6 HELIX 32 AD5 ASP I 99 LYS I 117 1 19 HELIX 33 AD6 LEU I 122 CYS I 126 5 5 HELIX 34 AD7 ASN I 195 THR I 198 5 4 HELIX 35 AD8 GLU I 335 LYS I 350 1 16 HELIX 36 AD9 ASP I 368 THR I 373 1 6 HELIX 37 AE1 MET I 473 SER I 479 1 7 HELIX 38 AE2 THR J 536 ASN J 543 1 8 HELIX 39 AE3 ILE J 573 TRP J 596 1 24 HELIX 40 AE4 THR J 627 SER J 636 1 10 HELIX 41 AE5 TYR J 638 ALA J 662 1 25 HELIX 42 AE6 THR K 28 TYR K 32 5 5 HELIX 43 AE7 ARG K 83 THR K 87 5 5 HELIX 44 AE8 GLN L 79 PHE L 83 5 5 HELIX 45 AE9 SER L 121 LYS L 126 1 6 HELIX 46 AF1 SER L 182 HIS L 189 1 8 SHEET 1 AA1 3 GLY A 493 THR A 497 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TRP A 35 O THR A 497 SHEET 3 AA1 3 ILE B 603 CYS B 604 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 GLU A 47 0 SHEET 2 AA2 5 TYR A 484 ILE A 489 -1 O LYS A 488 N LYS A 46 SHEET 3 AA2 5 TYR A 223 CYS A 228 -1 N ALA A 224 O VAL A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 5 AA2 5 MET A 84 VAL A 85 -1 N MET A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 3 LEU A 129 ASN A 130 0 SHEET 2 AA4 3 GLN A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 3 AA4 3 ILE A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA5 2 SER A 158 THR A 162 0 SHEET 2 AA5 2 ARG A 169 ASN A 173 -1 O GLU A 170 N ILE A 161 SHEET 1 AA6 3 THR A 202 GLN A 203 0 SHEET 2 AA6 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA7 7 LEU A 260 LEU A 261 0 SHEET 2 AA7 7 ILE A 443 ASP A 457 -1 O THR A 450 N LEU A 260 SHEET 3 AA7 7 ILE A 284 ARG A 298 -1 N ILE A 284 O LEU A 454 SHEET 4 AA7 7 TYR A 330 ASN A 334 -1 O TYR A 330 N THR A 297 SHEET 5 AA7 7 THR A 413 ILE A 420 -1 O ILE A 414 N ILE A 333 SHEET 6 AA7 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA7 7 HIS A 374 CYS A 378 -1 N CYS A 378 O GLU A 381 SHEET 1 AA8 6 ILE A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 284 ARG A 298 -1 O ILE A 285 N ARG A 273 SHEET 3 AA8 6 ILE A 443 ASP A 457 -1 O LEU A 454 N ILE A 284 SHEET 4 AA8 6 THR A 463 PRO A 468 -1 O THR A 465 N ASP A 457 SHEET 5 AA8 6 ASN A 357 PHE A 361 1 N THR A 359 O GLU A 464 SHEET 6 AA8 6 THR A 394 TYR A 395 -1 O TYR A 395 N ILE A 358 SHEET 1 AA9 2 ARG A 304 ARG A 308 0 SHEET 2 AA9 2 ALA A 316 THR A 320 -1 O ALA A 319 N THR A 305 SHEET 1 AB1 4 LEU C 4 SER C 7 0 SHEET 2 AB1 4 VAL C 18 ALA C 24 -1 O LYS C 23 N VAL C 5 SHEET 3 AB1 4 THR C 77 LEU C 82 -1 O LEU C 82 N VAL C 18 SHEET 4 AB1 4 VAL C 67 ASP C 72 -1 N THR C 68 O GLU C 81 SHEET 1 AB2 5 THR C 57 TYR C 59 0 SHEET 2 AB2 5 LEU C 45 ILE C 51 -1 N TRP C 50 O ASN C 58 SHEET 3 AB2 5 TYR C 33 GLN C 39 -1 N TRP C 36 O MET C 48 SHEET 4 AB2 5 ALA C 88 ASP C 95 -1 O VAL C 93 N HIS C 35 SHEET 5 AB2 5 PHE C 100E TRP C 103 -1 O TYR C 102 N ARG C 94 SHEET 1 AB3 5 THR C 57 TYR C 59 0 SHEET 2 AB3 5 LEU C 45 ILE C 51 -1 N TRP C 50 O ASN C 58 SHEET 3 AB3 5 TYR C 33 GLN C 39 -1 N TRP C 36 O MET C 48 SHEET 4 AB3 5 ALA C 88 ASP C 95 -1 O VAL C 93 N HIS C 35 SHEET 5 AB3 5 THR C 107 VAL C 109 -1 O THR C 107 N TYR C 90 SHEET 1 AB4 4 SER C 120 PHE C 122 0 SHEET 2 AB4 4 THR C 135 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AB4 4 LEU C 175 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AB4 4 HIS C 164 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AB5 4 SER C 120 PHE C 122 0 SHEET 2 AB5 4 THR C 135 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AB5 4 LEU C 175 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AB5 4 VAL C 169 GLN C 171 -1 N VAL C 169 O SER C 177 SHEET 1 AB6 3 THR C 151 TRP C 154 0 SHEET 2 AB6 3 CYS C 196 ASN C 199 -1 O ASN C 197 N SER C 153 SHEET 3 AB6 3 LYS C 206 LYS C 209 -1 O LYS C 209 N CYS C 196 SHEET 1 AB7 4 MET D 4 SER D 7 0 SHEET 2 AB7 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB7 4 GLU D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AB7 4 PHE D 62 SER D 67 -1 N SER D 65 O THR D 72 SHEET 1 AB8 5 THR D 10 VAL D 13 0 SHEET 2 AB8 5 THR D 102 ILE D 106 1 O GLU D 105 N VAL D 13 SHEET 3 AB8 5 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AB8 5 LEU D 33 GLN D 38 -1 N ALA D 34 O HIS D 89 SHEET 5 AB8 5 ARG D 45 ILE D 48 -1 O ARG D 45 N GLN D 37 SHEET 1 AB9 4 THR D 10 VAL D 13 0 SHEET 2 AB9 4 THR D 102 ILE D 106 1 O GLU D 105 N VAL D 13 SHEET 3 AB9 4 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AB9 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC1 4 SER D 114 PHE D 118 0 SHEET 2 AC1 4 SER D 131 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AC1 4 TYR D 173 THR D 180 -1 O LEU D 179 N VAL D 132 SHEET 4 AC1 4 SER D 159 GLN D 160 -1 N GLN D 160 O THR D 178 SHEET 1 AC2 4 ALA D 153 LEU D 154 0 SHEET 2 AC2 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC2 4 VAL D 191 THR D 197 -1 O THR D 197 N LYS D 145 SHEET 4 AC2 4 VAL D 205 ASN D 210 -1 O PHE D 209 N TYR D 192 SHEET 1 AC3 3 GLY E 493 THR E 497 0 SHEET 2 AC3 3 TRP E 35 TYR E 39 -1 N TYR E 39 O GLY E 493 SHEET 3 AC3 3 ILE F 603 CYS F 604 -1 O CYS F 604 N VAL E 38 SHEET 1 AC4 5 TRP E 45 GLU E 47 0 SHEET 2 AC4 5 TYR E 484 ILE E 489 -1 O LYS E 488 N LYS E 46 SHEET 3 AC4 5 TYR E 223 CYS E 228 -1 N ALA E 224 O VAL E 487 SHEET 4 AC4 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC4 5 GLU E 83 VAL E 85 -1 N MET E 84 O THR E 244 SHEET 1 AC5 2 PHE E 53 ALA E 55 0 SHEET 2 AC5 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC6 3 LEU E 129 ASN E 130 0 SHEET 2 AC6 3 GLN E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 3 AC6 3 ILE E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC7 2 SER E 158 THR E 162 0 SHEET 2 AC7 2 ARG E 169 ASN E 173 -1 O GLU E 170 N ILE E 161 SHEET 1 AC8 3 THR E 202 GLN E 203 0 SHEET 2 AC8 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC8 3 ILE E 423 ILE E 424 -1 O ILE E 424 N MET E 434 SHEET 1 AC9 7 LEU E 260 LEU E 261 0 SHEET 2 AC9 7 ILE E 443 ASP E 457 -1 O THR E 450 N LEU E 260 SHEET 3 AC9 7 ILE E 284 ARG E 298 -1 N ILE E 284 O LEU E 454 SHEET 4 AC9 7 TYR E 330 ASN E 334 -1 O TYR E 330 N THR E 297 SHEET 5 AC9 7 THR E 413 ILE E 420 -1 O ILE E 414 N ILE E 333 SHEET 6 AC9 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC9 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AD1 6 ILE E 271 ARG E 273 0 SHEET 2 AD1 6 ILE E 284 ARG E 298 -1 O ILE E 285 N ARG E 273 SHEET 3 AD1 6 ILE E 443 ASP E 457 -1 O LEU E 454 N ILE E 284 SHEET 4 AD1 6 THR E 463 PRO E 468 -1 O THR E 465 N ASP E 457 SHEET 5 AD1 6 ASN E 357 PHE E 361 1 N THR E 359 O GLU E 464 SHEET 6 AD1 6 THR E 394 TYR E 395 -1 O TYR E 395 N ILE E 358 SHEET 1 AD2 2 ARG E 304 ILE E 309 0 SHEET 2 AD2 2 GLN E 315 THR E 320 -1 O ALA E 319 N THR E 305 SHEET 1 AD3 4 LEU G 4 SER G 7 0 SHEET 2 AD3 4 VAL G 18 ALA G 24 -1 O LYS G 23 N VAL G 5 SHEET 3 AD3 4 THR G 77 LEU G 82 -1 O LEU G 82 N VAL G 18 SHEET 4 AD3 4 VAL G 67 ASP G 72 -1 N THR G 70 O TYR G 79 SHEET 1 AD4 5 THR G 57 TYR G 59 0 SHEET 2 AD4 5 LEU G 45 ILE G 51 -1 N TRP G 50 O ASN G 58 SHEET 3 AD4 5 TYR G 33 GLN G 39 -1 N ILE G 34 O ILE G 51 SHEET 4 AD4 5 ALA G 88 ASP G 95 -1 O VAL G 93 N HIS G 35 SHEET 5 AD4 5 PHE G 100E TRP G 103 -1 O TYR G 102 N ARG G 94 SHEET 1 AD5 5 THR G 57 TYR G 59 0 SHEET 2 AD5 5 LEU G 45 ILE G 51 -1 N TRP G 50 O ASN G 58 SHEET 3 AD5 5 TYR G 33 GLN G 39 -1 N ILE G 34 O ILE G 51 SHEET 4 AD5 5 ALA G 88 ASP G 95 -1 O VAL G 93 N HIS G 35 SHEET 5 AD5 5 THR G 107 VAL G 109 -1 O THR G 107 N TYR G 90 SHEET 1 AD6 4 SER G 120 PHE G 122 0 SHEET 2 AD6 4 THR G 135 TYR G 145 -1 O LYS G 143 N SER G 120 SHEET 3 AD6 4 LEU G 175 PRO G 185 -1 O VAL G 184 N ALA G 136 SHEET 4 AD6 4 HIS G 164 THR G 165 -1 N HIS G 164 O VAL G 181 SHEET 1 AD7 4 SER G 120 PHE G 122 0 SHEET 2 AD7 4 THR G 135 TYR G 145 -1 O LYS G 143 N SER G 120 SHEET 3 AD7 4 LEU G 175 PRO G 185 -1 O VAL G 184 N ALA G 136 SHEET 4 AD7 4 VAL G 169 GLN G 171 -1 N VAL G 169 O SER G 177 SHEET 1 AD8 3 THR G 151 TRP G 154 0 SHEET 2 AD8 3 CYS G 196 ASN G 199 -1 O ASN G 197 N SER G 153 SHEET 3 AD8 3 LYS G 206 LYS G 209 -1 O LYS G 209 N CYS G 196 SHEET 1 AD9 4 MET H 4 SER H 7 0 SHEET 2 AD9 4 ALA H 19 ALA H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AD9 4 GLU H 70 ILE H 75 -1 O PHE H 71 N CYS H 23 SHEET 4 AD9 4 PHE H 62 SER H 67 -1 N SER H 65 O THR H 72 SHEET 1 AE1 5 THR H 10 VAL H 13 0 SHEET 2 AE1 5 THR H 102 ILE H 106 1 O GLU H 105 N VAL H 13 SHEET 3 AE1 5 VAL H 85 GLN H 90 -1 N TYR H 86 O THR H 102 SHEET 4 AE1 5 LEU H 33 GLN H 38 -1 N GLN H 38 O VAL H 85 SHEET 5 AE1 5 ARG H 45 ILE H 48 -1 O ARG H 45 N GLN H 37 SHEET 1 AE2 4 SER H 114 PHE H 118 0 SHEET 2 AE2 4 SER H 131 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 AE2 4 THR H 178 THR H 180 -1 O LEU H 179 N VAL H 132 SHEET 4 AE2 4 SER H 159 GLN H 160 -1 N GLN H 160 O THR H 178 SHEET 1 AE3 3 SER H 114 PHE H 118 0 SHEET 2 AE3 3 SER H 131 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 AE3 3 TYR H 173 LEU H 175 -1 O TYR H 173 N PHE H 139 SHEET 1 AE4 4 ALA H 153 LEU H 154 0 SHEET 2 AE4 4 LYS H 145 VAL H 150 -1 N VAL H 150 O ALA H 153 SHEET 3 AE4 4 VAL H 191 THR H 197 -1 O THR H 197 N LYS H 145 SHEET 4 AE4 4 VAL H 205 ASN H 210 -1 O PHE H 209 N TYR H 192 SHEET 1 AE5 3 GLY I 493 THR I 497 0 SHEET 2 AE5 3 TRP I 35 TYR I 39 -1 N TRP I 35 O THR I 497 SHEET 3 AE5 3 ILE J 603 CYS J 604 -1 O CYS J 604 N VAL I 38 SHEET 1 AE6 5 TRP I 45 GLU I 47 0 SHEET 2 AE6 5 TYR I 484 ILE I 489 -1 O LYS I 488 N LYS I 46 SHEET 3 AE6 5 TYR I 223 CYS I 228 -1 N ALA I 224 O VAL I 487 SHEET 4 AE6 5 VAL I 242 VAL I 245 -1 O VAL I 245 N ILE I 225 SHEET 5 AE6 5 MET I 84 VAL I 85 -1 N MET I 84 O THR I 244 SHEET 1 AE7 2 PHE I 53 ALA I 55 0 SHEET 2 AE7 2 HIS I 216 CYS I 218 -1 O HIS I 216 N ALA I 55 SHEET 1 AE8 3 LEU I 129 ASN I 130 0 SHEET 2 AE8 3 GLN I 190 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 3 AE8 3 ILE I 181 GLN I 183 -1 N VAL I 182 O ARG I 192 SHEET 1 AE9 2 SER I 158 THR I 162 0 SHEET 2 AE9 2 ARG I 169 ASN I 173 -1 O GLU I 170 N ILE I 161 SHEET 1 AF1 3 THR I 202 GLN I 203 0 SHEET 2 AF1 3 MET I 434 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AF1 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AF2 7 LEU I 260 LEU I 261 0 SHEET 2 AF2 7 ILE I 443 ASP I 457 -1 O THR I 450 N LEU I 260 SHEET 3 AF2 7 ILE I 284 ARG I 298 -1 N ILE I 284 O LEU I 454 SHEET 4 AF2 7 TYR I 330 ASN I 334 -1 O TYR I 330 N THR I 297 SHEET 5 AF2 7 THR I 413 ILE I 420 -1 O ILE I 414 N ILE I 333 SHEET 6 AF2 7 GLU I 381 CYS I 385 -1 N TYR I 384 O ARG I 419 SHEET 7 AF2 7 HIS I 374 CYS I 378 -1 N HIS I 374 O CYS I 385 SHEET 1 AF3 6 ILE I 271 SER I 274 0 SHEET 2 AF3 6 ILE I 284 ARG I 298 -1 O ILE I 285 N ARG I 273 SHEET 3 AF3 6 ILE I 443 ASP I 457 -1 O LEU I 454 N ILE I 284 SHEET 4 AF3 6 THR I 463 PRO I 468 -1 O THR I 465 N ASP I 457 SHEET 5 AF3 6 ASN I 357 PHE I 361 1 N THR I 359 O GLU I 464 SHEET 6 AF3 6 THR I 394 TYR I 395 -1 O TYR I 395 N ILE I 358 SHEET 1 AF4 2 ARG I 304 ARG I 308 0 SHEET 2 AF4 2 ALA I 316 THR I 320 -1 O ALA I 319 N THR I 305 SHEET 1 AF5 4 GLN K 6 SER K 7 0 SHEET 2 AF5 4 VAL K 18 LYS K 23 -1 O SER K 21 N SER K 7 SHEET 3 AF5 4 THR K 77 LEU K 82 -1 O LEU K 82 N VAL K 18 SHEET 4 AF5 4 VAL K 67 ASP K 72 -1 N ASP K 72 O THR K 77 SHEET 1 AF6 6 VAL K 11 LYS K 12 0 SHEET 2 AF6 6 THR K 107 VAL K 111 1 O THR K 110 N LYS K 12 SHEET 3 AF6 6 ALA K 88 ASP K 95 -1 N TYR K 90 O THR K 107 SHEET 4 AF6 6 TYR K 33 GLN K 39 -1 N HIS K 35 O VAL K 93 SHEET 5 AF6 6 LEU K 45 ILE K 51 -1 O MET K 48 N TRP K 36 SHEET 6 AF6 6 THR K 57 TYR K 59 -1 O ASN K 58 N TRP K 50 SHEET 1 AF7 4 VAL K 11 LYS K 12 0 SHEET 2 AF7 4 THR K 107 VAL K 111 1 O THR K 110 N LYS K 12 SHEET 3 AF7 4 ALA K 88 ASP K 95 -1 N TYR K 90 O THR K 107 SHEET 4 AF7 4 PHE K 100E TRP K 103 -1 O TYR K 102 N ARG K 94 SHEET 1 AF8 4 SER K 120 PHE K 122 0 SHEET 2 AF8 4 THR K 135 TYR K 145 -1 O LYS K 143 N SER K 120 SHEET 3 AF8 4 LEU K 175 PRO K 185 -1 O VAL K 184 N ALA K 136 SHEET 4 AF8 4 HIS K 164 THR K 165 -1 N HIS K 164 O VAL K 181 SHEET 1 AF9 4 SER K 120 PHE K 122 0 SHEET 2 AF9 4 THR K 135 TYR K 145 -1 O LYS K 143 N SER K 120 SHEET 3 AF9 4 LEU K 175 PRO K 185 -1 O VAL K 184 N ALA K 136 SHEET 4 AF9 4 VAL K 169 GLN K 171 -1 N GLN K 171 O LEU K 175 SHEET 1 AG1 3 THR K 151 TRP K 154 0 SHEET 2 AG1 3 CYS K 196 ASN K 199 -1 O ASN K 197 N SER K 153 SHEET 3 AG1 3 LYS K 206 LYS K 209 -1 O LYS K 209 N CYS K 196 SHEET 1 AG2 4 MET L 4 SER L 7 0 SHEET 2 AG2 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AG2 4 GLU L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AG2 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AG3 5 THR L 10 VAL L 13 0 SHEET 2 AG3 5 THR L 102 ILE L 106 1 O GLU L 105 N VAL L 13 SHEET 3 AG3 5 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AG3 5 LEU L 33 GLN L 38 -1 N ALA L 34 O HIS L 89 SHEET 5 AG3 5 ARG L 45 ILE L 48 -1 O ARG L 45 N GLN L 37 SHEET 1 AG4 4 THR L 10 VAL L 13 0 SHEET 2 AG4 4 THR L 102 ILE L 106 1 O GLU L 105 N VAL L 13 SHEET 3 AG4 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AG4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AG5 4 SER L 114 PHE L 118 0 SHEET 2 AG5 4 SER L 131 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AG5 4 THR L 178 THR L 180 -1 O LEU L 179 N VAL L 132 SHEET 4 AG5 4 SER L 159 GLN L 160 -1 N GLN L 160 O THR L 178 SHEET 1 AG6 3 SER L 114 PHE L 118 0 SHEET 2 AG6 3 SER L 131 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AG6 3 TYR L 173 LEU L 175 -1 O TYR L 173 N PHE L 139 SHEET 1 AG7 4 ALA L 153 LEU L 154 0 SHEET 2 AG7 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AG7 4 VAL L 191 THR L 197 -1 O THR L 197 N LYS L 145 SHEET 4 AG7 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS A 499 CYS B 605 1555 1555 2.03 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 13 CYS C 140 CYS C 196 1555 1555 2.03 SSBOND 14 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 15 CYS D 134 CYS D 194 1555 1555 2.03 SSBOND 16 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 17 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 18 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 19 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 20 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 21 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 22 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 23 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 24 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 25 CYS E 499 CYS F 605 1555 1555 2.03 SSBOND 26 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 27 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 28 CYS G 140 CYS G 196 1555 1555 2.03 SSBOND 29 CYS H 23 CYS H 88 1555 1555 2.04 SSBOND 30 CYS H 134 CYS H 194 1555 1555 2.03 SSBOND 31 CYS I 54 CYS I 74 1555 1555 2.04 SSBOND 32 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 33 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 34 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 35 CYS I 218 CYS I 247 1555 1555 2.03 SSBOND 36 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 37 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 38 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 39 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 40 CYS I 499 CYS J 605 1555 1555 2.03 SSBOND 41 CYS J 598 CYS J 604 1555 1555 2.03 SSBOND 42 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 43 CYS K 140 CYS K 196 1555 1555 2.03 SSBOND 44 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 45 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 VAL A 75 PRO A 76 0 3.28 CISPEP 2 GLY A 312 PRO A 313 0 2.08 CISPEP 3 PHE C 146 PRO C 147 0 -6.53 CISPEP 4 GLU C 148 PRO C 149 0 2.67 CISPEP 5 SER D 7 PRO D 8 0 -10.41 CISPEP 6 TYR D 140 PRO D 141 0 -9.09 CISPEP 7 VAL E 75 PRO E 76 0 1.56 CISPEP 8 GLY E 312 PRO E 313 0 3.03 CISPEP 9 PHE G 146 PRO G 147 0 -7.13 CISPEP 10 GLU G 148 PRO G 149 0 0.84 CISPEP 11 SER H 7 PRO H 8 0 -10.10 CISPEP 12 TYR H 140 PRO H 141 0 -8.80 CISPEP 13 VAL I 75 PRO I 76 0 3.62 CISPEP 14 GLY I 312 PRO I 313 0 2.19 CISPEP 15 PHE K 146 PRO K 147 0 -6.43 CISPEP 16 GLU K 148 PRO K 149 0 1.68 CISPEP 17 SER L 7 PRO L 8 0 -9.70 CISPEP 18 TYR L 140 PRO L 141 0 -8.94 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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