HEADER VIRAL PROTEIN 12-DEC-24 9MI0 TITLE 61-12A01 FAB IN COMPLEX WITH HIV-1 GT1.1 V4.1 SOSIP ENV TRIMER AND TITLE 2 RM20A3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: 61_12A01 HEAVY CHAIN FV; COMPND 3 CHAIN: H, K, P; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 61_12A01 KAPPA CHAIN FV; COMPND 7 CHAIN: L, N, R; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RM20A3 HEAVY CHAIN FV; COMPND 11 CHAIN: G, J, O; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: RM20A3 LIGHT CHAIN FV; COMPND 15 CHAIN: I, M, Q; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: GT1.1 V4.1 SOSIP GP120; COMPND 19 CHAIN: A, C, E; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 23 CHAIN: B, D, F; COMPND 24 FRAGMENT: UNP RESIDUES 509-611; COMPND 25 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 13 ORGANISM_TAXID: 9544; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 18 ORGANISM_TAXID: 9544; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 23 ORGANISM_TAXID: 11676; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 MOL_ID: 6; SOURCE 27 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 28 ORGANISM_TAXID: 11676; SOURCE 29 GENE: ENV; SOURCE 30 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, SOSIP, GERMLINE TARGETING, VRC01, CLINICAL TRIAL, HUMAN, KEYWDS 2 PRECURSOR ANTIBODY, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.PHULERA,G.OZOROWSKI,A.B.WARD REVDAT 1 21-MAY-25 9MI0 0 JRNL AUTH T.G.CANIELS,M.PRABHAKARAN,G.OZOROWSKI,K.J.MACPHEE,W.WU, JRNL AUTH 2 K.VAN DER STRATEN,S.AGRAWAL,R.DERKING,E.I.M.M.REISS, JRNL AUTH 3 K.MILLARD,M.TURROJA,A.DESROSIERS,J.BETHONY,E.MALKIN, JRNL AUTH 4 M.H.LIESDEK,A.VAN DER VEEN,M.KLOUWENS,S.PHULERA,I.A.WILSON, JRNL AUTH 5 A.B.WARD JRNL TITL PRECISE TARGETING OF HIV BROADLY NEUTRALIZING ANTIBODY JRNL TITL 2 PRECURSORS IN HUMANS JRNL REF SCIENCE 2025 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADV5572 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, UCSF CHIMERAX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, PHENIX 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) : 2.800 REMARK 3 NUMBER OF PARTICLES : 165097 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 9MI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290995. 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 : 61-12A01 FAB IN COMPLEX WITH REMARK 245 HIV-1 GT1.1 V4.1 SOSIP ENV REMARK 245 TRIMER AND RM20A3 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.10 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 : 3867 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) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4520.00 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, G, I, A, B, K, N, J, M, REMARK 350 AND CHAINS: C, D, P, R, O, Q, E, F, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g 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 GLN H 1 REMARK 465 SER G 112 REMARK 465 SER G 113 REMARK 465 LEU I 107 REMARK 465 GLY I 108 REMARK 465 GLN I 109 REMARK 465 PRO I 110 REMARK 465 LYS I 111 REMARK 465 ALA I 112 REMARK 465 SER I 113 REMARK 465 PRO I 114 REMARK 465 THR I 115 REMARK 465 VAL I 116 REMARK 465 THR I 117 REMARK 465 LEU I 118 REMARK 465 PHE I 119 REMARK 465 PRO I 120 REMARK 465 PRO I 121 REMARK 465 SER I 122 REMARK 465 SER I 123 REMARK 465 GLU I 124 REMARK 465 GLU I 125 REMARK 465 LEU I 126 REMARK 465 MET A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 MET A -1 REMARK 465 LYS A 0 REMARK 465 ARG A 1 REMARK 465 GLY A 2 REMARK 465 LEU A 3 REMARK 465 CYS A 4 REMARK 465 CYS A 5 REMARK 465 VAL A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 CYS A 10 REMARK 465 GLY A 11 REMARK 465 ALA A 12 REMARK 465 VAL A 13 REMARK 465 PHE A 14 REMARK 465 VAL A 15 REMARK 465 SER A 16 REMARK 465 PRO A 17 REMARK 465 SER A 18 REMARK 465 GLN A 19 REMARK 465 GLU A 20 REMARK 465 ILE A 21 REMARK 465 HIS A 22 REMARK 465 ALA A 23 REMARK 465 ARG A 24 REMARK 465 PHE A 25 REMARK 465 ARG A 26 REMARK 465 ARG A 27 REMARK 465 GLY A 28 REMARK 465 ALA A 29 REMARK 465 ARG A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 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 ASN A 411 REMARK 465 VAL A 505 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 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 GLN K 1 REMARK 465 SER J 112 REMARK 465 SER J 113 REMARK 465 LEU M 107 REMARK 465 GLY M 108 REMARK 465 GLN M 109 REMARK 465 PRO M 110 REMARK 465 LYS M 111 REMARK 465 ALA M 112 REMARK 465 SER M 113 REMARK 465 PRO M 114 REMARK 465 THR M 115 REMARK 465 VAL M 116 REMARK 465 THR M 117 REMARK 465 LEU M 118 REMARK 465 PHE M 119 REMARK 465 PRO M 120 REMARK 465 PRO M 121 REMARK 465 SER M 122 REMARK 465 SER M 123 REMARK 465 GLU M 124 REMARK 465 GLU M 125 REMARK 465 LEU M 126 REMARK 465 MET C -4 REMARK 465 ASP C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 LYS C 0 REMARK 465 ARG C 1 REMARK 465 GLY C 2 REMARK 465 LEU C 3 REMARK 465 CYS C 4 REMARK 465 CYS C 5 REMARK 465 VAL C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 LEU C 9 REMARK 465 CYS C 10 REMARK 465 GLY C 11 REMARK 465 ALA C 12 REMARK 465 VAL C 13 REMARK 465 PHE C 14 REMARK 465 VAL C 15 REMARK 465 SER C 16 REMARK 465 PRO C 17 REMARK 465 SER C 18 REMARK 465 GLN C 19 REMARK 465 GLU C 20 REMARK 465 ILE C 21 REMARK 465 HIS C 22 REMARK 465 ALA C 23 REMARK 465 ARG C 24 REMARK 465 PHE C 25 REMARK 465 ARG C 26 REMARK 465 ARG C 27 REMARK 465 GLY C 28 REMARK 465 ALA C 29 REMARK 465 ARG C 30 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 ASN C 411 REMARK 465 VAL C 505 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 REMARK 465 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 GLN P 1 REMARK 465 SER O 112 REMARK 465 SER O 113 REMARK 465 LEU Q 107 REMARK 465 GLY Q 108 REMARK 465 GLN Q 109 REMARK 465 PRO Q 110 REMARK 465 LYS Q 111 REMARK 465 ALA Q 112 REMARK 465 SER Q 113 REMARK 465 PRO Q 114 REMARK 465 THR Q 115 REMARK 465 VAL Q 116 REMARK 465 THR Q 117 REMARK 465 LEU Q 118 REMARK 465 PHE Q 119 REMARK 465 PRO Q 120 REMARK 465 PRO Q 121 REMARK 465 SER Q 122 REMARK 465 SER Q 123 REMARK 465 GLU Q 124 REMARK 465 GLU Q 125 REMARK 465 LEU Q 126 REMARK 465 MET E -4 REMARK 465 ASP E -3 REMARK 465 ALA E -2 REMARK 465 MET E -1 REMARK 465 LYS E 0 REMARK 465 ARG E 1 REMARK 465 GLY E 2 REMARK 465 LEU E 3 REMARK 465 CYS E 4 REMARK 465 CYS E 5 REMARK 465 VAL E 6 REMARK 465 LEU E 7 REMARK 465 LEU E 8 REMARK 465 LEU E 9 REMARK 465 CYS E 10 REMARK 465 GLY E 11 REMARK 465 ALA E 12 REMARK 465 VAL E 13 REMARK 465 PHE E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 PRO E 17 REMARK 465 SER E 18 REMARK 465 GLN E 19 REMARK 465 GLU E 20 REMARK 465 ILE E 21 REMARK 465 HIS E 22 REMARK 465 ALA E 23 REMARK 465 ARG E 24 REMARK 465 PHE E 25 REMARK 465 ARG E 26 REMARK 465 ARG E 27 REMARK 465 GLY E 28 REMARK 465 ALA E 29 REMARK 465 ARG E 30 REMARK 465 ALA E 31 REMARK 465 GLU E 32 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 ASN E 411 REMARK 465 VAL E 505 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 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 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 SG CYS A 54 SG CYS A 74 1.32 REMARK 500 SG CYS C 54 SG CYS C 74 1.32 REMARK 500 SG CYS E 54 SG CYS E 74 1.32 REMARK 500 SG CYS A 54 CB CYS A 74 1.58 REMARK 500 SG CYS C 54 CB CYS C 74 1.58 REMARK 500 SG CYS E 54 CB CYS E 74 1.58 REMARK 500 OG1 THR E 37 OG1 THR E 499 2.03 REMARK 500 OG1 THR C 37 OG1 THR C 499 2.03 REMARK 500 OG1 THR A 37 OG1 THR A 499 2.03 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 A 54 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 CYS C 54 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 CYS E 54 CA - CB - SG ANGL. DEV. = 6.9 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 GLU L 81 49.34 -87.39 REMARK 500 ASP L 82 17.56 -140.94 REMARK 500 ALA L 84 -169.84 -161.56 REMARK 500 TYR L 91 -118.06 62.04 REMARK 500 VAL I 51 -63.95 70.35 REMARK 500 LEU A 122 58.39 -92.81 REMARK 500 GLN A 258 -9.36 72.66 REMARK 500 ASN A 392 41.96 -144.40 REMARK 500 TRP A 427 32.60 71.31 REMARK 500 ASN B 625 19.24 -140.36 REMARK 500 GLU N 81 49.33 -87.38 REMARK 500 ASP N 82 17.61 -140.96 REMARK 500 ALA N 84 -169.83 -161.57 REMARK 500 TYR N 91 -118.07 62.08 REMARK 500 VAL M 51 -63.99 70.39 REMARK 500 LEU C 122 58.40 -92.84 REMARK 500 GLN C 258 -9.40 72.69 REMARK 500 ASN C 392 41.89 -144.37 REMARK 500 TRP C 427 32.59 71.30 REMARK 500 ASN D 625 19.26 -140.35 REMARK 500 GLU R 81 49.34 -87.38 REMARK 500 ASP R 82 17.54 -140.95 REMARK 500 ALA R 84 -169.85 -161.53 REMARK 500 TYR R 91 -118.05 62.08 REMARK 500 VAL Q 51 -63.93 70.39 REMARK 500 LEU E 122 58.41 -92.80 REMARK 500 GLN E 258 -9.38 72.69 REMARK 500 ASN E 392 41.93 -144.39 REMARK 500 TRP E 427 32.58 71.34 REMARK 500 ASN F 625 19.18 -140.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG L 24 0.25 SIDE CHAIN REMARK 500 ARG I 94 0.12 SIDE CHAIN REMARK 500 ARG N 24 0.25 SIDE CHAIN REMARK 500 ARG M 94 0.12 SIDE CHAIN REMARK 500 ARG R 24 0.25 SIDE CHAIN REMARK 500 ARG Q 94 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48283 RELATED DB: EMDB REMARK 900 61-12A01 FAB IN COMPLEX WITH HIV-1 GT1.1 V4.1 SOSIP ENV TRIMER AND REMARK 900 RM20A3 FAB DBREF 9MI0 H 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 L 1 107 PDB 9MI0 9MI0 1 107 DBREF 9MI0 G 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 I 3 126 PDB 9MI0 9MI0 3 126 DBREF 9MI0 A -4 513 PDB 9MI0 9MI0 -4 513 DBREF 9MI0 B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9MI0 K 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 N 1 107 PDB 9MI0 9MI0 1 107 DBREF 9MI0 J 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 M 3 126 PDB 9MI0 9MI0 3 126 DBREF 9MI0 C -4 513 PDB 9MI0 9MI0 -4 513 DBREF 9MI0 D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 9MI0 P 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 R 1 107 PDB 9MI0 9MI0 1 107 DBREF 9MI0 O 1 113 PDB 9MI0 9MI0 1 113 DBREF 9MI0 Q 3 126 PDB 9MI0 9MI0 3 126 DBREF 9MI0 E -4 513 PDB 9MI0 9MI0 -4 513 DBREF 9MI0 F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 9MI0 PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MI0 CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9MI0 PRO D 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MI0 CYS D 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9MI0 PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9MI0 CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 H 123 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS GLN SEQRES 2 H 123 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 123 TYR THR PHE SER ASP HIS PHE MET HIS TRP VAL ARG GLN SEQRES 4 H 123 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 123 PRO LYS SER GLY GLY PRO ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 123 GLY ARG VAL THR MET THR ARG ASP ARG SER ILE SER THR SEQRES 7 H 123 ALA TYR MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 H 123 ALA ILE TYR TYR CYS ALA ARG PRO MET HIS ASP TYR ASP SEQRES 9 H 123 ASP HIS ASP TRP TYR PHE ASP LEU TRP GLY ARG GLY THR SEQRES 10 H 123 LEU VAL THR VAL SER SER SEQRES 1 L 104 VAL SER VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 104 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 104 GLN THR VAL GLY SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 104 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 104 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 104 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 104 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 104 TYR GLU ALA PHE GLY GLN GLY THR LYS VAL GLU ILE LYS 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 A 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 A 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 A 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 A 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 A 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 A 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 A 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 A 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 A 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 A 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 A 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 A 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 A 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 A 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 A 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 A 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 A 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 A 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 A 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 A 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 A 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 A 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 A 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 A 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 A 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 A 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 A 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 A 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 A 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 A 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 A 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 A 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 A 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 A 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 A 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 A 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 A 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 A 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 A 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 A 509 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 PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU 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 K 123 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS GLN SEQRES 2 K 123 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 K 123 TYR THR PHE SER ASP HIS PHE MET HIS TRP VAL ARG GLN SEQRES 4 K 123 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 K 123 PRO LYS SER GLY GLY PRO ASN TYR ALA GLN LYS PHE GLN SEQRES 6 K 123 GLY ARG VAL THR MET THR ARG ASP ARG SER ILE SER THR SEQRES 7 K 123 ALA TYR MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 K 123 ALA ILE TYR TYR CYS ALA ARG PRO MET HIS ASP TYR ASP SEQRES 9 K 123 ASP HIS ASP TRP TYR PHE ASP LEU TRP GLY ARG GLY THR SEQRES 10 K 123 LEU VAL THR VAL SER SER SEQRES 1 N 104 VAL SER VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 N 104 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 N 104 GLN THR VAL GLY SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 N 104 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 N 104 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 N 104 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 N 104 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 N 104 TYR GLU ALA PHE GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 J 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 J 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 J 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 J 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 J 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 J 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 J 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 J 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 J 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 J 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 M 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 M 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 M 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 M 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 M 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 M 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 M 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 M 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 M 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 M 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 C 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 C 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 C 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 C 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 C 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 C 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 C 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 C 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 C 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 C 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 C 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 C 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 C 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 C 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 C 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 C 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 C 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 C 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 C 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 C 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 C 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 C 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 C 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 C 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 C 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 C 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 C 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 C 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 C 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 C 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 C 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 C 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 C 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 C 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 C 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 C 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 C 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 C 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 C 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 C 509 ARG ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 P 123 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS GLN SEQRES 2 P 123 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 P 123 TYR THR PHE SER ASP HIS PHE MET HIS TRP VAL ARG GLN SEQRES 4 P 123 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 P 123 PRO LYS SER GLY GLY PRO ASN TYR ALA GLN LYS PHE GLN SEQRES 6 P 123 GLY ARG VAL THR MET THR ARG ASP ARG SER ILE SER THR SEQRES 7 P 123 ALA TYR MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 P 123 ALA ILE TYR TYR CYS ALA ARG PRO MET HIS ASP TYR ASP SEQRES 9 P 123 ASP HIS ASP TRP TYR PHE ASP LEU TRP GLY ARG GLY THR SEQRES 10 P 123 LEU VAL THR VAL SER SER SEQRES 1 R 104 VAL SER VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 R 104 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 R 104 GLN THR VAL GLY SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 R 104 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 R 104 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 R 104 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 R 104 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 R 104 TYR GLU ALA PHE GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 O 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 O 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 O 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 O 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 O 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 O 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 O 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 O 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 O 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 O 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 Q 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 Q 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 Q 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 Q 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 Q 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 Q 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 Q 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 Q 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 Q 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 Q 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 E 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 E 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 E 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 E 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 E 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 E 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 E 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 E 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 E 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 E 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 E 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 E 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 E 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 E 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 E 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 E 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 E 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 E 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 E 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 E 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 E 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 E 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 E 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 E 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 E 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 E 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 E 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 E 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 E 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 E 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 E 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 E 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 E 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 E 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 E 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 E 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 E 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 E 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 E 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 E 509 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 PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU 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 HET NAG S 1 14 HET NAG S 2 14 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 NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET MAN e 4 11 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 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 B 701 14 HET NAG B 702 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG C 606 14 HET NAG D 701 14 HET NAG D 702 14 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 F 701 14 HET NAG F 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 19 NAG 54(C8 H15 N O6) FORMUL 21 BMA 3(C6 H12 O6) FORMUL 21 MAN 3(C6 H12 O6) HELIX 1 AA1 GLN H 61 GLN H 64 5 4 HELIX 2 AA2 GLU L 79 PHE L 83 5 5 HELIX 3 AA3 THR G 28 PHE G 32 5 5 HELIX 4 AA4 ASP G 61 LYS G 64 5 4 HELIX 5 AA5 ARG G 83 THR G 87 5 5 HELIX 6 AA6 GLN I 79 GLU I 83 5 5 HELIX 7 AA7 ASP A 57 LYS A 64 1 8 HELIX 8 AA8 ASN A 98 LYS A 117 1 20 HELIX 9 AA9 LYS A 335 GLY A 354 1 20 HELIX 10 AB1 ASP A 368 THR A 373 1 6 HELIX 11 AB2 ASN A 425 ARG A 429 5 5 HELIX 12 AB3 ASP A 474 ASN A 478 5 5 HELIX 13 AB4 THR B 529 SER B 534 1 6 HELIX 14 AB5 THR B 536 ARG B 542 1 7 HELIX 15 AB6 VAL B 570 ILE B 595 1 26 HELIX 16 AB7 ASN B 618 ASN B 625 1 8 HELIX 17 AB8 THR B 627 SER B 636 1 10 HELIX 18 AB9 TYR B 638 GLU B 648 1 11 HELIX 19 AC1 GLU B 648 LEU B 663 1 16 HELIX 20 AC2 GLN K 61 GLN K 64 5 4 HELIX 21 AC3 GLU N 79 PHE N 83 5 5 HELIX 22 AC4 THR J 28 PHE J 32 5 5 HELIX 23 AC5 ASP J 61 LYS J 64 5 4 HELIX 24 AC6 ARG J 83 THR J 87 5 5 HELIX 25 AC7 GLN M 79 GLU M 83 5 5 HELIX 26 AC8 ASP C 57 LYS C 64 1 8 HELIX 27 AC9 ASN C 98 LYS C 117 1 20 HELIX 28 AD1 LYS C 335 GLY C 354 1 20 HELIX 29 AD2 ASP C 368 THR C 373 1 6 HELIX 30 AD3 ASN C 425 ARG C 429 5 5 HELIX 31 AD4 ASP C 474 ASN C 478 5 5 HELIX 32 AD5 THR D 529 SER D 534 1 6 HELIX 33 AD6 THR D 536 ARG D 542 1 7 HELIX 34 AD7 VAL D 570 ILE D 595 1 26 HELIX 35 AD8 ASN D 618 ASN D 625 1 8 HELIX 36 AD9 THR D 627 SER D 636 1 10 HELIX 37 AE1 TYR D 638 GLU D 648 1 11 HELIX 38 AE2 GLU D 648 LEU D 663 1 16 HELIX 39 AE3 GLN P 61 GLN P 64 5 4 HELIX 40 AE4 GLU R 79 PHE R 83 5 5 HELIX 41 AE5 THR O 28 PHE O 32 5 5 HELIX 42 AE6 ASP O 61 LYS O 64 5 4 HELIX 43 AE7 ARG O 83 THR O 87 5 5 HELIX 44 AE8 GLN Q 79 GLU Q 83 5 5 HELIX 45 AE9 ASP E 57 LYS E 64 1 8 HELIX 46 AF1 ASN E 98 LYS E 117 1 20 HELIX 47 AF2 LYS E 335 GLY E 354 1 20 HELIX 48 AF3 ASP E 368 THR E 373 1 6 HELIX 49 AF4 ASN E 425 ARG E 429 5 5 HELIX 50 AF5 ASP E 474 ASN E 478 5 5 HELIX 51 AF6 THR F 529 SER F 534 1 6 HELIX 52 AF7 THR F 536 ARG F 542 1 7 HELIX 53 AF8 VAL F 570 ILE F 595 1 26 HELIX 54 AF9 ASN F 618 ASN F 625 1 8 HELIX 55 AG1 THR F 627 SER F 636 1 10 HELIX 56 AG2 TYR F 638 GLU F 648 1 11 HELIX 57 AG3 GLU F 648 LEU F 663 1 16 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 LEU H 108 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 AA2 6 ALA H 88 ALA H 93 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 PRO H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AA3 4 LEU L 4 THR L 5 0 SHEET 2 AA3 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA4 5 THR L 10 LEU L 13 0 SHEET 2 AA4 5 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA4 5 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA4 5 ALA L 34 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA4 5 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37 SHEET 1 AA5 4 THR L 10 LEU L 13 0 SHEET 2 AA5 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA5 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA5 4 ALA L 97 PHE L 98 -1 O ALA L 97 N GLN L 90 SHEET 1 AA6 4 GLN G 3 THR G 7 0 SHEET 2 AA6 4 LEU G 18 SER G 25 -1 O ARG G 23 N VAL G 5 SHEET 3 AA6 4 THR G 77 MET G 82 -1 O MET G 82 N LEU G 18 SHEET 4 AA6 4 PHE G 67 ASP G 72 -1 N SER G 70 O SER G 79 SHEET 1 AA7 5 THR G 57 TYR G 59 0 SHEET 2 AA7 5 LEU G 45 ILE G 51 -1 N LEU G 50 O PHE G 58 SHEET 3 AA7 5 MET G 34 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 4 AA7 5 ALA G 88 GLY G 95 -1 O TYR G 91 N VAL G 37 SHEET 5 AA7 5 PHE G 100H PHE G 102 -1 O PHE G 102 N THR G 94 SHEET 1 AA8 5 THR G 57 TYR G 59 0 SHEET 2 AA8 5 LEU G 45 ILE G 51 -1 N LEU G 50 O PHE G 58 SHEET 3 AA8 5 MET G 34 GLN G 39 -1 N ARG G 38 O GLU G 46 SHEET 4 AA8 5 ALA G 88 GLY G 95 -1 O TYR G 91 N VAL G 37 SHEET 5 AA8 5 ALA G 107 VAL G 109 -1 O ALA G 107 N TYR G 90 SHEET 1 AA9 2 SER I 9 SER I 12 0 SHEET 2 AA9 2 ARG I 103 THR I 105 1 O ARG I 103 N VAL I 11 SHEET 1 AB1 3 SER I 18 THR I 24 0 SHEET 2 AB1 3 THR I 70 SER I 76 -1 O ALA I 71 N CYS I 23 SHEET 3 AB1 3 PHE I 62 SER I 67 -1 N SER I 67 O THR I 70 SHEET 1 AB2 4 LYS I 45 ILE I 48 0 SHEET 2 AB2 4 VAL I 33 GLN I 38 -1 N TRP I 35 O MET I 47 SHEET 3 AB2 4 ASP I 85 TYR I 91 -1 O ASP I 85 N GLN I 38 SHEET 4 AB2 4 TYR I 96 PHE I 98 -1 O ILE I 97 N ALA I 90 SHEET 1 AB3 3 LEU A 494 THR A 499 0 SHEET 2 AB3 3 TRP A 35 TYR A 40 -1 N TRP A 35 O THR A 499 SHEET 3 AB3 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AB4 5 TRP A 45 ASP A 47 0 SHEET 2 AB4 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AB4 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AB4 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AB4 5 GLU A 83 LEU A 86 -1 N ILE A 84 O THR A 244 SHEET 1 AB5 2 PHE A 53 ALA A 55 0 SHEET 2 AB5 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AB6 2 GLU A 91 ASN A 94 0 SHEET 2 AB6 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AB7 5 ARG A 169 TYR A 177 0 SHEET 2 AB7 5 LEU A 154 THR A 162 -1 N MET A 161 O GLN A 170 SHEET 3 AB7 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AB7 5 SER A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AB7 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AB8 3 THR A 202 GLN A 203 0 SHEET 2 AB8 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AB8 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AB9 7 LEU A 259 LEU A 261 0 SHEET 2 AB9 7 GLY A 441 ARG A 456 -1 O THR A 450 N LEU A 260 SHEET 3 AB9 7 ILE A 284 ASN A 302 -1 N CYS A 296 O CYS A 445 SHEET 4 AB9 7 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 5 AB9 7 SER A 413 LYS A 421 -1 O LEU A 416 N CYS A 331 SHEET 6 AB9 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AB9 7 HIS A 374 CYS A 378 -1 N HIS A 374 O CYS A 385 SHEET 1 AC1 6 MET A 271 ARG A 273 0 SHEET 2 AC1 6 ILE A 284 ASN A 302 -1 O LEU A 285 N ARG A 273 SHEET 3 AC1 6 GLY A 441 ARG A 456 -1 O CYS A 445 N CYS A 296 SHEET 4 AC1 6 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AC1 6 ILE A 358 PHE A 361 1 N ILE A 358 O GLU A 466 SHEET 6 AC1 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AC2 2 LYS A 305 ARG A 308 0 SHEET 2 AC2 2 TRP A 316 ALA A 319 -1 O PHE A 317 N ILE A 307 SHEET 1 AC3 4 GLN K 3 GLN K 6 0 SHEET 2 AC3 4 VAL K 18 SER K 25 -1 O SER K 25 N GLN K 3 SHEET 3 AC3 4 THR K 77 LEU K 82 -1 O ALA K 78 N CYS K 22 SHEET 4 AC3 4 VAL K 67 ASP K 72 -1 N THR K 70 O TYR K 79 SHEET 1 AC4 6 GLU K 10 LYS K 12 0 SHEET 2 AC4 6 LEU K 108 VAL K 111 1 O THR K 110 N GLU K 10 SHEET 3 AC4 6 ALA K 88 ALA K 93 -1 N ALA K 88 O VAL K 109 SHEET 4 AC4 6 MET K 34 GLN K 39 -1 N HIS K 35 O ALA K 93 SHEET 5 AC4 6 LEU K 45 ILE K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AC4 6 PRO K 57 TYR K 59 -1 O ASN K 58 N TRP K 50 SHEET 1 AC5 4 LEU N 4 THR N 5 0 SHEET 2 AC5 4 ALA N 19 ALA N 25 -1 O ARG N 24 N THR N 5 SHEET 3 AC5 4 ASP N 70 ILE N 75 -1 O LEU N 73 N LEU N 21 SHEET 4 AC5 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AC6 5 THR N 10 LEU N 13 0 SHEET 2 AC6 5 THR N 102 ILE N 106 1 O LYS N 103 N LEU N 11 SHEET 3 AC6 5 VAL N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AC6 5 ALA N 34 GLN N 38 -1 N GLN N 38 O VAL N 85 SHEET 5 AC6 5 ARG N 45 TYR N 49 -1 O ARG N 45 N GLN N 37 SHEET 1 AC7 4 THR N 10 LEU N 13 0 SHEET 2 AC7 4 THR N 102 ILE N 106 1 O LYS N 103 N LEU N 11 SHEET 3 AC7 4 VAL N 85 GLN N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AC7 4 ALA N 97 PHE N 98 -1 O ALA N 97 N GLN N 90 SHEET 1 AC8 4 GLN J 3 THR J 7 0 SHEET 2 AC8 4 LEU J 18 SER J 25 -1 O ARG J 23 N VAL J 5 SHEET 3 AC8 4 THR J 77 MET J 82 -1 O MET J 82 N LEU J 18 SHEET 4 AC8 4 PHE J 67 ASP J 72 -1 N SER J 70 O SER J 79 SHEET 1 AC9 5 THR J 57 TYR J 59 0 SHEET 2 AC9 5 LEU J 45 ILE J 51 -1 N LEU J 50 O PHE J 58 SHEET 3 AC9 5 MET J 34 GLN J 39 -1 N ARG J 38 O GLU J 46 SHEET 4 AC9 5 ALA J 88 GLY J 95 -1 O TYR J 91 N VAL J 37 SHEET 5 AC9 5 PHE J 100H PHE J 102 -1 O PHE J 102 N THR J 94 SHEET 1 AD1 5 THR J 57 TYR J 59 0 SHEET 2 AD1 5 LEU J 45 ILE J 51 -1 N LEU J 50 O PHE J 58 SHEET 3 AD1 5 MET J 34 GLN J 39 -1 N ARG J 38 O GLU J 46 SHEET 4 AD1 5 ALA J 88 GLY J 95 -1 O TYR J 91 N VAL J 37 SHEET 5 AD1 5 ALA J 107 VAL J 109 -1 O ALA J 107 N TYR J 90 SHEET 1 AD2 2 SER M 9 SER M 12 0 SHEET 2 AD2 2 ARG M 103 THR M 105 1 O ARG M 103 N VAL M 11 SHEET 1 AD3 3 SER M 18 THR M 24 0 SHEET 2 AD3 3 THR M 70 SER M 76 -1 O ALA M 71 N CYS M 23 SHEET 3 AD3 3 PHE M 62 SER M 67 -1 N SER M 67 O THR M 70 SHEET 1 AD4 4 LYS M 45 ILE M 48 0 SHEET 2 AD4 4 VAL M 33 GLN M 38 -1 N TRP M 35 O MET M 47 SHEET 3 AD4 4 ASP M 85 TYR M 91 -1 O ASP M 85 N GLN M 38 SHEET 4 AD4 4 TYR M 96 PHE M 98 -1 O ILE M 97 N ALA M 90 SHEET 1 AD5 3 LEU C 494 THR C 499 0 SHEET 2 AD5 3 TRP C 35 TYR C 40 -1 N TRP C 35 O THR C 499 SHEET 3 AD5 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AD6 5 TRP C 45 ASP C 47 0 SHEET 2 AD6 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AD6 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AD6 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AD6 5 GLU C 83 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AD7 2 PHE C 53 ALA C 55 0 SHEET 2 AD7 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AD8 2 GLU C 91 ASN C 94 0 SHEET 2 AD8 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AD9 5 ARG C 169 TYR C 177 0 SHEET 2 AD9 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AD9 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AD9 5 SER C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AD9 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AE1 3 THR C 202 GLN C 203 0 SHEET 2 AE1 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AE1 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AE2 7 LEU C 259 LEU C 261 0 SHEET 2 AE2 7 GLY C 441 ARG C 456 -1 O THR C 450 N LEU C 260 SHEET 3 AE2 7 ILE C 284 ASN C 302 -1 N CYS C 296 O CYS C 445 SHEET 4 AE2 7 HIS C 330 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 5 AE2 7 SER C 413 LYS C 421 -1 O LEU C 416 N CYS C 331 SHEET 6 AE2 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AE2 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AE3 6 MET C 271 ARG C 273 0 SHEET 2 AE3 6 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 3 AE3 6 GLY C 441 ARG C 456 -1 O CYS C 445 N CYS C 296 SHEET 4 AE3 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AE3 6 ILE C 358 PHE C 361 1 N ILE C 358 O GLU C 466 SHEET 6 AE3 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AE4 2 LYS C 305 ARG C 308 0 SHEET 2 AE4 2 TRP C 316 ALA C 319 -1 O PHE C 317 N ILE C 307 SHEET 1 AE5 4 GLN P 3 GLN P 6 0 SHEET 2 AE5 4 VAL P 18 SER P 25 -1 O SER P 25 N GLN P 3 SHEET 3 AE5 4 THR P 77 LEU P 82 -1 O ALA P 78 N CYS P 22 SHEET 4 AE5 4 VAL P 67 ASP P 72 -1 N THR P 70 O TYR P 79 SHEET 1 AE6 6 GLU P 10 LYS P 12 0 SHEET 2 AE6 6 LEU P 108 VAL P 111 1 O THR P 110 N GLU P 10 SHEET 3 AE6 6 ALA P 88 ALA P 93 -1 N ALA P 88 O VAL P 109 SHEET 4 AE6 6 MET P 34 GLN P 39 -1 N HIS P 35 O ALA P 93 SHEET 5 AE6 6 LEU P 45 ILE P 51 -1 O GLU P 46 N ARG P 38 SHEET 6 AE6 6 PRO P 57 TYR P 59 -1 O ASN P 58 N TRP P 50 SHEET 1 AE7 4 LEU R 4 THR R 5 0 SHEET 2 AE7 4 ALA R 19 ALA R 25 -1 O ARG R 24 N THR R 5 SHEET 3 AE7 4 ASP R 70 ILE R 75 -1 O LEU R 73 N LEU R 21 SHEET 4 AE7 4 PHE R 62 SER R 67 -1 N SER R 63 O THR R 74 SHEET 1 AE8 5 THR R 10 LEU R 13 0 SHEET 2 AE8 5 THR R 102 ILE R 106 1 O LYS R 103 N LEU R 11 SHEET 3 AE8 5 VAL R 85 GLN R 90 -1 N TYR R 86 O THR R 102 SHEET 4 AE8 5 ALA R 34 GLN R 38 -1 N GLN R 38 O VAL R 85 SHEET 5 AE8 5 ARG R 45 TYR R 49 -1 O ARG R 45 N GLN R 37 SHEET 1 AE9 4 THR R 10 LEU R 13 0 SHEET 2 AE9 4 THR R 102 ILE R 106 1 O LYS R 103 N LEU R 11 SHEET 3 AE9 4 VAL R 85 GLN R 90 -1 N TYR R 86 O THR R 102 SHEET 4 AE9 4 ALA R 97 PHE R 98 -1 O ALA R 97 N GLN R 90 SHEET 1 AF1 4 GLN O 3 THR O 7 0 SHEET 2 AF1 4 LEU O 18 SER O 25 -1 O ARG O 23 N VAL O 5 SHEET 3 AF1 4 THR O 77 MET O 82 -1 O MET O 82 N LEU O 18 SHEET 4 AF1 4 PHE O 67 ASP O 72 -1 N SER O 70 O SER O 79 SHEET 1 AF2 5 THR O 57 TYR O 59 0 SHEET 2 AF2 5 LEU O 45 ILE O 51 -1 N LEU O 50 O PHE O 58 SHEET 3 AF2 5 MET O 34 GLN O 39 -1 N ARG O 38 O GLU O 46 SHEET 4 AF2 5 ALA O 88 GLY O 95 -1 O TYR O 91 N VAL O 37 SHEET 5 AF2 5 PHE O 100H PHE O 102 -1 O PHE O 102 N THR O 94 SHEET 1 AF3 5 THR O 57 TYR O 59 0 SHEET 2 AF3 5 LEU O 45 ILE O 51 -1 N LEU O 50 O PHE O 58 SHEET 3 AF3 5 MET O 34 GLN O 39 -1 N ARG O 38 O GLU O 46 SHEET 4 AF3 5 ALA O 88 GLY O 95 -1 O TYR O 91 N VAL O 37 SHEET 5 AF3 5 ALA O 107 VAL O 109 -1 O ALA O 107 N TYR O 90 SHEET 1 AF4 2 SER Q 9 SER Q 12 0 SHEET 2 AF4 2 ARG Q 103 THR Q 105 1 O ARG Q 103 N VAL Q 11 SHEET 1 AF5 3 SER Q 18 THR Q 24 0 SHEET 2 AF5 3 THR Q 70 SER Q 76 -1 O ALA Q 71 N CYS Q 23 SHEET 3 AF5 3 PHE Q 62 SER Q 67 -1 N SER Q 67 O THR Q 70 SHEET 1 AF6 4 LYS Q 45 ILE Q 48 0 SHEET 2 AF6 4 VAL Q 33 GLN Q 38 -1 N TRP Q 35 O MET Q 47 SHEET 3 AF6 4 ASP Q 85 TYR Q 91 -1 O ASP Q 85 N GLN Q 38 SHEET 4 AF6 4 TYR Q 96 PHE Q 98 -1 O ILE Q 97 N ALA Q 90 SHEET 1 AF7 3 LEU E 494 THR E 499 0 SHEET 2 AF7 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AF7 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AF8 5 TRP E 45 ASP E 47 0 SHEET 2 AF8 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AF8 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AF8 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AF8 5 GLU E 83 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AF9 2 PHE E 53 ALA E 55 0 SHEET 2 AF9 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AG1 2 GLU E 91 ASN E 94 0 SHEET 2 AG1 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AG2 5 ARG E 169 TYR E 177 0 SHEET 2 AG2 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AG2 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 156 SHEET 4 AG2 5 SER E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AG2 5 ILE E 181 PRO E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AG3 3 THR E 202 GLN E 203 0 SHEET 2 AG3 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AG3 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AG4 7 LEU E 259 LEU E 261 0 SHEET 2 AG4 7 GLY E 441 ARG E 456 -1 O THR E 450 N LEU E 260 SHEET 3 AG4 7 ILE E 284 ASN E 302 -1 N CYS E 296 O CYS E 445 SHEET 4 AG4 7 HIS E 330 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AG4 7 SER E 413 LYS E 421 -1 O LEU E 416 N CYS E 331 SHEET 6 AG4 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AG4 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AG5 6 MET E 271 ARG E 273 0 SHEET 2 AG5 6 ILE E 284 ASN E 302 -1 O LEU E 285 N ARG E 273 SHEET 3 AG5 6 GLY E 441 ARG E 456 -1 O CYS E 445 N CYS E 296 SHEET 4 AG5 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AG5 6 ILE E 358 PHE E 361 1 N ILE E 358 O GLU E 466 SHEET 6 AG5 6 SER E 393 TRP E 395 -1 O SER E 393 N PHE E 361 SHEET 1 AG6 2 LYS E 305 ARG E 308 0 SHEET 2 AG6 2 TRP E 316 ALA E 319 -1 O PHE E 317 N ILE E 307 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 3 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 4 CYS I 23 CYS I 88 1555 1555 2.03 SSBOND 5 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 6 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 7 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 8 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 9 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 10 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 11 CYS A 378 CYS A 445 1555 1555 2.36 SSBOND 12 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 13 CYS A 501 CYS B 605 1555 1555 2.23 SSBOND 14 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 15 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 16 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 17 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 18 CYS M 23 CYS M 88 1555 1555 2.03 SSBOND 19 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 20 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 21 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 22 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 23 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 24 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 25 CYS C 378 CYS C 445 1555 1555 2.36 SSBOND 26 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 27 CYS C 501 CYS D 605 1555 1555 2.23 SSBOND 28 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 29 CYS P 22 CYS P 92 1555 1555 2.03 SSBOND 30 CYS R 23 CYS R 88 1555 1555 2.04 SSBOND 31 CYS O 22 CYS O 92 1555 1555 2.03 SSBOND 32 CYS Q 23 CYS Q 88 1555 1555 2.03 SSBOND 33 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 34 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 35 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 36 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 37 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 38 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 39 CYS E 378 CYS E 445 1555 1555 2.36 SSBOND 40 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 41 CYS E 501 CYS F 605 1555 1555 2.23 SSBOND 42 CYS F 598 CYS F 604 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG T 1 1555 1555 1.43 LINK ND2 ASN A 448 C1 NAG A 603 1555 1555 1.43 LINK ND2 ASN B 611 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.45 LINK ND2 ASN C 88 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG X 1 1555 1555 1.43 LINK ND2 ASN C 160 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN C 448 C1 NAG C 603 1555 1555 1.43 LINK ND2 ASN D 611 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN D 637 C1 NAG D 701 1555 1555 1.45 LINK ND2 ASN E 88 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG c 1 1555 1555 1.43 LINK ND2 ASN E 160 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG d 1 1555 1555 1.43 LINK ND2 ASN E 448 C1 NAG E 603 1555 1555 1.43 LINK ND2 ASN F 611 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 701 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 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 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.44 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.44 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 5.90 CISPEP 2 SER N 7 PRO N 8 0 5.93 CISPEP 3 SER R 7 PRO R 8 0 5.90 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