HEADER VIRAL PROTEIN/IMMUNE SYSTEM 29-DEC-23 8VGW TITLE VRC01 FAB BOUND TO THE HIV-1 CH848 DE3 SOSIP COMPND MOL_ID: 1; COMPND 2 MOLECULE: CH848 DE3 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: CH848 DE3 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: VRC01 FAB HEAVY CHAIN; COMPND 13 CHAIN: C, G, K; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: VRC01 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 8VGW 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. 3.90 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) : 3.900 REMARK 3 NUMBER OF PARTICLES : 220881 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 8VGW 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_1000280212. 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) : 420.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 4710.00 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) : 6000.00 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 SER A 361 REMARK 465 THR A 362 REMARK 465 ASN A 363 REMARK 465 SER A 364 REMARK 465 SER A 365 REMARK 465 ALA A 366 REMARK 465 ASN A 367 REMARK 465 SER A 368 REMARK 465 THR A 369 REMARK 465 SER A 370 REMARK 465 GLN B 510 REMARK 465 GLN B 511 REMARK 465 GLN B 512 REMARK 465 SER B 513 REMARK 465 ASN B 514 REMARK 465 LEU B 515 REMARK 465 LEU B 516 REMARK 465 ARG B 517 REMARK 465 ALA B 518 REMARK 465 ILE B 519 REMARK 465 GLU B 520 REMARK 465 ALA B 521 REMARK 465 GLN B 522 REMARK 465 GLN B 523 REMARK 465 HIS B 524 REMARK 465 MET B 525 REMARK 465 LEU B 526 REMARK 465 SER E 361 REMARK 465 THR E 362 REMARK 465 ASN E 363 REMARK 465 SER E 364 REMARK 465 SER E 365 REMARK 465 ALA E 366 REMARK 465 ASN E 367 REMARK 465 SER E 368 REMARK 465 THR E 369 REMARK 465 SER E 370 REMARK 465 GLN F 510 REMARK 465 GLN F 511 REMARK 465 GLN F 512 REMARK 465 SER F 513 REMARK 465 ASN F 514 REMARK 465 LEU F 515 REMARK 465 LEU F 516 REMARK 465 ARG F 517 REMARK 465 ALA F 518 REMARK 465 ILE F 519 REMARK 465 GLU F 520 REMARK 465 ALA F 521 REMARK 465 GLN F 522 REMARK 465 GLN F 523 REMARK 465 HIS F 524 REMARK 465 MET F 525 REMARK 465 LEU F 526 REMARK 465 SER I 361 REMARK 465 THR I 362 REMARK 465 ASN I 363 REMARK 465 SER I 364 REMARK 465 SER I 365 REMARK 465 ALA I 366 REMARK 465 ASN I 367 REMARK 465 SER I 368 REMARK 465 THR I 369 REMARK 465 SER I 370 REMARK 465 GLN J 510 REMARK 465 GLN J 511 REMARK 465 GLN J 512 REMARK 465 SER J 513 REMARK 465 ASN J 514 REMARK 465 LEU J 515 REMARK 465 LEU J 516 REMARK 465 ARG J 517 REMARK 465 ALA J 518 REMARK 465 ILE J 519 REMARK 465 GLU J 520 REMARK 465 ALA J 521 REMARK 465 GLN J 522 REMARK 465 GLN J 523 REMARK 465 HIS J 524 REMARK 465 MET J 525 REMARK 465 LEU J 526 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 OG1 THR I 259 O ILE I 401 2.04 REMARK 500 OG1 THR E 259 O ILE E 401 2.05 REMARK 500 O GLY L 51 OH TYR L 71 2.10 REMARK 500 O GLY H 51 OH TYR H 71 2.10 REMARK 500 OH TYR E 10 O GLY E 453 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS E 258 CA - CB - SG ANGL. DEV. = 9.8 DEGREES REMARK 500 CYS I 258 CA - CB - SG ANGL. DEV. = 9.6 DEGREES 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 ALA A 28 -151.96 58.20 REMARK 500 THR A 41 -163.32 -78.92 REMARK 500 HIS A 211 -179.93 -69.89 REMARK 500 GLN A 220 -10.41 73.73 REMARK 500 ALA A 243 -164.77 -77.48 REMARK 500 LYS A 244 -177.30 67.75 REMARK 500 GLN A 289 145.33 68.91 REMARK 500 CYS A 338 112.94 -160.08 REMARK 500 ASN A 349 15.60 -141.74 REMARK 500 LEU A 350 43.38 -91.20 REMARK 500 PHE A 351 -17.08 -146.17 REMARK 500 LEU A 452 -158.68 -85.66 REMARK 500 ARG A 469 -152.94 -90.28 REMARK 500 ALA B 477 -152.15 46.69 REMARK 500 LEU B 480 46.53 -89.95 REMARK 500 ASN B 578 26.61 -143.21 REMARK 500 ASN B 616 55.16 -91.21 REMARK 500 ASP B 619 -68.39 -94.71 REMARK 500 LEU B 620 -51.83 -127.55 REMARK 500 ALA C 60 -69.45 -97.10 REMARK 500 PRO C 62 -5.59 -53.93 REMARK 500 VAL D 47 -61.92 -101.86 REMARK 500 GLN D 90 -162.73 -124.97 REMARK 500 ALA E 28 -152.17 58.26 REMARK 500 THR E 41 -162.92 -79.14 REMARK 500 THR E 98 97.90 -68.58 REMARK 500 GLN E 220 -10.48 73.70 REMARK 500 ALA E 243 -164.82 -76.92 REMARK 500 LYS E 244 -167.95 66.80 REMARK 500 GLN E 289 144.93 68.89 REMARK 500 ASN E 349 15.86 -141.26 REMARK 500 LEU E 350 43.20 -91.12 REMARK 500 PHE E 351 -17.06 -146.52 REMARK 500 ILE F 475 -57.84 -131.16 REMARK 500 ALA F 477 -145.83 47.82 REMARK 500 LEU F 480 48.92 -87.97 REMARK 500 LEU F 505 -60.10 -94.68 REMARK 500 ASN F 578 24.22 -145.66 REMARK 500 ASP F 619 -102.88 80.63 REMARK 500 ALA G 60 -66.55 -96.39 REMARK 500 PRO G 62 -7.79 -52.24 REMARK 500 VAL H 47 -62.35 -107.51 REMARK 500 ALA I 28 -152.79 57.99 REMARK 500 TRP I 39 -6.54 79.01 REMARK 500 THR I 41 -162.67 -78.32 REMARK 500 THR I 98 97.47 -68.38 REMARK 500 LYS I 138 141.05 -170.77 REMARK 500 HIS I 211 -179.50 -69.84 REMARK 500 GLN I 220 -11.30 74.25 REMARK 500 ALA I 243 -164.51 -77.30 REMARK 500 REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 TYR A 10 GLY A 11 -146.07 REMARK 500 VAL A 38 TRP A 39 -146.95 REMARK 500 PHE A 351 ASN A 352 -148.95 REMARK 500 TYR E 9 TYR E 10 -140.94 REMARK 500 TYR E 10 GLY E 11 136.42 REMARK 500 VAL E 38 TRP E 39 -146.90 REMARK 500 PHE E 351 ASN E 352 -148.98 REMARK 500 PRO E 451 LEU E 452 -143.92 REMARK 500 ASP F 619 LEU F 620 -144.92 REMARK 500 VAL I 38 TRP I 39 -149.26 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43228 RELATED DB: EMDB REMARK 900 VRC01 FAB BOUND TO THE HIV-1 CH848 DE3 SOSIP DBREF1 8VGW A 4 469 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW A A0A1W6IPB2 30 495 DBREF1 8VGW B 472 624 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW B A0A1W6IPB2 496 648 DBREF 8VGW C 1 113 PDB 8VGW 8VGW 1 113 DBREF 8VGW D 1 107 PDB 8VGW 8VGW 1 107 DBREF1 8VGW E 4 469 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW E A0A1W6IPB2 30 495 DBREF1 8VGW F 472 624 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW F A0A1W6IPB2 496 648 DBREF 8VGW G 1 113 PDB 8VGW 8VGW 1 113 DBREF 8VGW H 1 107 PDB 8VGW 8VGW 1 107 DBREF1 8VGW I 4 469 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW I A0A1W6IPB2 30 495 DBREF1 8VGW J 472 624 UNP A0A1W6IPB2_9HIV1 DBREF2 8VGW J A0A1W6IPB2 496 648 DBREF 8VGW K 1 113 PDB 8VGW 8VGW 1 113 DBREF 8VGW L 1 107 PDB 8VGW 8VGW 1 107 SEQADV 8VGW ALA A 1 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW GLU A 2 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ASN A 3 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW CYS A 163 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGW CYS A 391 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGW LYS A 448 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGW GLU A 450 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGW VAL A 454 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGW ARG A 458 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGW CYS A 459 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGW GLY A 465 UNP A0A1W6IPB GLU 491 CONFLICT SEQADV 8VGW ARG A 467 UNP A0A1W6IPB GLU 493 CONFLICT SEQADV 8VGW ARG A 468 UNP A0A1W6IPB LYS 494 CONFLICT SEQADV 8VGW ARG A 470 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ARG A 471 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW VAL B 473 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGW ILE B 475 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGW VAL B 478 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGW MET B 495 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGW ASN B 503 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGW LYS B 527 UNP A0A1W6IPB GLN 551 CONFLICT SEQADV 8VGW VAL B 543 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGW ARG B 548 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGW ILE B 555 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGW CYS B 565 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGW SER B 572 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGW ARG B 577 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGW ASN B 578 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGW LEU B 579 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGW SER B 580 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGW GLU B 581 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGW LEU B 589 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGW ASP B 592 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGW LYS B 593 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGW GLN B 600 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGW ILE B 601 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGW GLY B 604 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGW GLU B 608 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGW LYS B 615 UNP A0A1W6IPB ARG 639 CONFLICT SEQADV 8VGW ALA E 1 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW GLU E 2 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ASN E 3 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW CYS E 163 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGW CYS E 391 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGW LYS E 448 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGW GLU E 450 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGW VAL E 454 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGW ARG E 458 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGW CYS E 459 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGW GLY E 465 UNP A0A1W6IPB GLU 491 CONFLICT SEQADV 8VGW ARG E 467 UNP A0A1W6IPB GLU 493 CONFLICT SEQADV 8VGW ARG E 468 UNP A0A1W6IPB LYS 494 CONFLICT SEQADV 8VGW ARG E 470 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ARG E 471 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW VAL F 473 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGW ILE F 475 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGW VAL F 478 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGW MET F 495 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGW ASN F 503 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGW LYS F 527 UNP A0A1W6IPB GLN 551 CONFLICT SEQADV 8VGW VAL F 543 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGW ARG F 548 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGW ILE F 555 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGW CYS F 565 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGW SER F 572 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGW ARG F 577 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGW ASN F 578 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGW LEU F 579 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGW SER F 580 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGW GLU F 581 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGW LEU F 589 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGW ASP F 592 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGW LYS F 593 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGW GLN F 600 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGW ILE F 601 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGW GLY F 604 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGW GLU F 608 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGW LYS F 615 UNP A0A1W6IPB ARG 639 CONFLICT SEQADV 8VGW ALA I 1 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW GLU I 2 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ASN I 3 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW CYS I 163 UNP A0A1W6IPB VAL 189 CONFLICT SEQADV 8VGW CYS I 391 UNP A0A1W6IPB ALA 417 CONFLICT SEQADV 8VGW LYS I 448 UNP A0A1W6IPB GLU 474 CONFLICT SEQADV 8VGW GLU I 450 UNP A0A1W6IPB GLN 476 CONFLICT SEQADV 8VGW VAL I 454 UNP A0A1W6IPB ILE 480 CONFLICT SEQADV 8VGW ARG I 458 UNP A0A1W6IPB GLY 484 CONFLICT SEQADV 8VGW CYS I 459 UNP A0A1W6IPB ALA 485 CONFLICT SEQADV 8VGW GLY I 465 UNP A0A1W6IPB GLU 491 CONFLICT SEQADV 8VGW ARG I 467 UNP A0A1W6IPB GLU 493 CONFLICT SEQADV 8VGW ARG I 468 UNP A0A1W6IPB LYS 494 CONFLICT SEQADV 8VGW ARG I 470 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW ARG I 471 UNP A0A1W6IPB EXPRESSION TAG SEQADV 8VGW VAL J 473 UNP A0A1W6IPB ALA 497 CONFLICT SEQADV 8VGW ILE J 475 UNP A0A1W6IPB LEU 499 CONFLICT SEQADV 8VGW VAL J 478 UNP A0A1W6IPB LEU 502 CONFLICT SEQADV 8VGW MET J 495 UNP A0A1W6IPB ILE 519 CONFLICT SEQADV 8VGW ASN J 503 UNP A0A1W6IPB GLN 527 CONFLICT SEQADV 8VGW LYS J 527 UNP A0A1W6IPB GLN 551 CONFLICT SEQADV 8VGW VAL J 543 UNP A0A1W6IPB LEU 567 CONFLICT SEQADV 8VGW ARG J 548 UNP A0A1W6IPB LYS 572 CONFLICT SEQADV 8VGW ILE J 555 UNP A0A1W6IPB MET 579 CONFLICT SEQADV 8VGW CYS J 565 UNP A0A1W6IPB THR 589 CONFLICT SEQADV 8VGW SER J 572 UNP A0A1W6IPB THR 596 CONFLICT SEQADV 8VGW ARG J 577 UNP A0A1W6IPB LYS 601 CONFLICT SEQADV 8VGW ASN J 578 UNP A0A1W6IPB SER 602 CONFLICT SEQADV 8VGW LEU J 579 UNP A0A1W6IPB GLU 603 CONFLICT SEQADV 8VGW SER J 580 UNP A0A1W6IPB THR 604 CONFLICT SEQADV 8VGW GLU J 581 UNP A0A1W6IPB ASP 605 CONFLICT SEQADV 8VGW LEU J 589 UNP A0A1W6IPB MET 613 CONFLICT SEQADV 8VGW ASP J 592 UNP A0A1W6IPB GLU 616 CONFLICT SEQADV 8VGW LYS J 593 UNP A0A1W6IPB ARG 617 CONFLICT SEQADV 8VGW GLN J 600 UNP A0A1W6IPB GLU 624 CONFLICT SEQADV 8VGW ILE J 601 UNP A0A1W6IPB THR 625 CONFLICT SEQADV 8VGW GLY J 604 UNP A0A1W6IPB LYS 628 CONFLICT SEQADV 8VGW GLU J 608 UNP A0A1W6IPB ASP 632 CONFLICT SEQADV 8VGW LYS J 615 UNP A0A1W6IPB ARG 639 CONFLICT SEQRES 1 A 471 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 471 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 A 471 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 A 471 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 A 471 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 A 471 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 A 471 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 471 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 A 471 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 A 471 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 A 471 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 A 471 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 A 471 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 A 471 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 A 471 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 A 471 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 A 471 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 A 471 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 A 471 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 A 471 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 A 471 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 A 471 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 A 471 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 A 471 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 A 471 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 A 471 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 A 471 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 A 471 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 A 471 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 A 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 A 471 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 A 471 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 A 471 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 A 471 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 A 471 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 A 471 PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG SEQRES 37 A 471 ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 B 153 HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 121 GLN VAL GLN LEU VAL GLN SER GLY GLY GLN MET LYS LYS SEQRES 2 C 121 PRO GLY GLU SER MET ARG ILE SER CYS ARG ALA SER GLY SEQRES 3 C 121 TYR GLU PHE ILE ASP CYS THR LEU ASN TRP ILE ARG LEU SEQRES 4 C 121 ALA PRO GLY LYS ARG PRO GLU TRP MET GLY TRP LEU LYS SEQRES 5 C 121 PRO ARG GLY GLY ALA VAL ASN TYR ALA ARG PRO LEU GLN SEQRES 6 C 121 GLY ARG VAL THR MET THR ARG ASP VAL TYR SER ASP THR SEQRES 7 C 121 ALA PHE LEU GLU LEU ARG SER LEU THR VAL ASP ASP THR SEQRES 8 C 121 ALA VAL TYR PHE CYS THR ARG GLY LYS ASN CYS ASP TYR SEQRES 9 C 121 ASN TRP ASP PHE GLU HIS TRP GLY ARG GLY THR PRO VAL SEQRES 10 C 121 ILE VAL SER SER SEQRES 1 D 101 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 D 101 SER PRO GLY GLU THR ALA ILE ILE SER CYS ARG THR SER SEQRES 3 D 101 GLN TYR GLY SER LEU ALA TRP TYR GLN GLN ARG PRO GLY SEQRES 4 D 101 GLN ALA PRO ARG LEU VAL ILE TYR SER GLY SER THR ARG SEQRES 5 D 101 ALA ALA GLY ILE PRO ASP ARG PHE SER GLY SER ARG TRP SEQRES 6 D 101 GLY PRO ASP TYR ASN LEU THR ILE SER ASN LEU GLU SER SEQRES 7 D 101 GLY ASP PHE GLY VAL TYR TYR CYS GLN GLN TYR GLU PHE SEQRES 8 D 101 PHE GLY GLN GLY THR LYS VAL GLN VAL ASP SEQRES 1 E 471 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 471 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 E 471 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 E 471 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 E 471 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 E 471 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 E 471 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 471 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 E 471 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 E 471 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 E 471 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 E 471 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 E 471 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 E 471 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 E 471 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 E 471 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 E 471 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 E 471 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 E 471 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 E 471 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 E 471 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 E 471 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 E 471 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 E 471 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 E 471 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 E 471 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 E 471 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 E 471 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 E 471 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 E 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 E 471 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 E 471 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 E 471 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 E 471 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 E 471 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 E 471 PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG SEQRES 37 E 471 ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 F 153 HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 121 GLN VAL GLN LEU VAL GLN SER GLY GLY GLN MET LYS LYS SEQRES 2 G 121 PRO GLY GLU SER MET ARG ILE SER CYS ARG ALA SER GLY SEQRES 3 G 121 TYR GLU PHE ILE ASP CYS THR LEU ASN TRP ILE ARG LEU SEQRES 4 G 121 ALA PRO GLY LYS ARG PRO GLU TRP MET GLY TRP LEU LYS SEQRES 5 G 121 PRO ARG GLY GLY ALA VAL ASN TYR ALA ARG PRO LEU GLN SEQRES 6 G 121 GLY ARG VAL THR MET THR ARG ASP VAL TYR SER ASP THR SEQRES 7 G 121 ALA PHE LEU GLU LEU ARG SER LEU THR VAL ASP ASP THR SEQRES 8 G 121 ALA VAL TYR PHE CYS THR ARG GLY LYS ASN CYS ASP TYR SEQRES 9 G 121 ASN TRP ASP PHE GLU HIS TRP GLY ARG GLY THR PRO VAL SEQRES 10 G 121 ILE VAL SER SER SEQRES 1 H 101 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 H 101 SER PRO GLY GLU THR ALA ILE ILE SER CYS ARG THR SER SEQRES 3 H 101 GLN TYR GLY SER LEU ALA TRP TYR GLN GLN ARG PRO GLY SEQRES 4 H 101 GLN ALA PRO ARG LEU VAL ILE TYR SER GLY SER THR ARG SEQRES 5 H 101 ALA ALA GLY ILE PRO ASP ARG PHE SER GLY SER ARG TRP SEQRES 6 H 101 GLY PRO ASP TYR ASN LEU THR ILE SER ASN LEU GLU SER SEQRES 7 H 101 GLY ASP PHE GLY VAL TYR TYR CYS GLN GLN TYR GLU PHE SEQRES 8 H 101 PHE GLY GLN GLY THR LYS VAL GLN VAL ASP SEQRES 1 I 471 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 I 471 VAL TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER SEQRES 3 I 471 ASP ALA ARG ALA TYR GLU LYS GLU VAL HIS ASN VAL TRP SEQRES 4 I 471 ALA THR HIS ALA CYS VAL PRO THR ASP PRO SER PRO GLN SEQRES 5 I 471 GLU LEU VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET SEQRES 6 I 471 TRP LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP ILE SEQRES 7 I 471 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 I 471 LEU THR PRO LEU CYS VAL THR LEU ILE CYS SER ASN ALA SEQRES 9 I 471 THR VAL LYS ASN GLY THR VAL GLU GLU MET LYS ASN CYS SEQRES 10 I 471 SER PHE ASN THR THR THR GLU ILE ARG ASP LYS GLU LYS SEQRES 11 I 471 LYS GLU TYR ALA LEU PHE TYR LYS PRO ASP ILE VAL PRO SEQRES 12 I 471 LEU SER GLU THR ASN ASN THR SER GLU TYR ARG LEU ILE SEQRES 13 I 471 ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO LYS SEQRES 14 I 471 VAL THR PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 I 471 ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP GLU THR PHE SEQRES 16 I 471 ASN GLY THR GLY PRO CYS SER ASN VAL SER THR VAL GLN SEQRES 17 I 471 CYS THR HIS GLY ILE ARG PRO VAL VAL SER THR GLN LEU SEQRES 18 I 471 LEU LEU ASN GLY SER LEU ALA GLU LYS GLU ILE VAL ILE SEQRES 19 I 471 ARG SER GLU ASN LEU THR ASN ASN ALA LYS ILE ILE ILE SEQRES 20 I 471 VAL HIS LEU HIS THR PRO VAL GLU ILE VAL CYS THR ARG SEQRES 21 I 471 PRO ASN ASN ASN THR ARG LYS SER VAL ARG ILE GLY PRO SEQRES 22 I 471 GLY GLN THR PHE TYR ALA THR GLY ASP ILE ILE GLY ASP SEQRES 23 I 471 ILE LYS GLN ALA HIS CYS ASN ILE SER GLU GLU LYS TRP SEQRES 24 I 471 ASN ASP THR LEU GLN LYS VAL GLY ILE GLU LEU GLN LYS SEQRES 25 I 471 HIS PHE PRO ASN LYS THR ILE LYS TYR ASN GLN SER ALA SEQRES 26 I 471 GLY GLY ASP MET GLU ILE THR THR HIS SER PHE ASN CYS SEQRES 27 I 471 GLY GLY GLU PHE PHE TYR CYS ASN THR SER ASN LEU PHE SEQRES 28 I 471 ASN GLY THR TYR ASN GLY THR TYR ILE SER THR ASN SER SEQRES 29 I 471 SER ALA ASN SER THR SER THR ILE THR LEU GLN CYS ARG SEQRES 30 I 471 ILE LYS GLN ILE ILE ASN MET TRP GLN GLY VAL GLY ARG SEQRES 31 I 471 CYS MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 I 471 ARG SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 I 471 GLY THR ASN SER ASN GLU THR GLU THR PHE ARG PRO ALA SEQRES 34 I 471 GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR SEQRES 35 I 471 LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA SEQRES 36 I 471 PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG SEQRES 37 I 471 ARG ARG ARG SEQRES 1 J 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 J 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 J 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 J 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 J 153 HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 J 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 J 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 J 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 J 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 J 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 J 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 J 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 K 121 GLN VAL GLN LEU VAL GLN SER GLY GLY GLN MET LYS LYS SEQRES 2 K 121 PRO GLY GLU SER MET ARG ILE SER CYS ARG ALA SER GLY SEQRES 3 K 121 TYR GLU PHE ILE ASP CYS THR LEU ASN TRP ILE ARG LEU SEQRES 4 K 121 ALA PRO GLY LYS ARG PRO GLU TRP MET GLY TRP LEU LYS SEQRES 5 K 121 PRO ARG GLY GLY ALA VAL ASN TYR ALA ARG PRO LEU GLN SEQRES 6 K 121 GLY ARG VAL THR MET THR ARG ASP VAL TYR SER ASP THR SEQRES 7 K 121 ALA PHE LEU GLU LEU ARG SER LEU THR VAL ASP ASP THR SEQRES 8 K 121 ALA VAL TYR PHE CYS THR ARG GLY LYS ASN CYS ASP TYR SEQRES 9 K 121 ASN TRP ASP PHE GLU HIS TRP GLY ARG GLY THR PRO VAL SEQRES 10 K 121 ILE VAL SER SER SEQRES 1 L 101 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 101 SER PRO GLY GLU THR ALA ILE ILE SER CYS ARG THR SER SEQRES 3 L 101 GLN TYR GLY SER LEU ALA TRP TYR GLN GLN ARG PRO GLY SEQRES 4 L 101 GLN ALA PRO ARG LEU VAL ILE TYR SER GLY SER THR ARG SEQRES 5 L 101 ALA ALA GLY ILE PRO ASP ARG PHE SER GLY SER ARG TRP SEQRES 6 L 101 GLY PRO ASP TYR ASN LEU THR ILE SER ASN LEU GLU SER SEQRES 7 L 101 GLY ASP PHE GLY VAL TYR TYR CYS GLN GLN TYR GLU PHE SEQRES 8 L 101 PHE GLY GLN GLY THR LYS VAL GLN VAL ASP HELIX 1 AA1 ARG A 29 VAL A 35 1 7 HELIX 2 AA2 ASN A 68 LYS A 87 1 20 HELIX 3 AA3 LEU A 92 CYS A 96 5 5 HELIX 4 AA4 SER A 295 PHE A 314 1 20 HELIX 5 AA5 ASP A 328 THR A 333 1 6 HELIX 6 AA6 MET A 433 ARG A 438 1 6 HELIX 7 AA7 VAL B 478 LEU B 483 1 6 HELIX 8 AA8 GLY B 484 GLY B 487 5 4 HELIX 9 AA9 GLY B 491 MET B 495 5 5 HELIX 10 AB1 LEU B 497 LEU B 504 1 8 HELIX 11 AB2 THR B 529 GLY B 557 1 29 HELIX 12 AB3 ASN B 578 ILE B 582 5 5 HELIX 13 AB4 THR B 587 ASP B 592 1 6 HELIX 14 AB5 LYS B 593 ILE B 595 5 3 HELIX 15 AB6 TYR B 598 ASN B 616 1 19 HELIX 16 AB7 LEU B 620 ASP B 624 5 5 HELIX 17 AB8 ARG C 61 GLY C 65 5 5 HELIX 18 AB9 VAL C 73 SER C 75 5 3 HELIX 19 AC1 THR C 83 THR C 87 5 5 HELIX 20 AC2 GLU D 79 PHE D 83 5 5 HELIX 21 AC3 ARG E 29 VAL E 35 1 7 HELIX 22 AC4 ASN E 68 LEU E 86 1 19 HELIX 23 AC5 LEU E 92 CYS E 96 5 5 HELIX 24 AC6 SER E 295 PHE E 314 1 20 HELIX 25 AC7 MET E 433 ARG E 438 1 6 HELIX 26 AC8 SER E 439 TYR E 442 5 4 HELIX 27 AC9 ARG E 462 ARG E 466 5 5 HELIX 28 AD1 VAL F 478 LEU F 483 1 6 HELIX 29 AD2 GLY F 484 GLY F 487 5 4 HELIX 30 AD3 THR F 489 SER F 494 1 6 HELIX 31 AD4 LEU F 497 LEU F 504 1 8 HELIX 32 AD5 THR F 529 GLY F 557 1 29 HELIX 33 AD6 ASN F 578 TRP F 583 1 6 HELIX 34 AD7 THR F 587 ASP F 592 1 6 HELIX 35 AD8 TYR F 598 ASN F 616 1 19 HELIX 36 AD9 ARG G 61 GLY G 65 5 5 HELIX 37 AE1 VAL G 73 SER G 75 5 3 HELIX 38 AE2 THR G 83 THR G 87 5 5 HELIX 39 AE3 ARG I 29 VAL I 35 1 7 HELIX 40 AE4 MET I 70 LYS I 87 1 18 HELIX 41 AE5 LEU I 92 CYS I 96 5 5 HELIX 42 AE6 SER I 295 PHE I 314 1 20 HELIX 43 AE7 ASP I 432 ARG I 438 1 7 HELIX 44 AE8 ARG I 462 ARG I 466 5 5 HELIX 45 AE9 VAL J 478 LEU J 483 1 6 HELIX 46 AF1 GLY J 484 GLY J 487 5 4 HELIX 47 AF2 THR J 489 MET J 495 1 7 HELIX 48 AF3 LEU J 497 LEU J 504 1 8 HELIX 49 AF4 THR J 529 GLY J 557 1 29 HELIX 50 AF5 ASN J 578 TRP J 583 1 6 HELIX 51 AF6 THR J 587 ASP J 592 1 6 HELIX 52 AF7 TYR J 598 ASN J 616 1 19 HELIX 53 AF8 ARG K 61 GLY K 65 5 5 HELIX 54 AF9 THR K 83 THR K 87 5 5 HELIX 55 AG1 GLU L 79 PHE L 83 5 5 SHEET 1 AA1 2 TRP A 5 VAL A 8 0 SHEET 2 AA1 2 CYS B 564 PRO B 569 -1 O CYS B 564 N VAL A 8 SHEET 1 AA2 5 TRP A 15 GLU A 17 0 SHEET 2 AA2 5 TYR A 444 ILE A 449 -1 O LYS A 448 N LYS A 16 SHEET 3 AA2 5 TYR A 185 CYS A 190 -1 N ALA A 186 O VAL A 447 SHEET 4 AA2 5 VAL A 204 VAL A 207 -1 O SER A 205 N LYS A 189 SHEET 5 AA2 5 GLU A 53 VAL A 55 -1 N LEU A 54 O THR A 206 SHEET 1 AA3 2 PHE A 23 SER A 26 0 SHEET 2 AA3 2 ILE A 177 CYS A 180 -1 O HIS A 178 N ALA A 25 SHEET 1 AA4 2 ASN A 37 VAL A 38 0 SHEET 2 AA4 2 THR A 171 PHE A 172 1 O THR A 171 N VAL A 38 SHEET 1 AA5 2 GLU A 61 ASN A 64 0 SHEET 2 AA5 2 THR A 198 CYS A 201 -1 O CYS A 201 N GLU A 61 SHEET 1 AA6 5 GLU A 129 PHE A 136 0 SHEET 2 AA6 5 GLY A 109 THR A 122 -1 N PHE A 119 O GLU A 132 SHEET 3 AA6 5 LEU A 99 VAL A 106 -1 N SER A 102 O ASN A 116 SHEET 4 AA6 5 GLU A 152 ARG A 154 -1 O TYR A 153 N LEU A 99 SHEET 5 AA6 5 VAL A 142 PRO A 143 -1 N VAL A 142 O ARG A 154 SHEET 1 AA7 3 THR A 164 GLN A 165 0 SHEET 2 AA7 3 CYS A 391 TYR A 393 1 O TYR A 393 N THR A 164 SHEET 3 AA7 3 ILE A 381 ASN A 383 -1 N ILE A 382 O MET A 392 SHEET 1 AA8 4 LEU A 221 LEU A 223 0 SHEET 2 AA8 4 ILE A 401 ARG A 414 -1 O GLY A 409 N LEU A 222 SHEET 3 AA8 4 THR A 423 PRO A 428 -1 O ARG A 427 N THR A 413 SHEET 4 AA8 4 THR A 318 TYR A 321 1 N LYS A 320 O GLU A 424 SHEET 1 AA9 8 VAL A 233 ARG A 235 0 SHEET 2 AA9 8 ILE A 246 HIS A 249 -1 O HIS A 249 N VAL A 233 SHEET 3 AA9 8 ILE A 401 ARG A 414 -1 O LEU A 410 N VAL A 248 SHEET 4 AA9 8 VAL A 254 ARG A 260 -1 N CYS A 258 O CYS A 403 SHEET 5 AA9 8 HIS A 291 ILE A 294 -1 O ASN A 293 N VAL A 257 SHEET 6 AA9 8 ILE A 372 LYS A 379 -1 O ILE A 372 N ILE A 294 SHEET 7 AA9 8 GLU A 341 CYS A 345 -1 N TYR A 344 O ARG A 377 SHEET 8 AA9 8 HIS A 334 CYS A 338 -1 N HIS A 334 O CYS A 345 SHEET 1 AB1 2 ASN A 264 VAL A 269 0 SHEET 2 AB1 2 PHE A 277 ILE A 283 -1 O PHE A 277 N VAL A 269 SHEET 1 AB2 4 GLN C 3 SER C 7 0 SHEET 2 AB2 4 MET C 18 SER C 25 -1 O ARG C 23 N VAL C 5 SHEET 3 AB2 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22 SHEET 4 AB2 4 VAL C 67 ASP C 72 -1 N THR C 68 O GLU C 81 SHEET 1 AB3 6 GLN C 10 LYS C 12 0 SHEET 2 AB3 6 THR C 107 VAL C 111 1 O ILE C 110 N LYS C 12 SHEET 3 AB3 6 ALA C 88 ASN C 97 -1 N ALA C 88 O VAL C 109 SHEET 4 AB3 6 LEU C 34 LEU C 39 -1 N ILE C 37 O PHE C 91 SHEET 5 AB3 6 GLU C 46 LEU C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB3 6 VAL C 57 ASN C 58 -1 O ASN C 58 N TRP C 50 SHEET 1 AB4 4 GLN C 10 LYS C 12 0 SHEET 2 AB4 4 THR C 107 VAL C 111 1 O ILE C 110 N LYS C 12 SHEET 3 AB4 4 ALA C 88 ASN C 97 -1 N ALA C 88 O VAL C 109 SHEET 4 AB4 4 TYR C 100 TRP C 103 -1 O HIS C 102 N ARG C 94 SHEET 1 AB5 4 LEU D 4 SER D 7 0 SHEET 2 AB5 4 ALA D 19 THR D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AB5 4 ASP D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AB5 4 PHE D 62 ARG D 66 -1 N SER D 63 O THR D 74 SHEET 1 AB6 6 THR D 10 LEU D 13 0 SHEET 2 AB6 6 THR D 102 VAL D 106 1 O GLN D 105 N LEU D 11 SHEET 3 AB6 6 GLY D 84 GLN D 89 -1 N GLY D 84 O VAL D 104 SHEET 4 AB6 6 ALA D 34 GLN D 38 -1 N GLN D 38 O VAL D 85 SHEET 5 AB6 6 ARG D 45 TYR D 49 -1 O ARG D 45 N GLN D 37 SHEET 6 AB6 6 THR D 53 ARG D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AB7 3 ALA E 455 THR E 457 0 SHEET 2 AB7 3 TRP E 5 VAL E 8 -1 N TRP E 5 O THR E 457 SHEET 3 AB7 3 CYS F 564 PRO F 569 -1 O CYS F 564 N VAL E 8 SHEET 1 AB8 5 TRP E 15 GLU E 17 0 SHEET 2 AB8 5 TYR E 444 ILE E 449 -1 O LYS E 448 N LYS E 16 SHEET 3 AB8 5 TYR E 185 CYS E 190 -1 N ALA E 186 O VAL E 447 SHEET 4 AB8 5 VAL E 204 VAL E 207 -1 O SER E 205 N LYS E 189 SHEET 5 AB8 5 GLU E 53 VAL E 55 -1 N LEU E 54 O THR E 206 SHEET 1 AB9 2 PHE E 23 SER E 26 0 SHEET 2 AB9 2 ILE E 177 CYS E 180 -1 O HIS E 178 N ALA E 25 SHEET 1 AC1 2 ASN E 37 VAL E 38 0 SHEET 2 AC1 2 THR E 171 PHE E 172 1 O THR E 171 N VAL E 38 SHEET 1 AC2 2 GLU E 61 ASN E 64 0 SHEET 2 AC2 2 THR E 198 CYS E 201 -1 O CYS E 201 N GLU E 61 SHEET 1 AC3 5 GLU E 129 PHE E 136 0 SHEET 2 AC3 5 GLY E 109 THR E 122 -1 N CYS E 117 O ALA E 134 SHEET 3 AC3 5 LEU E 99 VAL E 106 -1 N SER E 102 O ASN E 116 SHEET 4 AC3 5 GLU E 152 ARG E 154 -1 O TYR E 153 N LEU E 99 SHEET 5 AC3 5 VAL E 142 PRO E 143 -1 N VAL E 142 O ARG E 154 SHEET 1 AC4 3 THR E 164 GLN E 165 0 SHEET 2 AC4 3 CYS E 391 TYR E 393 1 O TYR E 393 N THR E 164 SHEET 3 AC4 3 ILE E 381 ASN E 383 -1 N ILE E 382 O MET E 392 SHEET 1 AC5 4 LEU E 221 LEU E 223 0 SHEET 2 AC5 4 ILE E 401 ARG E 414 -1 O GLY E 409 N LEU E 222 SHEET 3 AC5 4 THR E 423 PRO E 428 -1 O ARG E 427 N THR E 413 SHEET 4 AC5 4 THR E 318 TYR E 321 1 N LYS E 320 O GLU E 424 SHEET 1 AC6 8 VAL E 233 ARG E 235 0 SHEET 2 AC6 8 ILE E 246 HIS E 249 -1 O HIS E 249 N VAL E 233 SHEET 3 AC6 8 ILE E 401 ARG E 414 -1 O LEU E 410 N VAL E 248 SHEET 4 AC6 8 VAL E 254 ARG E 260 -1 N CYS E 258 O CYS E 403 SHEET 5 AC6 8 HIS E 291 ILE E 294 -1 O ASN E 293 N VAL E 257 SHEET 6 AC6 8 ILE E 372 LYS E 379 -1 O LEU E 374 N CYS E 292 SHEET 7 AC6 8 GLU E 341 CYS E 345 -1 N TYR E 344 O ARG E 377 SHEET 8 AC6 8 HIS E 334 CYS E 338 -1 N HIS E 334 O CYS E 345 SHEET 1 AC7 2 ASN E 264 VAL E 269 0 SHEET 2 AC7 2 PHE E 277 ILE E 283 -1 O PHE E 277 N VAL E 269 SHEET 1 AC8 4 GLN G 3 SER G 7 0 SHEET 2 AC8 4 MET G 18 SER G 25 -1 O ARG G 23 N VAL G 5 SHEET 3 AC8 4 THR G 77 LEU G 82 -1 O ALA G 78 N CYS G 22 SHEET 4 AC8 4 VAL G 67 ASP G 72 -1 N THR G 68 O GLU G 81 SHEET 1 AC9 6 GLN G 10 LYS G 12 0 SHEET 2 AC9 6 THR G 107 VAL G 111 1 O ILE G 110 N LYS G 12 SHEET 3 AC9 6 ALA G 88 ASN G 97 -1 N ALA G 88 O VAL G 109 SHEET 4 AC9 6 LEU G 34 LEU G 39 -1 N LEU G 39 O VAL G 89 SHEET 5 AC9 6 GLU G 46 LYS G 52 -1 O GLU G 46 N ARG G 38 SHEET 6 AC9 6 ALA G 56 VAL G 57 -1 O ALA G 56 N LYS G 52 SHEET 1 AD1 4 GLN G 10 LYS G 12 0 SHEET 2 AD1 4 THR G 107 VAL G 111 1 O ILE G 110 N LYS G 12 SHEET 3 AD1 4 ALA G 88 ASN G 97 -1 N ALA G 88 O VAL G 109 SHEET 4 AD1 4 TYR G 100 TRP G 103 -1 O HIS G 102 N ARG G 94 SHEET 1 AD2 4 LEU H 4 SER H 7 0 SHEET 2 AD2 4 ALA H 19 THR H 25 -1 O ARG H 24 N THR H 5 SHEET 3 AD2 4 TYR H 71 ILE H 75 -1 O LEU H 73 N ILE H 21 SHEET 4 AD2 4 PHE H 62 ARG H 66 -1 N SER H 63 O THR H 74 SHEET 1 AD3 6 THR H 10 LEU H 13 0 SHEET 2 AD3 6 THR H 102 VAL H 106 1 O GLN H 105 N LEU H 11 SHEET 3 AD3 6 GLY H 84 GLN H 89 -1 N TYR H 86 O THR H 102 SHEET 4 AD3 6 ALA H 34 GLN H 38 -1 N GLN H 38 O VAL H 85 SHEET 5 AD3 6 ARG H 45 TYR H 49 -1 O ARG H 45 N GLN H 37 SHEET 6 AD3 6 THR H 53 ARG H 54 -1 O THR H 53 N TYR H 49 SHEET 1 AD4 2 TRP I 5 VAL I 8 0 SHEET 2 AD4 2 CYS J 564 PRO J 569 -1 O CYS J 564 N VAL I 8 SHEET 1 AD5 5 TRP I 15 GLU I 17 0 SHEET 2 AD5 5 TYR I 444 ILE I 449 -1 O LYS I 448 N LYS I 16 SHEET 3 AD5 5 TYR I 185 CYS I 190 -1 N ALA I 186 O VAL I 447 SHEET 4 AD5 5 VAL I 204 VAL I 207 -1 O SER I 205 N LYS I 189 SHEET 5 AD5 5 GLU I 53 LEU I 56 -1 N LEU I 56 O VAL I 204 SHEET 1 AD6 2 PHE I 23 SER I 26 0 SHEET 2 AD6 2 ILE I 177 CYS I 180 -1 O HIS I 178 N ALA I 25 SHEET 1 AD7 2 ASN I 37 VAL I 38 0 SHEET 2 AD7 2 THR I 171 PHE I 172 1 O THR I 171 N VAL I 38 SHEET 1 AD8 2 GLU I 61 ASN I 64 0 SHEET 2 AD8 2 THR I 198 CYS I 201 -1 O GLY I 199 N PHE I 63 SHEET 1 AD9 5 GLU I 129 PHE I 136 0 SHEET 2 AD9 5 GLY I 109 THR I 122 -1 N PHE I 119 O GLU I 132 SHEET 3 AD9 5 LEU I 99 VAL I 106 -1 N SER I 102 O ASN I 116 SHEET 4 AD9 5 GLU I 152 ARG I 154 -1 O TYR I 153 N LEU I 99 SHEET 5 AD9 5 VAL I 142 PRO I 143 -1 N VAL I 142 O ARG I 154 SHEET 1 AE1 3 THR I 164 GLN I 165 0 SHEET 2 AE1 3 CYS I 391 TYR I 393 1 O TYR I 393 N THR I 164 SHEET 3 AE1 3 ILE I 381 ASN I 383 -1 N ILE I 382 O MET I 392 SHEET 1 AE2 7 LEU I 221 LEU I 223 0 SHEET 2 AE2 7 ILE I 401 ARG I 414 -1 O GLY I 409 N LEU I 222 SHEET 3 AE2 7 VAL I 254 ARG I 260 -1 N CYS I 258 O CYS I 403 SHEET 4 AE2 7 HIS I 291 ILE I 294 -1 O ASN I 293 N VAL I 257 SHEET 5 AE2 7 ILE I 372 LYS I 379 -1 O LEU I 374 N CYS I 292 SHEET 6 AE2 7 GLU I 341 CYS I 345 -1 N TYR I 344 O ARG I 377 SHEET 7 AE2 7 HIS I 334 CYS I 338 -1 N HIS I 334 O CYS I 345 SHEET 1 AE3 6 VAL I 233 ARG I 235 0 SHEET 2 AE3 6 ILE I 246 HIS I 249 -1 O HIS I 249 N VAL I 233 SHEET 3 AE3 6 ILE I 401 ARG I 414 -1 O LEU I 410 N VAL I 248 SHEET 4 AE3 6 THR I 423 PRO I 428 -1 O ARG I 427 N THR I 413 SHEET 5 AE3 6 THR I 318 TYR I 321 1 N LYS I 320 O GLU I 424 SHEET 6 AE3 6 THR I 354 TYR I 355 -1 O TYR I 355 N ILE I 319 SHEET 1 AE4 2 ASN I 264 GLY I 272 0 SHEET 2 AE4 2 GLN I 275 ILE I 283 -1 O PHE I 277 N VAL I 269 SHEET 1 AE5 4 GLN K 3 SER K 7 0 SHEET 2 AE5 4 MET K 18 SER K 25 -1 O ARG K 23 N VAL K 5 SHEET 3 AE5 4 THR K 77 LEU K 82 -1 O ALA K 78 N CYS K 22 SHEET 4 AE5 4 VAL K 67 ASP K 72 -1 N THR K 68 O GLU K 81 SHEET 1 AE6 6 GLN K 10 LYS K 12 0 SHEET 2 AE6 6 THR K 107 VAL K 111 1 O ILE K 110 N LYS K 12 SHEET 3 AE6 6 ALA K 88 ASN K 97 -1 N ALA K 88 O VAL K 109 SHEET 4 AE6 6 LEU K 34 ARG K 38 -1 N ILE K 37 O PHE K 91 SHEET 5 AE6 6 GLU K 46 LYS K 52 -1 O GLU K 46 N ARG K 38 SHEET 6 AE6 6 ALA K 56 ASN K 58 -1 O ALA K 56 N LYS K 52 SHEET 1 AE7 4 GLN K 10 LYS K 12 0 SHEET 2 AE7 4 THR K 107 VAL K 111 1 O ILE K 110 N LYS K 12 SHEET 3 AE7 4 ALA K 88 ASN K 97 -1 N ALA K 88 O VAL K 109 SHEET 4 AE7 4 TYR K 100 TRP K 103 -1 O HIS K 102 N ARG K 94 SHEET 1 AE8 4 THR L 5 SER L 7 0 SHEET 2 AE8 4 ALA L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AE8 4 TYR L 71 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AE8 4 PHE L 62 ARG L 66 -1 N SER L 63 O THR L 74 SHEET 1 AE9 6 THR L 10 LEU L 13 0 SHEET 2 AE9 6 THR L 102 VAL L 106 1 O GLN L 105 N LEU L 11 SHEET 3 AE9 6 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AE9 6 ALA L 34 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AE9 6 ARG L 45 TYR L 49 -1 O VAL L 47 N TRP L 35 SHEET 6 AE9 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AF1 4 THR L 10 LEU L 13 0 SHEET 2 AF1 4 THR L 102 VAL L 106 1 O GLN L 105 N LEU L 11 SHEET 3 AF1 4 GLY L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AF1 4 PHE L 97 PHE L 98 -1 O PHE L 97 N GLN L 90 SSBOND 1 CYS A 24 CYS A 44 1555 1555 2.03 SSBOND 2 CYS A 89 CYS A 167 1555 1555 2.03 SSBOND 3 CYS A 96 CYS A 158 1555 1555 2.02 SSBOND 4 CYS A 101 CYS A 117 1555 1555 2.03 SSBOND 5 CYS A 180 CYS A 209 1555 1555 2.03 SSBOND 6 CYS A 190 CYS A 201 1555 1555 2.03 SSBOND 7 CYS A 258 CYS A 292 1555 1555 2.03 SSBOND 8 CYS A 338 CYS A 403 1555 1555 2.02 SSBOND 9 CYS A 345 CYS A 376 1555 1555 2.04 SSBOND 10 CYS A 459 CYS B 565 1555 1555 2.03 SSBOND 11 CYS B 558 CYS B 564 1555 1555 2.03 SSBOND 12 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 13 CYS C 32 CYS C 98 1555 1555 2.03 SSBOND 14 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 15 CYS E 24 CYS E 44 1555 1555 2.03 SSBOND 16 CYS E 89 CYS E 167 1555 1555 2.03 SSBOND 17 CYS E 96 CYS E 158 1555 1555 2.02 SSBOND 18 CYS E 101 CYS E 117 1555 1555 2.03 SSBOND 19 CYS E 180 CYS E 209 1555 1555 2.03 SSBOND 20 CYS E 190 CYS E 201 1555 1555 2.03 SSBOND 21 CYS E 258 CYS E 292 1555 1555 2.04 SSBOND 22 CYS E 338 CYS E 403 1555 1555 2.03 SSBOND 23 CYS E 345 CYS E 376 1555 1555 2.04 SSBOND 24 CYS E 459 CYS F 565 1555 1555 2.03 SSBOND 25 CYS F 558 CYS F 564 1555 1555 2.03 SSBOND 26 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 27 CYS G 32 CYS G 98 1555 1555 2.03 SSBOND 28 CYS H 23 CYS H 88 1555 1555 2.03 SSBOND 29 CYS I 24 CYS I 44 1555 1555 2.03 SSBOND 30 CYS I 89 CYS I 167 1555 1555 2.03 SSBOND 31 CYS I 96 CYS I 158 1555 1555 2.02 SSBOND 32 CYS I 101 CYS I 117 1555 1555 2.03 SSBOND 33 CYS I 180 CYS I 209 1555 1555 2.03 SSBOND 34 CYS I 190 CYS I 201 1555 1555 2.03 SSBOND 35 CYS I 258 CYS I 292 1555 1555 2.04 SSBOND 36 CYS I 338 CYS I 403 1555 1555 2.03 SSBOND 37 CYS I 345 CYS I 376 1555 1555 2.03 SSBOND 38 CYS I 459 CYS J 565 1555 1555 2.03 SSBOND 39 CYS J 558 CYS J 564 1555 1555 2.03 SSBOND 40 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 41 CYS K 32 CYS K 98 1555 1555 2.03 SSBOND 42 CYS L 23 CYS L 88 1555 1555 2.03 CISPEP 1 HIS A 42 ALA A 43 0 10.86 CISPEP 2 SER A 50 PRO A 51 0 -4.65 CISPEP 3 GLY A 416 GLY A 417 0 -1.44 CISPEP 4 SER C 7 GLY C 8 0 0.14 CISPEP 5 SER D 7 PRO D 8 0 -2.23 CISPEP 6 HIS E 42 ALA E 43 0 10.50 CISPEP 7 SER E 50 PRO E 51 0 -4.64 CISPEP 8 GLY E 416 GLY E 417 0 6.86 CISPEP 9 SER G 7 GLY G 8 0 0.82 CISPEP 10 SER H 7 PRO H 8 0 -2.33 CISPEP 11 HIS I 42 ALA I 43 0 11.59 CISPEP 12 SER I 50 PRO I 51 0 -6.04 CISPEP 13 GLY I 416 GLY I 417 0 -7.31 CISPEP 14 SER K 7 GLY K 8 0 -0.15 CISPEP 15 SER L 7 PRO L 8 0 -1.35 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