HEADER VIRAL PROTEIN/IMMUNE SYSTEM 22-DEC-23 8VFV TITLE HIV ENV BG505_MD39_B16 SOSIP BOOSTING TRIMER IN COMPLEX WITH B16_D77.5 TITLE 2 MOUSE FAB AND RM20A3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM20A3 FAB HEAVY CHAIN; COMPND 3 CHAIN: G, C, M; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM20A3 FAB LIGHT CHAIN; COMPND 7 CHAIN: I, D, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: E, A, J; COMPND 12 SYNONYM: ENV POLYPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: TRANSMEMBRANE PROTEIN GP41; COMPND 16 CHAIN: F, B, K; COMPND 17 SYNONYM: TM, GLYCOPROTEIN 41, GP41; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: B16_D77.5 MOUSE FAB HEAVY CHAIN FV; COMPND 21 CHAIN: H; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: B16_D77.5 MOUSE FAB LIGHT CHAIN FV; COMPND 25 CHAIN: L; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 11 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 12 ORGANISM_TAXID: 9544; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 18 ORGANISM_TAXID: 11676; SOURCE 19 GENE: ENV; SOURCE 20 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 25 ORGANISM_TAXID: 11676; SOURCE 26 GENE: ENV; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 MOL_ID: 5; SOURCE 31 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 32 ORGANISM_COMMON: MOUSE; SOURCE 33 ORGANISM_TAXID: 10090; SOURCE 34 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 35 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 36 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 37 MOL_ID: 6; SOURCE 38 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 39 ORGANISM_COMMON: MOUSE; SOURCE 40 ORGANISM_TAXID: 10090; SOURCE 41 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 42 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 43 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MOUSE ANTIBODY, GERMLINE TARGETING, HIV-1, VACCINE DESIGN, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.OZOROWSKI,J.L.TORRES,A.B.WARD JRNL AUTH Z.XIE,Y.C.LIN,J.M.STEICHEN,G.OZOROWSKI,S.KRATOCHVIL,R.RAY, JRNL AUTH 2 J.L.TORRES,A.LIGUORI,O.KALYUZHNIY,X.WANG,J.E.WARNER, JRNL AUTH 3 S.R.WELDON,G.A.DALE,K.H.KIRSCH,U.NAIR,S.BABOO,E.GEORGESON, JRNL AUTH 4 Y.ADACHI,M.KUBITZ,A.M.JACKSON,S.T.RICHEY,R.M.VOLK,J.H.LEE, JRNL AUTH 5 J.K.DIEDRICH,T.PRUM,S.FALCONE,S.HIMANSU,A.CARFI,J.R.YATES, JRNL AUTH 6 J.C.PAULSON,D.SOK,A.B.WARD,W.R.SCHIEF,F.D.BATISTA JRNL TITL MRNA-LNP HIV-1 TRIMER BOOSTERS ELICIT PRECURSORS TO BROAD JRNL TITL 2 NEUTRALIZING ANTIBODIES JRNL REF SCIENCE 2024 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADK0582 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, CRYOSPARC, CRYOSPARC 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) : 3.300 REMARK 3 NUMBER OF PARTICLES : 39822 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 8VFV 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_1000280126. 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 : IV ENV BG505_MD39_B16 SOSIP REMARK 245 BOOSTING TRIMER IN COMPLEX WITH REMARK 245 B16_D77.5 MOUSE FAB AND RM20A3 REMARK 245 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 6.90 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : TFS GLACIOS REMARK 245 DETECTOR TYPE : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 45.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: TETRADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, E, F, C, D, H, L, A, B, REMARK 350 AND CHAINS: M, N, J, K, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W 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 VAL G 111 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 GLY I 107 REMARK 465 GLN I 108 REMARK 465 PRO I 109 REMARK 465 LYS I 110 REMARK 465 ALA I 111 REMARK 465 SER I 112 REMARK 465 PRO I 113 REMARK 465 THR I 114 REMARK 465 VAL I 115 REMARK 465 THR I 116 REMARK 465 LEU I 117 REMARK 465 PHE I 118 REMARK 465 PRO I 119 REMARK 465 PRO I 120 REMARK 465 SER I 121 REMARK 465 SER I 122 REMARK 465 GLU I 123 REMARK 465 GLU I 124 REMARK 465 LEU I 125 REMARK 465 ALA E 31 REMARK 465 GLU E 32 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 GLY E 185D REMARK 465 ASN E 185E REMARK 465 ARG E 185F REMARK 465 SER E 185G REMARK 465 ASN E 185H REMARK 465 ASN E 185I REMARK 465 SER E 185J REMARK 465 ASN E 185K REMARK 465 ASN E 399 REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 GLY E 459 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 ASN E 462 REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 ARG E 509 REMARK 465 ARG E 510 REMARK 465 ARG E 511 REMARK 465 ARG E 512 REMARK 465 ARG E 513 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 VAL F 518 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 PRO 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 ASP F 568 REMARK 465 THR F 569 REMARK 465 HIS F 570 REMARK 465 TRP F 571 REMARK 465 SER C 112 REMARK 465 SER C 113 REMARK 465 GLY D 107 REMARK 465 GLN D 108 REMARK 465 PRO D 109 REMARK 465 LYS D 110 REMARK 465 ALA D 111 REMARK 465 SER D 112 REMARK 465 PRO D 113 REMARK 465 THR D 114 REMARK 465 VAL D 115 REMARK 465 THR D 116 REMARK 465 LEU D 117 REMARK 465 PHE D 118 REMARK 465 PRO D 119 REMARK 465 PRO D 120 REMARK 465 SER D 121 REMARK 465 SER D 122 REMARK 465 GLU D 123 REMARK 465 GLU D 124 REMARK 465 LEU D 125 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 SER A 185J REMARK 465 ASN A 185K REMARK 465 ASN A 399 REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 GLY A 459 REMARK 465 SER A 460 REMARK 465 THR A 461 REMARK 465 ASN A 462 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 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 VAL B 518 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 PRO 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 ASP B 568 REMARK 465 THR B 569 REMARK 465 HIS B 570 REMARK 465 TRP B 571 REMARK 465 SER M 112 REMARK 465 SER M 113 REMARK 465 GLY N 107 REMARK 465 GLN N 108 REMARK 465 PRO N 109 REMARK 465 LYS N 110 REMARK 465 ALA N 111 REMARK 465 SER N 112 REMARK 465 PRO N 113 REMARK 465 THR N 114 REMARK 465 VAL N 115 REMARK 465 THR N 116 REMARK 465 LEU N 117 REMARK 465 PHE N 118 REMARK 465 PRO N 119 REMARK 465 PRO N 120 REMARK 465 SER N 121 REMARK 465 SER N 122 REMARK 465 GLU N 123 REMARK 465 GLU N 124 REMARK 465 LEU N 125 REMARK 465 ALA J 31 REMARK 465 GLU J 32 REMARK 465 ALA J 58 REMARK 465 LYS J 59 REMARK 465 ALA J 60 REMARK 465 TYR J 61 REMARK 465 GLU J 62 REMARK 465 THR J 63 REMARK 465 GLU J 64 REMARK 465 LYS J 65 REMARK 465 GLU J 185A REMARK 465 ASN J 185B REMARK 465 GLN J 185C REMARK 465 GLY J 185D REMARK 465 ASN J 185E REMARK 465 ARG J 185F REMARK 465 SER J 185G REMARK 465 ASN J 185H REMARK 465 ASN J 185I REMARK 465 SER J 185J REMARK 465 ASN J 185K REMARK 465 ASN J 399 REMARK 465 THR J 400 REMARK 465 SER J 401 REMARK 465 VAL J 402 REMARK 465 GLN J 403 REMARK 465 GLY J 404 REMARK 465 SER J 405 REMARK 465 ASN J 406 REMARK 465 SER J 407 REMARK 465 THR J 408 REMARK 465 GLY J 409 REMARK 465 SER J 410 REMARK 465 GLY J 459 REMARK 465 SER J 460 REMARK 465 THR J 461 REMARK 465 ASN J 462 REMARK 465 VAL J 506 REMARK 465 GLY J 507 REMARK 465 ARG J 508 REMARK 465 ARG J 509 REMARK 465 ARG J 510 REMARK 465 ARG J 511 REMARK 465 ARG J 512 REMARK 465 ARG J 513 REMARK 465 ALA K 512 REMARK 465 VAL K 513 REMARK 465 GLY K 514 REMARK 465 ILE K 515 REMARK 465 GLY K 516 REMARK 465 ALA K 517 REMARK 465 VAL K 518 REMARK 465 GLY K 547 REMARK 465 ILE K 548 REMARK 465 VAL K 549 REMARK 465 GLN K 550 REMARK 465 GLN K 551 REMARK 465 GLN K 552 REMARK 465 SER K 553 REMARK 465 ASN K 554 REMARK 465 LEU K 555 REMARK 465 LEU K 556 REMARK 465 ARG K 557 REMARK 465 ALA K 558 REMARK 465 PRO K 559 REMARK 465 GLU K 560 REMARK 465 PRO K 561 REMARK 465 GLN K 562 REMARK 465 GLN K 563 REMARK 465 HIS K 564 REMARK 465 LEU K 565 REMARK 465 LEU K 566 REMARK 465 LYS K 567 REMARK 465 ASP K 568 REMARK 465 THR K 569 REMARK 465 HIS K 570 REMARK 465 TRP K 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 O SER G 62 NH1 ARG G 66 1.70 REMARK 500 OG1 THR A 303 OD1 ASP A 322 1.94 REMARK 500 O ASN E 197 NH1 ARG A 308 2.00 REMARK 500 OG SER C 35 O SER C 49 2.00 REMARK 500 O VAL J 36 OG1 THR K 606 2.05 REMARK 500 OG SER B 528 O7 NAG A 601 2.11 REMARK 500 OG SER K 528 O7 NAG J 601 2.12 REMARK 500 OG1 THR A 297 O ILE A 443 2.14 REMARK 500 OG SER F 528 O7 NAG E 601 2.16 REMARK 500 O GLY M 10 OG1 THR M 110 2.18 REMARK 500 O GLY C 96 OH TYR D 96 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 SER G 82B -54.48 73.39 REMARK 500 ASP G 86 32.10 -89.62 REMARK 500 ALA G 100 -10.57 77.13 REMARK 500 LYS G 100E -94.71 -105.02 REMARK 500 ASP I 27B -81.00 -127.83 REMARK 500 ASP I 50 -179.89 62.44 REMARK 500 LEU E 154 92.25 66.53 REMARK 500 GLN E 258 -57.26 64.33 REMARK 500 ASN E 262 -125.72 54.70 REMARK 500 ILE E 277 -55.61 69.10 REMARK 500 THR E 387 -2.39 68.98 REMARK 500 TRP E 427 33.33 72.05 REMARK 500 GLU E 492 79.98 -118.32 REMARK 500 SER F 612 -48.80 67.61 REMARK 500 SER C 82B -54.50 73.47 REMARK 500 ALA C 100 -37.63 59.85 REMARK 500 LYS C 100E -93.48 -112.83 REMARK 500 ASP D 27B -90.11 -111.62 REMARK 500 ASP D 50 -176.92 63.29 REMARK 500 SER H 15 -1.56 75.80 REMARK 500 ALA L 51 -48.54 70.19 REMARK 500 ARG L 68 -109.26 54.39 REMARK 500 LEU A 154 84.81 62.49 REMARK 500 GLN A 258 -56.58 65.66 REMARK 500 ASN A 262 -123.75 53.50 REMARK 500 ASN A 276 -35.80 -131.59 REMARK 500 ILE A 277 -57.00 68.32 REMARK 500 THR A 387 -3.62 67.87 REMARK 500 SER B 612 -48.32 66.74 REMARK 500 SER B 615 124.21 -173.28 REMARK 500 SER M 82B -52.88 72.56 REMARK 500 ALA M 100 -36.21 60.65 REMARK 500 LYS M 100E -92.56 -113.85 REMARK 500 ASP N 27B -80.33 -126.38 REMARK 500 ASP N 50 -178.16 64.31 REMARK 500 LEU J 154 84.96 61.21 REMARK 500 GLN J 258 -62.31 64.64 REMARK 500 ASN J 262 -125.84 54.10 REMARK 500 ASN J 276 -34.14 -131.60 REMARK 500 ILE J 277 -57.91 69.48 REMARK 500 PRO J 313 98.53 -69.57 REMARK 500 THR J 387 -2.59 66.73 REMARK 500 ASN J 392 57.65 -143.08 REMARK 500 GLU J 492 79.97 -119.06 REMARK 500 SER K 612 -48.29 67.47 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43190 RELATED DB: EMDB REMARK 900 HIV ENV BG505_MD39_B16 SOSIP BOOSTING TRIMER IN COMPLEX WITH B16_ REMARK 900 D77.5 MOUSE FAB AND RM20A3 FAB DBREF 8VFV G 1 113 PDB 8VFV 8VFV 1 113 DBREF 8VFV I 3 125 PDB 8VFV 8VFV 3 125 DBREF 8VFV E 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8VFV F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8VFV C 1 113 PDB 8VFV 8VFV 1 113 DBREF 8VFV D 3 125 PDB 8VFV 8VFV 3 125 DBREF 8VFV H 1 113 PDB 8VFV 8VFV 1 113 DBREF 8VFV L 1 107 PDB 8VFV 8VFV 1 107 DBREF 8VFV A 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8VFV B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8VFV M 1 113 PDB 8VFV 8VFV 1 113 DBREF 8VFV N 3 125 PDB 8VFV 8VFV 3 125 DBREF 8VFV J 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8VFV K 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 8VFV GLU E 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 8VFV TYR E 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 8VFV GLU E 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 8VFV LYS E 137 UNP Q2N0S6 ASN 136 CONFLICT SEQADV 8VFV LEU E 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 8VFV ARG E 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 8VFV SER E 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 8VFV MET E 141 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 8VFV LYS E 151 UNP Q2N0S6 ARG 142 CONFLICT SEQADV 8VFV ILE E 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 8VFV LEU E 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 8VFV VAL E 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 8VFV TYR E 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 8VFV HIS E 325 UNP Q2N0S6 ASP 323 CONFLICT SEQADV 8VFV ASN E 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8VFV GLN E 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 8VFV CYS E 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8VFV ARG E 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8VFV ARG E 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8VFV ARG E 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8VFV ARG E 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8VFV SER F 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 8VFV PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8VFV PRO F 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 8VFV ASP F 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 8VFV HIS F 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 8VFV HIS F 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 8VFV CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8VFV GLU A 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 8VFV TYR A 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 8VFV GLU A 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 8VFV LYS A 137 UNP Q2N0S6 ASN 136 CONFLICT SEQADV 8VFV LEU A 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 8VFV ARG A 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 8VFV SER A 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 8VFV MET A 141 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 8VFV LYS A 151 UNP Q2N0S6 ARG 142 CONFLICT SEQADV 8VFV ILE A 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 8VFV LEU A 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 8VFV VAL A 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 8VFV TYR A 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 8VFV HIS A 325 UNP Q2N0S6 ASP 323 CONFLICT SEQADV 8VFV ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8VFV GLN A 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 8VFV CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8VFV ARG A 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8VFV ARG A 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8VFV ARG A 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8VFV ARG A 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8VFV SER B 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 8VFV PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8VFV PRO B 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 8VFV ASP B 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 8VFV HIS B 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 8VFV HIS B 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 8VFV CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8VFV GLU J 106 UNP Q2N0S6 THR 105 CONFLICT SEQADV 8VFV TYR J 134 UNP Q2N0S6 VAL 133 CONFLICT SEQADV 8VFV GLU J 136 UNP Q2N0S6 ASN 135 CONFLICT SEQADV 8VFV LYS J 137 UNP Q2N0S6 ASN 136 CONFLICT SEQADV 8VFV LEU J 138 UNP Q2N0S6 ILE 137 CONFLICT SEQADV 8VFV ARG J 139 UNP Q2N0S6 THR 138 CONFLICT SEQADV 8VFV SER J 140 UNP Q2N0S6 ASP 139 CONFLICT SEQADV 8VFV MET J 141 UNP Q2N0S6 ASP 140 CONFLICT SEQADV 8VFV LYS J 151 UNP Q2N0S6 ARG 142 CONFLICT SEQADV 8VFV ILE J 271 UNP Q2N0S6 MET 270 CONFLICT SEQADV 8VFV LEU J 288 UNP Q2N0S6 PHE 287 CONFLICT SEQADV 8VFV VAL J 304 UNP Q2N0S6 ARG 303 CONFLICT SEQADV 8VFV TYR J 319 UNP Q2N0S6 ALA 316 CONFLICT SEQADV 8VFV HIS J 325 UNP Q2N0S6 ASP 323 CONFLICT SEQADV 8VFV ASN J 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8VFV GLN J 363 UNP Q2N0S6 ASN 361 CONFLICT SEQADV 8VFV CYS J 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8VFV ARG J 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8VFV ARG J 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8VFV ARG J 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8VFV ARG J 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8VFV SER K 519 UNP Q2N0S6 PHE 516 CONFLICT SEQADV 8VFV PRO K 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8VFV PRO K 561 UNP Q2N0S6 ALA 558 CONFLICT SEQADV 8VFV ASP K 568 UNP Q2N0S6 LEU 565 CONFLICT SEQADV 8VFV HIS K 570 UNP Q2N0S6 VAL 567 CONFLICT SEQADV 8VFV HIS K 585 UNP Q2N0S6 ARG 582 CONFLICT SEQADV 8VFV CYS K 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 G 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 G 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 G 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 G 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 G 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 G 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 G 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 G 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 G 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 G 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 I 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 I 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 I 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 I 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 I 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 I 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 I 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 I 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 I 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 I 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 E 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 E 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 E 481 THR GLU LYS LEU ARG SER MET MET LYS GLY GLU LEU LYS SEQRES 10 E 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 E 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 E 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 E 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 E 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 E 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 E 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 E 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 E 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 E 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 E 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 E 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 E 481 TYR THR GLY ASP ILE ILE GLY HIS ILE ARG GLN ALA HIS SEQRES 24 E 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 E 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 E 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 E 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 E 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 E 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 E 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 E 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 E 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 E 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 E 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 E 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 E 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 E 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL SER 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 PRO GLU PRO GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS 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 C 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 C 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 C 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 C 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 C 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 C 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 C 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 C 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 C 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 C 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 D 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 D 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 D 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 D 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 D 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 D 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 D 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 D 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 D 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 D 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 H 130 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 130 GLY SER ILE SER SER GLY HIS TRP TRP SER TRP VAL ARG SEQRES 4 H 130 GLN SER PRO GLY LYS GLY LEU GLU TRP ILE GLY THR ILE SEQRES 5 H 130 TYR HIS SER GLY SER ALA ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 130 SER ARG VAL THR ILE SER VAL ASP LYS SER LYS ASN GLN SEQRES 7 H 130 PHE SER LEU LYS LEU THR SER VAL THR ALA ALA ASP THR SEQRES 8 H 130 ALA VAL TYR PHE CYS ALA ARG ASN ALA ILE LEU ILE PHE SEQRES 9 H 130 GLY VAL ILE ALA PHE GLY GLU TYR TYR PHE CYS GLY MET SEQRES 10 H 130 ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER SEQRES 1 L 111 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 L 111 SER LEU GLY GLN ARG ALA THR ILE PHE CYS ARG ALA SER SEQRES 3 L 111 ASP THR VAL ASP ILE SER GLY ASP SER PHE MET HIS TRP SEQRES 4 L 111 TYR GLN GLN LYS PRO GLY GLN PRO PRO ASN LEU LEU ILE SEQRES 5 L 111 TYR ARG ALA SER ASN LEU GLN SER GLY ILE PRO ALA ARG SEQRES 6 L 111 PHE SER GLY SER GLY SER ARG ALA ASP PHE THR LEU THR SEQRES 7 L 111 ILE ASP PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR SEQRES 8 L 111 CYS GLN GLN SER SER GLU ASP PRO LEU THR PHE GLY ALA SEQRES 9 L 111 GLY THR LYS LEU GLU LEU LYS SEQRES 1 A 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 A 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 A 481 THR GLU LYS LEU ARG SER MET MET LYS GLY GLU LEU LYS SEQRES 10 A 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 A 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 A 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 481 TYR THR GLY ASP ILE ILE GLY HIS ILE ARG GLN ALA HIS SEQRES 24 A 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 A 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 A 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL SER 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 PRO GLU PRO GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS 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 M 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 M 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 M 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 M 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 M 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 M 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 M 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 M 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 M 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 M 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 N 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 N 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 N 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 N 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 N 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 N 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 N 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 N 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 N 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 N 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 J 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 J 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 J 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 J 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 J 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 J 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 J 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 J 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 J 481 THR GLU LYS LEU ARG SER MET MET LYS GLY GLU LEU LYS SEQRES 10 J 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 J 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 J 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 J 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 J 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 J 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 J 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 J 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 J 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 J 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 J 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 J 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 J 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 J 481 TYR THR GLY ASP ILE ILE GLY HIS ILE ARG GLN ALA HIS SEQRES 24 J 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 J 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 J 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 J 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 J 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 J 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 J 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 J 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 J 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 J 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 J 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 J 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 J 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 J 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 K 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 K 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 K 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 K 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 K 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 K 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 K 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 K 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 K 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 K 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 K 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 K 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG E 606 14 HET NAG E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG E 610 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG J 601 14 HET NAG J 602 14 HET NAG J 603 14 HET NAG J 604 14 HET NAG J 605 14 HET NAG J 606 14 HET NAG J 607 14 HET NAG J 608 14 HET NAG J 609 14 HET NAG J 610 14 HET NAG K 701 14 HET NAG K 702 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET MAN O 4 11 HET MAN O 5 11 HET MAN O 6 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET MAN P 4 11 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET MAN R 6 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET MAN S 4 11 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET MAN U 5 11 HET MAN U 6 11 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET NAG W 1 14 HET NAG W 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 15 NAG 54(C8 H15 N O6) FORMUL 51 BMA 6(C6 H12 O6) FORMUL 51 MAN 12(C6 H12 O6) HELIX 1 AA1 THR G 28 PHE G 32 5 5 HELIX 2 AA2 ASP G 61 LYS G 64 5 4 HELIX 3 AA3 ARG G 83 THR G 87 5 5 HELIX 4 AA4 GLN I 79 GLU I 83 5 5 HELIX 5 AA5 ASN E 98 LYS E 117 1 20 HELIX 6 AA6 LEU E 122 CYS E 126 5 5 HELIX 7 AA7 TYR E 177 LEU E 179 5 3 HELIX 8 AA8 ASN E 195 THR E 198 5 4 HELIX 9 AA9 LYS E 335 GLY E 354 1 20 HELIX 10 AB1 ASP E 368 THR E 373 1 6 HELIX 11 AB2 THR E 387 PHE E 391 5 5 HELIX 12 AB3 MET E 475 TYR E 484 1 10 HELIX 13 AB4 THR F 529 SER F 534 1 6 HELIX 14 AB5 THR F 536 ASN F 543 1 8 HELIX 15 AB6 ILE F 573 TRP F 596 1 24 HELIX 16 AB7 ASN F 618 ASP F 624 1 7 HELIX 17 AB8 THR F 627 ILE F 635 1 9 HELIX 18 AB9 TYR F 638 LEU F 661 1 24 HELIX 19 AC1 THR C 28 PHE C 32 5 5 HELIX 20 AC2 ASP C 61 LYS C 64 5 4 HELIX 21 AC3 ARG C 83 THR C 87 5 5 HELIX 22 AC4 GLN D 79 GLU D 83 5 5 HELIX 23 AC5 THR H 83 THR H 87 5 5 HELIX 24 AC6 VAL H 100B GLY H 100F 5 5 HELIX 25 AC7 GLU L 79 VAL L 83 5 5 HELIX 26 AC8 ASN A 98 LYS A 117 1 20 HELIX 27 AC9 LEU A 122 CYS A 126 5 5 HELIX 28 AD1 TYR A 177 LEU A 179 5 3 HELIX 29 AD2 ASN A 195 THR A 198 5 4 HELIX 30 AD3 LYS A 335 GLY A 354 1 20 HELIX 31 AD4 ASP A 368 THR A 373 1 6 HELIX 32 AD5 THR A 387 PHE A 391 5 5 HELIX 33 AD6 ASN A 425 ARG A 429 5 5 HELIX 34 AD7 MET A 475 LEU A 483 1 9 HELIX 35 AD8 LEU B 523 SER B 528 5 6 HELIX 36 AD9 THR B 529 SER B 534 1 6 HELIX 37 AE1 THR B 536 ASN B 543 1 8 HELIX 38 AE2 ILE B 573 TRP B 596 1 24 HELIX 39 AE3 ASN B 618 ASP B 624 1 7 HELIX 40 AE4 THR B 627 SER B 636 1 10 HELIX 41 AE5 TYR B 638 LEU B 661 1 24 HELIX 42 AE6 THR M 28 PHE M 32 5 5 HELIX 43 AE7 ASP M 61 LYS M 64 5 4 HELIX 44 AE8 ARG M 83 THR M 87 5 5 HELIX 45 AE9 GLN N 79 GLU N 83 5 5 HELIX 46 AF1 ALA J 70 CYS J 74 5 5 HELIX 47 AF2 ASN J 98 LYS J 117 1 20 HELIX 48 AF3 LEU J 122 CYS J 126 5 5 HELIX 49 AF4 TYR J 177 LEU J 179 5 3 HELIX 50 AF5 ASN J 195 THR J 198 5 4 HELIX 51 AF6 LYS J 335 GLY J 354 1 20 HELIX 52 AF7 ASP J 368 THR J 373 1 6 HELIX 53 AF8 THR J 387 PHE J 391 5 5 HELIX 54 AF9 MET J 475 TYR J 484 1 10 HELIX 55 AG1 THR K 529 SER K 534 1 6 HELIX 56 AG2 THR K 536 ASN K 543 1 8 HELIX 57 AG3 ILE K 573 TRP K 596 1 24 HELIX 58 AG4 ASN K 618 ASP K 624 1 7 HELIX 59 AG5 THR K 627 SER K 636 1 10 HELIX 60 AG6 TYR K 638 LEU K 661 1 24 SHEET 1 AA1 4 GLN G 3 THR G 7 0 SHEET 2 AA1 4 LEU G 18 SER G 25 -1 O SER G 21 N THR G 7 SHEET 3 AA1 4 THR G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 4 AA1 4 PHE G 67 ASP G 72 -1 N THR G 68 O GLN G 81 SHEET 1 AA2 6 MET G 34 GLN G 39 0 SHEET 2 AA2 6 LEU G 45 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 3 AA2 6 THR G 57 TYR G 59 -1 O PHE G 58 N LEU G 50 SHEET 4 AA2 6 ALA G 88 GLY G 95 -1 O TYR G 91 N VAL G 37 SHEET 5 AA2 6 PHE G 100H TRP G 103 -1 O PHE G 102 N THR G 94 SHEET 6 AA2 6 ALA G 107 VAL G 109 -1 O ALA G 107 N TYR G 90 SHEET 1 AA3 6 SER I 9 GLY I 13 0 SHEET 2 AA3 6 VAL I 33 GLN I 38 0 SHEET 3 AA3 6 LYS I 45 TYR I 49 -1 O LYS I 45 N GLN I 37 SHEET 4 AA3 6 ALA I 84 TYR I 91 -1 O ASP I 85 N GLN I 38 SHEET 5 AA3 6 TYR I 96 PHE I 98 -1 O ILE I 97 N ALA I 90 SHEET 6 AA3 6 THR I 102 VAL I 106 -1 O LEU I 104 N ALA I 84 SHEET 1 AA4 3 VAL I 19 THR I 24 0 SHEET 2 AA4 3 THR I 70 ILE I 75 -1 O LEU I 73 N ILE I 21 SHEET 3 AA4 3 PHE I 62 SER I 67 -1 N SER I 67 O THR I 70 SHEET 1 AA5 3 LEU E 494 THR E 499 0 SHEET 2 AA5 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AA5 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AA6 5 TRP E 45 ASP E 47 0 SHEET 2 AA6 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AA6 5 PHE E 223 LYS E 227 -1 N ALA E 224 O VAL E 489 SHEET 4 AA6 5 SER E 243 VAL E 245 -1 O VAL E 245 N ILE E 225 SHEET 5 AA6 5 ILE E 84 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AA7 3 VAL E 75 PRO E 76 0 SHEET 2 AA7 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AA7 3 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AA8 2 GLU E 91 ASN E 94 0 SHEET 2 AA8 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AA9 5 LYS E 169 PHE E 176 0 SHEET 2 AA9 5 LYS E 155 THR E 162 -1 N PHE E 159 O VAL E 172 SHEET 3 AA9 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AA9 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AA9 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AB1 3 THR E 202 GLN E 203 0 SHEET 2 AB1 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AB1 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AB212 LEU E 259 LEU E 261 0 SHEET 2 AB212 ILE E 271 SER E 274 0 SHEET 3 AB212 ILE E 284 GLY E 312 -1 O GLN E 287 N ILE E 271 SHEET 4 AB212 GLN E 315 ILE E 323A-1 O GLN E 315 N ILE E 309 SHEET 5 AB212 ALA E 329 SER E 334 -1 O HIS E 330 N THR E 297 SHEET 6 AB212 ILE E 358 PHE E 361 0 SHEET 7 AB212 HIS E 374 CYS E 378 0 SHEET 8 AB212 GLU E 381 CYS E 385 -1 O PHE E 383 N PHE E 376 SHEET 9 AB212 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 10 AB212 SER E 413 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 11 AB212 GLY E 441 ARG E 456 -1 O THR E 450 N LEU E 288 SHEET 12 AB212 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AB3 4 GLN C 3 GLY C 8 0 SHEET 2 AB3 4 LEU C 18 SER C 25 -1 O SER C 21 N THR C 7 SHEET 3 AB3 4 THR C 77 MET C 82 -1 O LEU C 78 N CYS C 22 SHEET 4 AB3 4 PHE C 67 ASP C 72 -1 N ASP C 72 O THR C 77 SHEET 1 AB4 6 MET C 34 GLN C 39 0 SHEET 2 AB4 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 3 AB4 6 THR C 57 TYR C 59 -1 O PHE C 58 N LEU C 50 SHEET 4 AB4 6 ALA C 88 THR C 94 -1 O VAL C 89 N GLN C 39 SHEET 5 AB4 6 PHE C 102 TRP C 103 -1 O PHE C 102 N THR C 94 SHEET 6 AB4 6 ALA C 107 VAL C 109 -1 O VAL C 109 N ALA C 88 SHEET 1 AB5 6 SER D 9 GLY D 13 0 SHEET 2 AB5 6 VAL D 33 GLN D 38 0 SHEET 3 AB5 6 LYS D 45 ILE D 48 -1 O LYS D 45 N GLN D 37 SHEET 4 AB5 6 ALA D 84 TYR D 91 -1 O ASP D 85 N GLN D 38 SHEET 5 AB5 6 TYR D 96 PHE D 98 -1 O ILE D 97 N ALA D 90 SHEET 6 AB5 6 THR D 102 VAL D 106 -1 O LEU D 104 N ALA D 84 SHEET 1 AB6 3 VAL D 19 THR D 24 0 SHEET 2 AB6 3 THR D 70 ILE D 75 -1 O ALA D 71 N CYS D 23 SHEET 3 AB6 3 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AB7 4 GLN H 3 SER H 7 0 SHEET 2 AB7 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AB7 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AB7 4 VAL H 67 ASP H 72 -1 N THR H 68 O LYS H 81 SHEET 1 AB8 7 LEU H 11 VAL H 12 0 SHEET 2 AB8 7 TRP H 34 SER H 40 0 SHEET 3 AB8 7 LYS H 43 ILE H 51 -1 O ILE H 51 N TRP H 35 SHEET 4 AB8 7 ALA H 57 TYR H 59 -1 O ASN H 58 N THR H 50 SHEET 5 AB8 7 ALA H 88 ILE H 97 -1 O ASN H 95 N TRP H 34 SHEET 6 AB8 7 PHE H 100J TRP H 103 -1 O CYS H 100K N ALA H 96 SHEET 7 AB8 7 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 1 AB9 4 LEU L 4 SER L 7 0 SHEET 2 AB9 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB9 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB9 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AC1 7 SER L 10 VAL L 13 0 SHEET 2 AC1 7 MET L 33 GLN L 38 0 SHEET 3 AC1 7 PRO L 44 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 4 AC1 7 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 5 AC1 7 ALA L 84 GLN L 90 -1 O GLN L 89 N HIS L 34 SHEET 6 AC1 7 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 7 AC1 7 THR L 102 LEU L 106 -1 O LEU L 104 N ALA L 84 SHEET 1 AC2 2 ASP L 27C ILE L 27D 0 SHEET 2 AC2 2 ASP L 30 SER L 31 -1 O ASP L 30 N ILE L 27D SHEET 1 AC3 3 LEU A 494 THR A 499 0 SHEET 2 AC3 3 TRP A 35 TYR A 40 -1 N TRP A 35 O THR A 499 SHEET 3 AC3 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AC4 5 TRP A 45 ASP A 47 0 SHEET 2 AC4 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AC4 5 PHE A 223 LYS A 227 -1 N ALA A 224 O VAL A 489 SHEET 4 AC4 5 SER A 243 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AC4 5 ILE A 84 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AC5 2 PHE A 53 ALA A 55 0 SHEET 2 AC5 2 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AC6 2 GLU A 91 ASN A 94 0 SHEET 2 AC6 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AC7 5 LYS A 169 PHE A 176 0 SHEET 2 AC7 5 LYS A 155 THR A 162 -1 N LYS A 155 O PHE A 176 SHEET 3 AC7 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AC7 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AC7 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AC8 3 THR A 202 GLN A 203 0 SHEET 2 AC8 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AC8 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AC912 LEU A 259 LEU A 261 0 SHEET 2 AC912 ILE A 271 SER A 274 0 SHEET 3 AC912 ILE A 284 GLY A 312 -1 O GLN A 287 N ILE A 271 SHEET 4 AC912 GLN A 315 ILE A 323A-1 O GLN A 315 N ILE A 309 SHEET 5 AC912 ALA A 329 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 6 AC912 ILE A 358 PHE A 361 0 SHEET 7 AC912 HIS A 374 CYS A 378 0 SHEET 8 AC912 GLU A 381 CYS A 385 -1 O GLU A 381 N CYS A 378 SHEET 9 AC912 SER A 393 ILE A 396 -1 O TRP A 395 N ILE A 359 SHEET 10 AC912 SER A 413 ILE A 420 -1 O ARG A 419 N TYR A 384 SHEET 11 AC912 GLY A 441 ARG A 456 -1 O THR A 450 N LEU A 288 SHEET 12 AC912 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AD1 4 GLN M 3 THR M 7 0 SHEET 2 AD1 4 LEU M 18 SER M 25 -1 O SER M 21 N THR M 7 SHEET 3 AD1 4 THR M 77 MET M 82 -1 O LEU M 78 N CYS M 22 SHEET 4 AD1 4 THR M 68 ASP M 72 -1 N ASP M 72 O THR M 77 SHEET 1 AD2 6 MET M 34 GLN M 39 0 SHEET 2 AD2 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 3 AD2 6 THR M 57 TYR M 59 -1 O PHE M 58 N LEU M 50 SHEET 4 AD2 6 ALA M 88 GLY M 95 -1 O ALA M 93 N SER M 35 SHEET 5 AD2 6 PHE M 100H TRP M 103 -1 O PHE M 102 N THR M 94 SHEET 6 AD2 6 ALA M 107 VAL M 109 -1 O ALA M 107 N TYR M 90 SHEET 1 AD3 6 SER N 9 GLY N 13 0 SHEET 2 AD3 6 VAL N 33 GLN N 38 0 SHEET 3 AD3 6 LYS N 45 ILE N 48 -1 O MET N 47 N TRP N 35 SHEET 4 AD3 6 ALA N 84 TYR N 91 -1 O ASP N 85 N GLN N 38 SHEET 5 AD3 6 TYR N 96 PHE N 98 -1 O ILE N 97 N ALA N 90 SHEET 6 AD3 6 THR N 102 VAL N 106 -1 O LEU N 104 N ALA N 84 SHEET 1 AD4 3 VAL N 19 THR N 24 0 SHEET 2 AD4 3 THR N 70 ILE N 75 -1 O LEU N 73 N ILE N 21 SHEET 3 AD4 3 PHE N 62 SER N 67 -1 N SER N 67 O THR N 70 SHEET 1 AD5 3 LEU J 494 THR J 499 0 SHEET 2 AD5 3 TRP J 35 TYR J 40 -1 N TRP J 35 O THR J 499 SHEET 3 AD5 3 ILE K 603 PRO K 609 -1 O CYS K 604 N VAL J 38 SHEET 1 AD6 5 TRP J 45 ASP J 47 0 SHEET 2 AD6 5 TYR J 486 ILE J 491 -1 O LYS J 490 N LYS J 46 SHEET 3 AD6 5 PHE J 223 LYS J 227 -1 N LEU J 226 O LYS J 487 SHEET 4 AD6 5 SER J 243 VAL J 245 -1 O VAL J 245 N ILE J 225 SHEET 5 AD6 5 GLU J 83 HIS J 85 -1 N ILE J 84 O THR J 244 SHEET 1 AD7 4 VAL J 75 PRO J 76 0 SHEET 2 AD7 4 PHE J 53 SER J 56 1 N SER J 56 O VAL J 75 SHEET 3 AD7 4 ILE J 215 CYS J 218 -1 O CYS J 218 N PHE J 53 SHEET 4 AD7 4 CYS J 247 ILE J 251 -1 O THR J 248 N TYR J 217 SHEET 1 AD8 2 GLU J 91 ASN J 94 0 SHEET 2 AD8 2 THR J 236 CYS J 239 -1 O GLY J 237 N PHE J 93 SHEET 1 AD9 5 LYS J 169 PHE J 176 0 SHEET 2 AD9 5 LYS J 155 THR J 162 -1 N PHE J 159 O VAL J 172 SHEET 3 AD9 5 LEU J 129 ASN J 133 -1 N GLN J 130 O SER J 158 SHEET 4 AD9 5 GLU J 190 LEU J 193 -1 O TYR J 191 N LEU J 129 SHEET 5 AD9 5 VAL J 181 GLN J 183 -1 N VAL J 182 O ARG J 192 SHEET 1 AE1 3 THR J 202 GLN J 203 0 SHEET 2 AE1 3 MET J 434 TYR J 435 1 O TYR J 435 N THR J 202 SHEET 3 AE1 3 ILE J 423 ILE J 424 -1 N ILE J 424 O MET J 434 SHEET 1 AE212 LEU J 259 LEU J 261 0 SHEET 2 AE212 ILE J 271 SER J 274 0 SHEET 3 AE212 ILE J 284 GLY J 312 -1 O GLN J 287 N ILE J 271 SHEET 4 AE212 GLN J 315 ILE J 323A-1 O GLN J 315 N ILE J 309 SHEET 5 AE212 HIS J 330 SER J 334 -1 O HIS J 330 N THR J 297 SHEET 6 AE212 ILE J 358 PHE J 361 0 SHEET 7 AE212 HIS J 374 CYS J 378 0 SHEET 8 AE212 GLU J 381 CYS J 385 -1 O GLU J 381 N CYS J 378 SHEET 9 AE212 SER J 393 ILE J 396 -1 O SER J 393 N PHE J 361 SHEET 10 AE212 SER J 413 ILE J 420 -1 O ARG J 419 N TYR J 384 SHEET 11 AE212 GLY J 441 ARG J 456 -1 O THR J 450 N LEU J 288 SHEET 12 AE212 THR J 465 PRO J 470 -1 O ARG J 469 N THR J 455 SSBOND 1 CYS G 22 CYS G 92 1555 1555 2.04 SSBOND 2 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 3 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 4 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 5 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 6 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 7 CYS E 218 CYS E 247 1555 1555 2.05 SSBOND 8 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 9 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 10 CYS E 378 CYS E 445 1555 1555 2.02 SSBOND 11 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 12 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 13 CYS F 598 CYS F 604 1555 1555 2.02 SSBOND 14 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 15 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 17 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 18 CYS A 54 CYS A 74 1555 1555 2.02 SSBOND 19 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 20 CYS A 126 CYS A 196 1555 1555 2.04 SSBOND 21 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 22 CYS A 218 CYS A 247 1555 1555 2.05 SSBOND 23 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 24 CYS A 296 CYS A 331 1555 1555 1.99 SSBOND 25 CYS A 378 CYS A 445 1555 1555 2.02 SSBOND 26 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 27 CYS A 501 CYS B 605 1555 1555 2.02 SSBOND 28 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 29 CYS M 22 CYS M 92 1555 1555 2.04 SSBOND 30 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 31 CYS J 54 CYS J 74 1555 1555 2.01 SSBOND 32 CYS J 119 CYS J 205 1555 1555 2.03 SSBOND 33 CYS J 126 CYS J 196 1555 1555 2.04 SSBOND 34 CYS J 131 CYS J 157 1555 1555 2.03 SSBOND 35 CYS J 218 CYS J 247 1555 1555 2.04 SSBOND 36 CYS J 228 CYS J 239 1555 1555 2.04 SSBOND 37 CYS J 296 CYS J 331 1555 1555 2.03 SSBOND 38 CYS J 378 CYS J 445 1555 1555 2.03 SSBOND 39 CYS J 385 CYS J 418 1555 1555 2.03 SSBOND 40 CYS J 501 CYS K 605 1555 1555 2.02 SSBOND 41 CYS K 598 CYS K 604 1555 1555 2.02 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 610 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 604 1555 1555 1.43 LINK ND2 ASN E 234 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN E 276 C1 NAG E 606 1555 1555 1.45 LINK ND2 ASN E 295 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 608 1555 1555 1.45 LINK ND2 ASN E 332 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG Q 1 1555 1555 1.45 LINK ND2 ASN E 448 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.45 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG A 610 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 604 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG S 1 1555 1555 1.45 LINK ND2 ASN A 276 C1 NAG A 606 1555 1555 1.45 LINK ND2 ASN A 295 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 608 1555 1555 1.45 LINK ND2 ASN A 332 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG T 1 1555 1555 1.45 LINK ND2 ASN A 448 C1 NAG A 609 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN J 88 C1 NAG J 601 1555 1555 1.44 LINK ND2 ASN J 133 C1 NAG J 610 1555 1555 1.44 LINK ND2 ASN J 156 C1 NAG J 602 1555 1555 1.44 LINK ND2 ASN J 160 C1 NAG J 603 1555 1555 1.44 LINK ND2 ASN J 197 C1 NAG J 604 1555 1555 1.44 LINK ND2 ASN J 234 C1 NAG J 605 1555 1555 1.44 LINK ND2 ASN J 262 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN J 276 C1 NAG J 606 1555 1555 1.45 LINK ND2 ASN J 295 C1 NAG J 607 1555 1555 1.44 LINK ND2 ASN J 301 C1 NAG J 608 1555 1555 1.44 LINK ND2 ASN J 332 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN J 386 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN J 448 C1 NAG J 609 1555 1555 1.43 LINK ND2 ASN K 611 C1 NAG K 701 1555 1555 1.45 LINK ND2 ASN K 637 C1 NAG K 702 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O3 BMA O 3 C1 MAN O 4 1555 1555 1.44 LINK O6 BMA O 3 C1 MAN O 6 1555 1555 1.44 LINK O2 MAN O 4 C1 MAN O 5 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O3 BMA P 3 C1 MAN P 4 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.39 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.39 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.39 LINK O6 BMA R 3 C1 MAN R 6 1555 1555 1.40 LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.39 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.44 LINK O6 BMA U 3 C1 MAN U 6 1555 1555 1.45 LINK O2 MAN U 4 C1 MAN U 5 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.45 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -1.76 CISPEP 2 ASP L 76 PRO L 77 0 -7.54 CISPEP 3 ASP L 94 PRO L 95 0 -0.74 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