HEADER VIRAL PROTEIN/IMMUNE SYSTEM 08-JUN-23 8T4B TITLE MD65 N332-GT5 SOSIP IN COMPLEX WITH RM_N332_32 FAB AND RM20A3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MD65 N332-GT5 SOSIP GP120; COMPND 3 CHAIN: A, E, F; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM20A3 HEAVY CHAIN FV; COMPND 7 CHAIN: C, J, K; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RM20A3 LIGHT CHAIN FV; COMPND 11 CHAIN: D, M, N; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: MD65 N332-GT5 SOSIP GP41; COMPND 15 CHAIN: B, G, I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: RM_N332_32 HEAVY CHAIN FV; COMPND 19 CHAIN: H, O, P; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: RM_N332_32 LIGHT CHAIN FV; COMPND 23 CHAIN: L, Q, R; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; 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: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 18 ORGANISM_TAXID: 11676; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 23 ORGANISM_TAXID: 9544; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 MOL_ID: 6; SOURCE 27 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 28 ORGANISM_TAXID: 9544; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS GERMLINE TARGETING, NHP, SOSIP, ENV, HIV, BG18, IMMUNOGEN DESIGN, KEYWDS 2 ANTIBODY, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.OZOROWSKI,J.L.TORRES,A.B.WARD JRNL AUTH J.M.STEICHEN,I.PHUNG JRNL TITL VACCINE PRIMING OF RARE HIV BROADLY NEUTRALIZING ANTIBODY JRNL TITL 2 PRECURSORS IN NONHUMAN PRIMATES JRNL REF SCIENCE 2024 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADJ8321 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, 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) : 3.500 REMARK 3 NUMBER OF PARTICLES : 108784 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 8T4B 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_1000275178. 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 : MD65 N332-GT5 SOSIP IN COMPLEX REMARK 245 WITH RM_N332_32 FAB AND RM20A3 REMARK 245 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 6.00 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 : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (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) : 51.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 36000 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: A, C, D, B, H, L, E, J, M, G, REMARK 350 AND CHAINS: O, Q, F, K, N, I, P, R, S, REMARK 350 AND CHAINS: T, U, V, W, X REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 31 REMARK 465 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 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 ASN A 411 REMARK 465 GLY A 458 REMARK 465 GLY A 459 REMARK 465 SER A 460 REMARK 465 THR A 461 REMARK 465 ASN A 462 REMARK 465 THR 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 SER C 112 REMARK 465 SER C 113 REMARK 465 THR D 105 REMARK 465 VAL D 106 REMARK 465 LEU D 107 REMARK 465 GLY D 108 REMARK 465 GLN D 109 REMARK 465 PRO D 110 REMARK 465 LYS D 111 REMARK 465 ALA D 112 REMARK 465 SER D 113 REMARK 465 PRO D 114 REMARK 465 THR D 115 REMARK 465 VAL D 116 REMARK 465 THR D 117 REMARK 465 LEU D 118 REMARK 465 PHE D 119 REMARK 465 PRO D 120 REMARK 465 PRO D 121 REMARK 465 SER D 122 REMARK 465 SER D 123 REMARK 465 GLU D 124 REMARK 465 GLU D 125 REMARK 465 LEU D 126 REMARK 465 ALA B 512 REMARK 465 ALA B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 SER B 518 REMARK 465 SER B 519 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 GLN H 1 REMARK 465 SER H 110 REMARK 465 ILE H 111 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 ILE L 106 REMARK 465 LYS L 107 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 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 ASN E 411 REMARK 465 GLY E 458 REMARK 465 GLY E 459 REMARK 465 SER E 460 REMARK 465 THR E 461 REMARK 465 ASN E 462 REMARK 465 THR 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 SER J 112 REMARK 465 SER J 113 REMARK 465 THR M 105 REMARK 465 VAL M 106 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 ALA G 512 REMARK 465 ALA G 513 REMARK 465 GLY G 514 REMARK 465 ILE G 515 REMARK 465 GLY G 516 REMARK 465 ALA G 517 REMARK 465 SER G 518 REMARK 465 SER G 519 REMARK 465 GLY G 547 REMARK 465 ILE G 548 REMARK 465 VAL G 549 REMARK 465 GLN G 550 REMARK 465 GLN G 551 REMARK 465 GLN G 552 REMARK 465 SER G 553 REMARK 465 ASN G 554 REMARK 465 LEU G 555 REMARK 465 LEU G 556 REMARK 465 ARG G 557 REMARK 465 ALA G 558 REMARK 465 PRO G 559 REMARK 465 GLU G 560 REMARK 465 PRO G 561 REMARK 465 GLN G 562 REMARK 465 GLN G 563 REMARK 465 HIS G 564 REMARK 465 LEU G 565 REMARK 465 LEU G 566 REMARK 465 LYS G 567 REMARK 465 ASP G 568 REMARK 465 THR G 569 REMARK 465 HIS G 570 REMARK 465 TRP G 571 REMARK 465 GLN O 1 REMARK 465 SER O 110 REMARK 465 ILE O 111 REMARK 465 SER O 112 REMARK 465 SER O 113 REMARK 465 ILE Q 106 REMARK 465 LYS Q 107 REMARK 465 ALA F 31 REMARK 465 GLU F 32 REMARK 465 ALA F 58 REMARK 465 LYS F 59 REMARK 465 ALA F 60 REMARK 465 TYR F 61 REMARK 465 GLU F 62 REMARK 465 THR F 63 REMARK 465 GLU F 64 REMARK 465 LYS F 65 REMARK 465 GLU F 185A REMARK 465 ASN F 185B REMARK 465 GLN F 185C REMARK 465 GLY F 185D REMARK 465 ASN F 185E REMARK 465 ARG F 185F REMARK 465 SER F 185G REMARK 465 ASN F 185H REMARK 465 ASN F 185I REMARK 465 SER F 185J REMARK 465 ASN F 399 REMARK 465 THR F 400 REMARK 465 SER F 401 REMARK 465 VAL F 402 REMARK 465 GLN F 403 REMARK 465 GLY F 404 REMARK 465 SER F 405 REMARK 465 ASN F 406 REMARK 465 SER F 407 REMARK 465 THR F 408 REMARK 465 GLY F 409 REMARK 465 SER F 410 REMARK 465 ASN F 411 REMARK 465 GLY F 458 REMARK 465 GLY F 459 REMARK 465 SER F 460 REMARK 465 THR F 461 REMARK 465 ASN F 462 REMARK 465 THR F 505 REMARK 465 VAL F 506 REMARK 465 GLY F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 REMARK 465 ARG F 512 REMARK 465 ARG F 513 REMARK 465 SER K 112 REMARK 465 SER K 113 REMARK 465 THR N 105 REMARK 465 VAL N 106 REMARK 465 LEU N 107 REMARK 465 GLY N 108 REMARK 465 GLN N 109 REMARK 465 PRO N 110 REMARK 465 LYS N 111 REMARK 465 ALA N 112 REMARK 465 SER N 113 REMARK 465 PRO N 114 REMARK 465 THR N 115 REMARK 465 VAL N 116 REMARK 465 THR N 117 REMARK 465 LEU N 118 REMARK 465 PHE N 119 REMARK 465 PRO N 120 REMARK 465 PRO N 121 REMARK 465 SER N 122 REMARK 465 SER N 123 REMARK 465 GLU N 124 REMARK 465 GLU N 125 REMARK 465 LEU N 126 REMARK 465 ALA I 512 REMARK 465 ALA I 513 REMARK 465 GLY I 514 REMARK 465 ILE I 515 REMARK 465 GLY I 516 REMARK 465 ALA I 517 REMARK 465 SER I 518 REMARK 465 SER I 519 REMARK 465 GLY I 547 REMARK 465 ILE I 548 REMARK 465 VAL I 549 REMARK 465 GLN I 550 REMARK 465 GLN I 551 REMARK 465 GLN I 552 REMARK 465 SER I 553 REMARK 465 ASN I 554 REMARK 465 LEU I 555 REMARK 465 LEU I 556 REMARK 465 ARG I 557 REMARK 465 ALA I 558 REMARK 465 PRO I 559 REMARK 465 GLU I 560 REMARK 465 PRO I 561 REMARK 465 GLN I 562 REMARK 465 GLN I 563 REMARK 465 HIS I 564 REMARK 465 LEU I 565 REMARK 465 LEU I 566 REMARK 465 LYS I 567 REMARK 465 ASP I 568 REMARK 465 THR I 569 REMARK 465 HIS I 570 REMARK 465 TRP I 571 REMARK 465 GLN P 1 REMARK 465 SER P 110 REMARK 465 ILE P 111 REMARK 465 SER P 112 REMARK 465 SER P 113 REMARK 465 ILE R 106 REMARK 465 LYS R 107 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO L 80 CG PRO L 80 CD -0.199 REMARK 500 PRO Q 80 CG PRO Q 80 CD -0.199 REMARK 500 PRO R 80 CG PRO R 80 CD -0.199 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 ASP B 632 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 PRO L 80 CA - N - CD ANGL. DEV. = -13.8 DEGREES REMARK 500 PRO L 80 N - CD - CG ANGL. DEV. = -10.6 DEGREES REMARK 500 ASP G 632 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 PRO Q 80 CA - N - CD ANGL. DEV. = -13.9 DEGREES REMARK 500 PRO Q 80 N - CD - CG ANGL. DEV. = -10.5 DEGREES REMARK 500 ASP I 632 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 PRO R 80 CA - N - CD ANGL. DEV. = -13.9 DEGREES REMARK 500 PRO R 80 N - CD - CG ANGL. DEV. = -10.5 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 MET A 150 -1.74 83.38 REMARK 500 MET A 161 143.48 70.29 REMARK 500 GLN A 258 -48.52 66.66 REMARK 500 SER A 365 -90.56 -113.46 REMARK 500 THR A 387 -0.62 65.97 REMARK 500 SER C 82B -50.57 74.70 REMARK 500 LEU C 82C 75.06 44.20 REMARK 500 ALA C 100 -39.37 60.75 REMARK 500 LYS C 100E -86.95 -114.72 REMARK 500 ASP D 27B -76.75 -129.31 REMARK 500 ASP D 50 -129.96 56.00 REMARK 500 SER B 599 -89.78 -94.40 REMARK 500 SER B 612 -44.54 68.37 REMARK 500 LEU H 11 144.86 -175.89 REMARK 500 ARG H 66 -39.83 61.26 REMARK 500 LEU L 47 -62.05 -120.27 REMARK 500 ALA L 51 -47.12 68.76 REMARK 500 MET E 150 -1.78 83.39 REMARK 500 MET E 161 143.48 70.23 REMARK 500 GLN E 258 -48.53 66.66 REMARK 500 SER E 365 -90.57 -113.52 REMARK 500 THR E 387 -0.61 65.94 REMARK 500 SER J 82B -50.59 74.73 REMARK 500 LEU J 82C 75.08 44.18 REMARK 500 ALA J 100 -39.36 60.72 REMARK 500 LYS J 100E -87.00 -114.69 REMARK 500 ASP M 27B -76.77 -129.28 REMARK 500 ASP M 50 -130.00 56.00 REMARK 500 SER G 599 -89.79 -94.38 REMARK 500 SER G 612 -44.46 68.33 REMARK 500 LEU O 11 144.87 -175.86 REMARK 500 ARG O 66 -39.84 61.23 REMARK 500 LEU Q 47 -62.00 -120.29 REMARK 500 ALA Q 51 -47.10 68.71 REMARK 500 MET F 150 -1.77 83.39 REMARK 500 MET F 161 143.48 70.23 REMARK 500 GLN F 258 -48.53 66.67 REMARK 500 SER F 365 -90.59 -113.47 REMARK 500 THR F 387 -0.68 66.00 REMARK 500 SER K 82B -50.61 74.71 REMARK 500 LEU K 82C 75.05 44.23 REMARK 500 ALA K 100 -39.39 60.73 REMARK 500 LYS K 100E -86.99 -114.75 REMARK 500 ASP N 27B -76.71 -129.28 REMARK 500 ASP N 50 -129.97 55.99 REMARK 500 SER I 599 -89.80 -94.37 REMARK 500 SER I 612 -44.50 68.34 REMARK 500 LEU P 11 144.88 -175.86 REMARK 500 ARG P 66 -39.81 61.24 REMARK 500 LEU R 47 -62.04 -120.28 REMARK 500 REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-41026 RELATED DB: EMDB REMARK 900 MD65 N332-GT5 SOSIP IN COMPLEX WITH RM_N332_03 FAB AND RM20A3 FAB DBREF 8T4B A 31 513 PDB 8T4B 8T4B 31 513 DBREF 8T4B C 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B D 3 126 PDB 8T4B 8T4B 3 126 DBREF 8T4B B 512 664 PDB 8T4B 8T4B 512 664 DBREF 8T4B H 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B L 1 107 PDB 8T4B 8T4B 1 107 DBREF 8T4B E 31 513 PDB 8T4B 8T4B 31 513 DBREF 8T4B J 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B M 3 126 PDB 8T4B 8T4B 3 126 DBREF 8T4B G 512 664 PDB 8T4B 8T4B 512 664 DBREF 8T4B O 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B Q 1 107 PDB 8T4B 8T4B 1 107 DBREF 8T4B F 31 513 PDB 8T4B 8T4B 31 513 DBREF 8T4B K 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B N 3 126 PDB 8T4B 8T4B 3 126 DBREF 8T4B I 512 664 PDB 8T4B 8T4B 512 664 DBREF 8T4B P 1 113 PDB 8T4B 8T4B 1 113 DBREF 8T4B R 1 107 PDB 8T4B 8T4B 1 107 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 ALA PRO LYS LEU ARG SER MET MET ARG GLY GLU ILE 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 GLN ASN 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 SER VAL GLN ILE ASN CYS THR ARG PRO SER 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 PHE GLY ASP VAL LEU GLY HIS VAL ARG MET ALA HIS SEQRES 24 A 481 CYS ASN ILE 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 LEU ILE LEU PRO CYS TRP 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 THR VAL GLY ARG ARG ARG ARG ARG ARG 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 B 153 ALA ALA GLY ILE GLY ALA SER SER ASP 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 H 130 GLN LEU 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 ASP TYR CYS TRP ASN TRP ILE ARG GLN SEQRES 4 H 130 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE GLY SEQRES 5 H 130 GLY SER SER GLY SER THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 H 130 GLY ARG VAL THR ILE SER ALA ASP THR SER GLU ASN ARG SEQRES 7 H 130 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 H 130 ALA VAL TYR TYR CYS ALA ARG SER PRO ILE THR VAL PHE SEQRES 9 H 130 GLY VAL VAL ILE PHE ASP GLU TYR THR THR GLY ASN LEU SEQRES 10 H 130 ASP LEU TRP GLY PRO GLY THR PRO ILE SER ILE SER SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 107 SER VAL GLY ASP LYS VAL THR ILE THR CYS HIS ALA SER SEQRES 3 L 107 GLN ASP ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR TYR ALA SER SEQRES 5 L 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP TYR THR LEU THR ILE THR SER LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 107 ASP ASP LEU PRO PHE THR PHE GLY PRO GLY THR LYS LEU SEQRES 9 L 107 ASP ILE LYS 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 ALA PRO LYS LEU ARG SER MET MET ARG GLY GLU ILE 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 GLN ASN 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 SER VAL GLN ILE ASN CYS THR ARG PRO SER 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 PHE GLY ASP VAL LEU GLY HIS VAL ARG MET ALA HIS SEQRES 24 E 481 CYS ASN ILE 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 LEU ILE LEU PRO CYS TRP 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 THR VAL GLY ARG ARG ARG ARG ARG ARG 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 G 153 ALA ALA GLY ILE GLY ALA SER SER ASP GLY PHE LEU GLY SEQRES 2 G 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 G 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 G 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 G 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 G 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 G 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 G 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 G 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 G 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 G 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 G 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 O 130 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 O 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 O 130 GLY SER ILE SER ASP TYR CYS TRP ASN TRP ILE ARG GLN SEQRES 4 O 130 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE GLY SEQRES 5 O 130 GLY SER SER GLY SER THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 O 130 GLY ARG VAL THR ILE SER ALA ASP THR SER GLU ASN ARG SEQRES 7 O 130 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 O 130 ALA VAL TYR TYR CYS ALA ARG SER PRO ILE THR VAL PHE SEQRES 9 O 130 GLY VAL VAL ILE PHE ASP GLU TYR THR THR GLY ASN LEU SEQRES 10 O 130 ASP LEU TRP GLY PRO GLY THR PRO ILE SER ILE SER SER SEQRES 1 Q 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 Q 107 SER VAL GLY ASP LYS VAL THR ILE THR CYS HIS ALA SER SEQRES 3 Q 107 GLN ASP ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 Q 107 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR TYR ALA SER SEQRES 5 Q 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 Q 107 GLY SER GLY THR ASP TYR THR LEU THR ILE THR SER LEU SEQRES 7 Q 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 Q 107 ASP ASP LEU PRO PHE THR PHE GLY PRO GLY THR LYS LEU SEQRES 9 Q 107 ASP ILE LYS SEQRES 1 F 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 F 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 F 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 F 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 F 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 F 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 F 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 F 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN TYR SEQRES 9 F 481 ALA PRO LYS LEU ARG SER MET MET ARG GLY GLU ILE LYS SEQRES 10 F 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 F 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 F 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 F 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 F 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 F 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 F 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 F 481 CYS GLN ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 F 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 F 481 LEU ALA GLU GLU GLU VAL ILE ILE ARG SER GLU ASN ILE SEQRES 20 F 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN LEU ASN THR SEQRES 21 F 481 SER VAL GLN ILE ASN CYS THR ARG PRO SER ASN ASN THR SEQRES 22 F 481 VAL LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 F 481 TYR PHE GLY ASP VAL LEU GLY HIS VAL ARG MET ALA HIS SEQRES 24 F 481 CYS ASN ILE SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 F 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 F 481 THR ILE ILE ARG PHE ALA GLN SER SER GLY GLY ASP LEU SEQRES 27 F 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 F 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 F 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 F 481 SER ASN ASP SER LEU ILE LEU PRO CYS TRP ILE LYS GLN SEQRES 31 F 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 F 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 F 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 F 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 F 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 F 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 F 481 CYS LYS ARG ARG THR VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 K 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 K 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 K 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 K 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 K 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 K 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 K 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 K 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 K 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 K 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 I 153 ALA ALA GLY ILE GLY ALA SER SER ASP GLY PHE LEU GLY SEQRES 2 I 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 I 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 I 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 I 153 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 I 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 I 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 I 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 I 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 I 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 I 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 I 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 P 130 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 P 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 P 130 GLY SER ILE SER ASP TYR CYS TRP ASN TRP ILE ARG GLN SEQRES 4 P 130 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE GLY SEQRES 5 P 130 GLY SER SER GLY SER THR TYR TYR ASN PRO SER LEU LYS SEQRES 6 P 130 GLY ARG VAL THR ILE SER ALA ASP THR SER GLU ASN ARG SEQRES 7 P 130 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 P 130 ALA VAL TYR TYR CYS ALA ARG SER PRO ILE THR VAL PHE SEQRES 9 P 130 GLY VAL VAL ILE PHE ASP GLU TYR THR THR GLY ASN LEU SEQRES 10 P 130 ASP LEU TRP GLY PRO GLY THR PRO ILE SER ILE SER SER SEQRES 1 R 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 R 107 SER VAL GLY ASP LYS VAL THR ILE THR CYS HIS ALA SER SEQRES 3 R 107 GLN ASP ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 R 107 PRO GLY LYS ALA PRO LYS PRO LEU ILE TYR TYR ALA SER SEQRES 5 R 107 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 R 107 GLY SER GLY THR ASP TYR THR LEU THR ILE THR SER LEU SEQRES 7 R 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 R 107 ASP ASP LEU PRO PHE THR PHE GLY PRO GLY THR LYS LEU SEQRES 9 R 107 ASP ILE LYS 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 A 611 14 HET NAG A 612 14 HET NAG A 613 14 HET NAG B 701 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 E 607 14 HET NAG E 608 14 HET NAG E 609 14 HET NAG E 610 14 HET NAG E 611 14 HET NAG E 612 14 HET NAG E 613 14 HET NAG G 701 14 HET NAG F 601 14 HET NAG F 602 14 HET NAG F 603 14 HET NAG F 604 14 HET NAG F 605 14 HET NAG F 606 14 HET NAG F 607 14 HET NAG F 608 14 HET NAG F 609 14 HET NAG F 610 14 HET NAG F 611 14 HET NAG F 612 14 HET NAG F 613 14 HET NAG I 701 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET MAN S 4 11 HET MAN S 5 11 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET MAN T 4 11 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 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 HET BMA W 3 11 HET MAN W 4 11 HET MAN W 5 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET MAN X 4 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 19 NAG 54(C8 H15 N O6) FORMUL 61 BMA 6(C6 H12 O6) FORMUL 61 MAN 9(C6 H12 O6) HELIX 1 AA1 TRP A 96 ASN A 98 5 3 HELIX 2 AA2 ASN A 99 LYS A 117 1 19 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 ILE A 194 SER A 199 1 6 HELIX 5 AA5 LYS A 335 ARG A 350 1 16 HELIX 6 AA6 LYS A 351 PHE A 353 5 3 HELIX 7 AA7 ASP A 368 THR A 373 1 6 HELIX 8 AA8 THR A 387 PHE A 391 5 5 HELIX 9 AA9 ASN A 425 ARG A 429 5 5 HELIX 10 AB1 ARG A 476 TYR A 484 1 9 HELIX 11 AB2 THR C 28 PHE C 32 5 5 HELIX 12 AB3 ASP C 61 LYS C 64 5 4 HELIX 13 AB4 ARG C 83 THR C 87 5 5 HELIX 14 AB5 GLN D 79 GLU D 83 5 5 HELIX 15 AB6 LEU B 523 SER B 528 5 6 HELIX 16 AB7 THR B 529 SER B 534 1 6 HELIX 17 AB8 THR B 536 ARG B 542 1 7 HELIX 18 AB9 ILE B 573 ILE B 595 1 23 HELIX 19 AC1 ASN B 618 ASN B 625 1 8 HELIX 20 AC2 THR B 627 ILE B 635 1 9 HELIX 21 AC3 TYR B 638 LEU B 661 1 24 HELIX 22 AC4 SER H 28 TYR H 32 5 5 HELIX 23 AC5 THR H 83 THR H 87 5 5 HELIX 24 AC6 VAL H 100B ASP H 100F 5 5 HELIX 25 AC7 GLN L 79 PHE L 83 5 5 HELIX 26 AC8 TRP E 96 ASN E 98 5 3 HELIX 27 AC9 ASN E 99 LYS E 117 1 19 HELIX 28 AD1 LEU E 122 CYS E 126 5 5 HELIX 29 AD2 ILE E 194 SER E 199 1 6 HELIX 30 AD3 LYS E 335 ARG E 350 1 16 HELIX 31 AD4 LYS E 351 PHE E 353 5 3 HELIX 32 AD5 ASP E 368 THR E 373 1 6 HELIX 33 AD6 THR E 387 PHE E 391 5 5 HELIX 34 AD7 ASN E 425 ARG E 429 5 5 HELIX 35 AD8 ARG E 476 TYR E 484 1 9 HELIX 36 AD9 THR J 28 PHE J 32 5 5 HELIX 37 AE1 ASP J 61 LYS J 64 5 4 HELIX 38 AE2 ARG J 83 THR J 87 5 5 HELIX 39 AE3 GLN M 79 GLU M 83 5 5 HELIX 40 AE4 LEU G 523 SER G 528 5 6 HELIX 41 AE5 THR G 529 SER G 534 1 6 HELIX 42 AE6 THR G 536 ARG G 542 1 7 HELIX 43 AE7 ILE G 573 ILE G 595 1 23 HELIX 44 AE8 ASN G 618 ASN G 625 1 8 HELIX 45 AE9 THR G 627 ILE G 635 1 9 HELIX 46 AF1 TYR G 638 LEU G 661 1 24 HELIX 47 AF2 SER O 28 TYR O 32 5 5 HELIX 48 AF3 THR O 83 THR O 87 5 5 HELIX 49 AF4 VAL O 100B ASP O 100F 5 5 HELIX 50 AF5 GLN Q 79 PHE Q 83 5 5 HELIX 51 AF6 TRP F 96 ASN F 98 5 3 HELIX 52 AF7 ASN F 99 LYS F 117 1 19 HELIX 53 AF8 LEU F 122 CYS F 126 5 5 HELIX 54 AF9 ILE F 194 SER F 199 1 6 HELIX 55 AG1 LYS F 335 ARG F 350 1 16 HELIX 56 AG2 LYS F 351 PHE F 353 5 3 HELIX 57 AG3 ASP F 368 THR F 373 1 6 HELIX 58 AG4 THR F 387 PHE F 391 5 5 HELIX 59 AG5 ASN F 425 ARG F 429 5 5 HELIX 60 AG6 ARG F 476 TYR F 484 1 9 HELIX 61 AG7 THR K 28 PHE K 32 5 5 HELIX 62 AG8 ASP K 61 LYS K 64 5 4 HELIX 63 AG9 ARG K 83 THR K 87 5 5 HELIX 64 AH1 GLN N 79 GLU N 83 5 5 HELIX 65 AH2 LEU I 523 SER I 528 5 6 HELIX 66 AH3 THR I 529 SER I 534 1 6 HELIX 67 AH4 THR I 536 ARG I 542 1 7 HELIX 68 AH5 ILE I 573 ILE I 595 1 23 HELIX 69 AH6 ASN I 618 ASN I 625 1 8 HELIX 70 AH7 THR I 627 ILE I 635 1 9 HELIX 71 AH8 TYR I 638 LEU I 661 1 24 HELIX 72 AH9 SER P 28 TYR P 32 5 5 HELIX 73 AI1 THR P 83 THR P 87 5 5 HELIX 74 AI2 VAL P 100B ASP P 100F 5 5 HELIX 75 AI3 GLN R 79 PHE R 83 5 5 SHEET 1 AA1 3 LEU A 494 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TRP A 35 O THR A 499 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 LYS A 227 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 SER A 243 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA5 5 VAL A 172 TYR A 177 0 SHEET 2 AA5 5 ILE A 154 PHE A 159 -1 N PHE A 159 O VAL A 172 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AA5 5 LYS A 189 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 ILE A 201 GLN A 203 0 SHEET 2 AA6 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA712 LEU A 259 LEU A 261 0 SHEET 2 AA712 ILE A 271 SER A 274 0 SHEET 3 AA712 ILE A 284 GLY A 312 -1 O GLN A 287 N ILE A 271 SHEET 4 AA712 GLN A 315 VAL A 323 -1 O TYR A 319 N LYS A 305 SHEET 5 AA712 ALA A 329 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 6 AA712 ILE A 358 PHE A 361 0 SHEET 7 AA712 HIS A 374 CYS A 378 0 SHEET 8 AA712 GLU A 381 CYS A 385 -1 O PHE A 383 N PHE A 376 SHEET 9 AA712 SER A 393 ILE A 396 -1 O TRP A 395 N ILE A 359 SHEET 10 AA712 SER A 413 ILE A 420 -1 O TRP A 419 N TYR A 384 SHEET 11 AA712 GLY A 441 ARG A 456 -1 O GLY A 441 N ASN A 302 SHEET 12 AA712 THR A 465 ARG A 469 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 4 GLN C 3 GLU C 6 0 SHEET 2 AA8 4 GLY C 16 SER C 25 -1 O ARG C 23 N VAL C 5 SHEET 3 AA8 4 THR C 77 SER C 82B-1 O MET C 82 N LEU C 18 SHEET 4 AA8 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AA9 6 MET C 34 GLN C 39 0 SHEET 2 AA9 6 LEU C 45 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 3 AA9 6 THR C 57 TYR C 59 -1 O PHE C 58 N LEU C 50 SHEET 4 AA9 6 ALA C 88 GLY C 95 -1 O TYR C 91 N VAL C 37 SHEET 5 AA9 6 PHE C 100H TRP C 103 -1 O ASP C 101 N THR C 94 SHEET 6 AA9 6 ALA C 107 VAL C 109 -1 O ALA C 107 N TYR C 90 SHEET 1 AB1 3 VAL D 19 THR D 24 0 SHEET 2 AB1 3 THR D 70 ILE D 75 -1 O ALA D 71 N CYS D 23 SHEET 3 AB1 3 PHE D 62 SER D 67 -1 N SER D 67 O THR D 70 SHEET 1 AB2 5 VAL D 33 GLN D 38 0 SHEET 2 AB2 5 LYS D 45 ILE D 48 -1 O MET D 47 N TRP D 35 SHEET 3 AB2 5 ASP D 85 ALA D 92 -1 O ASP D 85 N GLN D 38 SHEET 4 AB2 5 THR D 95A PHE D 98 -1 O ILE D 97 N ALA D 90 SHEET 5 AB2 5 THR D 102 ARG D 103 -1 O THR D 102 N TYR D 86 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AB3 4 ARG H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AB3 4 VAL H 67 ASP H 72 -1 N THR H 68 O LYS H 81 SHEET 1 AB4 6 CYS H 33 GLN H 39 0 SHEET 2 AB4 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 3 AB4 6 THR H 57 TYR H 59 -1 O TYR H 58 N TYR H 50 SHEET 4 AB4 6 ALA H 88 SER H 95 -1 O VAL H 89 N GLN H 39 SHEET 5 AB4 6 LEU H 102 TRP H 103 -1 O LEU H 102 N ARG H 94 SHEET 6 AB4 6 THR H 107 ILE H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AB5 2 THR H 98 VAL H 99 0 SHEET 2 AB5 2 TYR H 100H THR H 100I-1 O THR H 100I N THR H 98 SHEET 1 AB6 4 MET L 4 SER L 7 0 SHEET 2 AB6 4 VAL L 19 ALA L 25 -1 O HIS L 24 N THR L 5 SHEET 3 AB6 4 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB6 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB7 7 SER L 10 SER L 12 0 SHEET 2 AB7 7 LEU L 33 GLN L 38 0 SHEET 3 AB7 7 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 4 AB7 7 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 5 AB7 7 THR L 85 GLN L 90 -1 O THR L 85 N GLN L 38 SHEET 6 AB7 7 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 7 AB7 7 THR L 102 ASP L 105 -1 O THR L 102 N TYR L 86 SHEET 1 AB8 3 LEU E 494 THR E 499 0 SHEET 2 AB8 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AB8 3 ILE G 603 PRO G 609 -1 O VAL G 608 N VAL E 36 SHEET 1 AB9 5 TRP E 45 ASP E 47 0 SHEET 2 AB9 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB9 5 PHE E 223 LYS E 227 -1 N ALA E 224 O VAL E 489 SHEET 4 AB9 5 SER E 243 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB9 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC1 2 PHE E 53 ALA E 55 0 SHEET 2 AC1 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC2 2 GLU E 91 ASN E 94 0 SHEET 2 AC2 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AC3 5 VAL E 172 TYR E 177 0 SHEET 2 AC3 5 ILE E 154 PHE E 159 -1 N PHE E 159 O VAL E 172 SHEET 3 AC3 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 156 SHEET 4 AC3 5 LYS E 189 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC3 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC4 3 ILE E 201 GLN E 203 0 SHEET 2 AC4 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC4 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC512 LEU E 259 LEU E 261 0 SHEET 2 AC512 ILE E 271 SER E 274 0 SHEET 3 AC512 ILE E 284 GLY E 312 -1 O GLN E 287 N ILE E 271 SHEET 4 AC512 GLN E 315 VAL E 323 -1 O TYR E 319 N LYS E 305 SHEET 5 AC512 ALA E 329 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AC512 ILE E 358 PHE E 361 0 SHEET 7 AC512 HIS E 374 CYS E 378 0 SHEET 8 AC512 GLU E 381 CYS E 385 -1 O PHE E 383 N PHE E 376 SHEET 9 AC512 SER E 393 ILE E 396 -1 O TRP E 395 N ILE E 359 SHEET 10 AC512 SER E 413 ILE E 420 -1 O TRP E 419 N TYR E 384 SHEET 11 AC512 GLY E 441 ARG E 456 -1 O GLY E 441 N ASN E 302 SHEET 12 AC512 THR E 465 ARG E 469 -1 O ARG E 469 N THR E 455 SHEET 1 AC6 4 GLN J 3 GLU J 6 0 SHEET 2 AC6 4 GLY J 16 SER J 25 -1 O ARG J 23 N VAL J 5 SHEET 3 AC6 4 THR J 77 SER J 82B-1 O MET J 82 N LEU J 18 SHEET 4 AC6 4 PHE J 67 ASP J 72 -1 N THR J 68 O GLN J 81 SHEET 1 AC7 6 MET J 34 GLN J 39 0 SHEET 2 AC7 6 LEU J 45 ILE J 51 -1 O ILE J 51 N MET J 34 SHEET 3 AC7 6 THR J 57 TYR J 59 -1 O PHE J 58 N LEU J 50 SHEET 4 AC7 6 ALA J 88 GLY J 95 -1 O TYR J 91 N VAL J 37 SHEET 5 AC7 6 PHE J 100H TRP J 103 -1 O ASP J 101 N THR J 94 SHEET 6 AC7 6 ALA J 107 VAL J 109 -1 O ALA J 107 N TYR J 90 SHEET 1 AC8 3 VAL M 19 THR M 24 0 SHEET 2 AC8 3 THR M 70 ILE M 75 -1 O ALA M 71 N CYS M 23 SHEET 3 AC8 3 PHE M 62 SER M 67 -1 N SER M 67 O THR M 70 SHEET 1 AC9 5 VAL M 33 GLN M 38 0 SHEET 2 AC9 5 LYS M 45 ILE M 48 -1 O MET M 47 N TRP M 35 SHEET 3 AC9 5 ASP M 85 ALA M 92 -1 O ASP M 85 N GLN M 38 SHEET 4 AC9 5 THR M 95A PHE M 98 -1 O ILE M 97 N ALA M 90 SHEET 5 AC9 5 THR M 102 ARG M 103 -1 O THR M 102 N TYR M 86 SHEET 1 AD1 4 GLN O 3 SER O 7 0 SHEET 2 AD1 4 LEU O 18 SER O 25 -1 O ALA O 23 N GLN O 5 SHEET 3 AD1 4 ARG O 77 LEU O 82 -1 O LEU O 80 N LEU O 20 SHEET 4 AD1 4 VAL O 67 ASP O 72 -1 N THR O 68 O LYS O 81 SHEET 1 AD2 6 CYS O 33 GLN O 39 0 SHEET 2 AD2 6 GLU O 46 ILE O 51 -1 O GLU O 46 N ARG O 38 SHEET 3 AD2 6 THR O 57 TYR O 59 -1 O TYR O 58 N TYR O 50 SHEET 4 AD2 6 ALA O 88 SER O 95 -1 O VAL O 89 N GLN O 39 SHEET 5 AD2 6 LEU O 102 TRP O 103 -1 O LEU O 102 N ARG O 94 SHEET 6 AD2 6 THR O 107 ILE O 109 -1 O THR O 107 N TYR O 90 SHEET 1 AD3 2 THR O 98 VAL O 99 0 SHEET 2 AD3 2 TYR O 100H THR O 100I-1 O THR O 100I N THR O 98 SHEET 1 AD4 4 MET Q 4 SER Q 7 0 SHEET 2 AD4 4 VAL Q 19 ALA Q 25 -1 O HIS Q 24 N THR Q 5 SHEET 3 AD4 4 ASP Q 70 ILE Q 75 -1 O ILE Q 75 N VAL Q 19 SHEET 4 AD4 4 PHE Q 62 SER Q 67 -1 N SER Q 65 O THR Q 72 SHEET 1 AD5 7 SER Q 10 SER Q 12 0 SHEET 2 AD5 7 LEU Q 33 GLN Q 38 0 SHEET 3 AD5 7 LYS Q 45 TYR Q 49 -1 O LYS Q 45 N GLN Q 37 SHEET 4 AD5 7 SER Q 53 LEU Q 54 -1 O SER Q 53 N TYR Q 49 SHEET 5 AD5 7 THR Q 85 GLN Q 90 -1 O THR Q 85 N GLN Q 38 SHEET 6 AD5 7 THR Q 97 PHE Q 98 -1 O THR Q 97 N GLN Q 90 SHEET 7 AD5 7 THR Q 102 ASP Q 105 -1 O THR Q 102 N TYR Q 86 SHEET 1 AD6 3 LEU F 494 THR F 499 0 SHEET 2 AD6 3 TRP F 35 TYR F 40 -1 N TRP F 35 O THR F 499 SHEET 3 AD6 3 ILE I 603 PRO I 609 -1 O VAL I 608 N VAL F 36 SHEET 1 AD7 5 TRP F 45 ASP F 47 0 SHEET 2 AD7 5 TYR F 486 ILE F 491 -1 O LYS F 490 N LYS F 46 SHEET 3 AD7 5 PHE F 223 LYS F 227 -1 N ALA F 224 O VAL F 489 SHEET 4 AD7 5 SER F 243 VAL F 245 -1 O SER F 243 N LYS F 227 SHEET 5 AD7 5 GLU F 83 HIS F 85 -1 N ILE F 84 O THR F 244 SHEET 1 AD8 2 PHE F 53 ALA F 55 0 SHEET 2 AD8 2 HIS F 216 CYS F 218 -1 O HIS F 216 N ALA F 55 SHEET 1 AD9 2 GLU F 91 ASN F 94 0 SHEET 2 AD9 2 THR F 236 CYS F 239 -1 O GLY F 237 N PHE F 93 SHEET 1 AE1 5 VAL F 172 TYR F 177 0 SHEET 2 AE1 5 ILE F 154 PHE F 159 -1 N PHE F 159 O VAL F 172 SHEET 3 AE1 5 LEU F 129 ASN F 133 -1 N THR F 132 O ASN F 156 SHEET 4 AE1 5 LYS F 189 LEU F 193 -1 O TYR F 191 N LEU F 129 SHEET 5 AE1 5 VAL F 181 GLN F 183 -1 N VAL F 182 O ARG F 192 SHEET 1 AE2 3 ILE F 201 GLN F 203 0 SHEET 2 AE2 3 ALA F 433 TYR F 435 1 O TYR F 435 N THR F 202 SHEET 3 AE2 3 ILE F 423 ILE F 424 -1 N ILE F 424 O MET F 434 SHEET 1 AE312 LEU F 259 LEU F 261 0 SHEET 2 AE312 ILE F 271 SER F 274 0 SHEET 3 AE312 ILE F 284 GLY F 312 -1 O GLN F 287 N ILE F 271 SHEET 4 AE312 GLN F 315 VAL F 323 -1 O TYR F 319 N LYS F 305 SHEET 5 AE312 ALA F 329 SER F 334 -1 O ASN F 332 N ASN F 295 SHEET 6 AE312 ILE F 358 PHE F 361 0 SHEET 7 AE312 HIS F 374 CYS F 378 0 SHEET 8 AE312 GLU F 381 CYS F 385 -1 O PHE F 383 N PHE F 376 SHEET 9 AE312 SER F 393 ILE F 396 -1 O TRP F 395 N ILE F 359 SHEET 10 AE312 SER F 413 ILE F 420 -1 O TRP F 419 N TYR F 384 SHEET 11 AE312 GLY F 441 ARG F 456 -1 O GLY F 441 N ASN F 302 SHEET 12 AE312 THR F 465 ARG F 469 -1 O ARG F 469 N THR F 455 SHEET 1 AE4 4 GLN K 3 GLU K 6 0 SHEET 2 AE4 4 GLY K 16 SER K 25 -1 O ARG K 23 N VAL K 5 SHEET 3 AE4 4 THR K 77 SER K 82B-1 O MET K 82 N LEU K 18 SHEET 4 AE4 4 PHE K 67 ASP K 72 -1 N THR K 68 O GLN K 81 SHEET 1 AE5 6 MET K 34 GLN K 39 0 SHEET 2 AE5 6 LEU K 45 ILE K 51 -1 O ILE K 51 N MET K 34 SHEET 3 AE5 6 THR K 57 TYR K 59 -1 O PHE K 58 N LEU K 50 SHEET 4 AE5 6 ALA K 88 GLY K 95 -1 O TYR K 91 N VAL K 37 SHEET 5 AE5 6 PHE K 100H TRP K 103 -1 O ASP K 101 N THR K 94 SHEET 6 AE5 6 ALA K 107 VAL K 109 -1 O ALA K 107 N TYR K 90 SHEET 1 AE6 3 VAL N 19 THR N 24 0 SHEET 2 AE6 3 THR N 70 ILE N 75 -1 O ALA N 71 N CYS N 23 SHEET 3 AE6 3 PHE N 62 SER N 67 -1 N SER N 67 O THR N 70 SHEET 1 AE7 5 VAL N 33 GLN N 38 0 SHEET 2 AE7 5 LYS N 45 ILE N 48 -1 O MET N 47 N TRP N 35 SHEET 3 AE7 5 ASP N 85 ALA N 92 -1 O ASP N 85 N GLN N 38 SHEET 4 AE7 5 THR N 95A PHE N 98 -1 O ILE N 97 N ALA N 90 SHEET 5 AE7 5 THR N 102 ARG N 103 -1 O THR N 102 N TYR N 86 SHEET 1 AE8 4 GLN P 3 SER P 7 0 SHEET 2 AE8 4 LEU P 18 SER P 25 -1 O ALA P 23 N GLN P 5 SHEET 3 AE8 4 ARG P 77 LEU P 82 -1 O LEU P 80 N LEU P 20 SHEET 4 AE8 4 VAL P 67 ASP P 72 -1 N THR P 68 O LYS P 81 SHEET 1 AE9 6 CYS P 33 GLN P 39 0 SHEET 2 AE9 6 GLU P 46 ILE P 51 -1 O GLU P 46 N ARG P 38 SHEET 3 AE9 6 THR P 57 TYR P 59 -1 O TYR P 58 N TYR P 50 SHEET 4 AE9 6 ALA P 88 SER P 95 -1 O VAL P 89 N GLN P 39 SHEET 5 AE9 6 LEU P 102 TRP P 103 -1 O LEU P 102 N ARG P 94 SHEET 6 AE9 6 THR P 107 ILE P 109 -1 O THR P 107 N TYR P 90 SHEET 1 AF1 2 THR P 98 VAL P 99 0 SHEET 2 AF1 2 TYR P 100H THR P 100I-1 O THR P 100I N THR P 98 SHEET 1 AF2 4 MET R 4 SER R 7 0 SHEET 2 AF2 4 VAL R 19 ALA R 25 -1 O HIS R 24 N THR R 5 SHEET 3 AF2 4 ASP R 70 ILE R 75 -1 O ILE R 75 N VAL R 19 SHEET 4 AF2 4 PHE R 62 SER R 67 -1 N SER R 65 O THR R 72 SHEET 1 AF3 7 SER R 10 SER R 12 0 SHEET 2 AF3 7 LEU R 33 GLN R 38 0 SHEET 3 AF3 7 LYS R 45 TYR R 49 -1 O LYS R 45 N GLN R 37 SHEET 4 AF3 7 SER R 53 LEU R 54 -1 O SER R 53 N TYR R 49 SHEET 5 AF3 7 THR R 85 GLN R 90 -1 O THR R 85 N GLN R 38 SHEET 6 AF3 7 THR R 97 PHE R 98 -1 O THR R 97 N GLN R 90 SHEET 7 AF3 7 THR R 102 ASP R 105 -1 O THR R 102 N TYR R 86 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.05 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.04 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.04 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 11 CYS C 22 CYS C 92 1555 1555 2.03 SSBOND 12 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 13 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 14 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 15 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 16 CYS E 54 CYS E 74 1555 1555 2.05 SSBOND 17 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 18 CYS E 126 CYS E 196 1555 1555 2.04 SSBOND 19 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 20 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 21 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 22 CYS E 296 CYS E 331 1555 1555 2.04 SSBOND 23 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 24 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 25 CYS E 501 CYS G 605 1555 1555 2.03 SSBOND 26 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 27 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 28 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 29 CYS O 22 CYS O 92 1555 1555 2.05 SSBOND 30 CYS Q 23 CYS Q 88 1555 1555 2.03 SSBOND 31 CYS F 54 CYS F 74 1555 1555 2.05 SSBOND 32 CYS F 119 CYS F 205 1555 1555 2.04 SSBOND 33 CYS F 126 CYS F 196 1555 1555 2.04 SSBOND 34 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 35 CYS F 218 CYS F 247 1555 1555 2.03 SSBOND 36 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 37 CYS F 296 CYS F 331 1555 1555 2.04 SSBOND 38 CYS F 378 CYS F 445 1555 1555 2.03 SSBOND 39 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 40 CYS F 501 CYS I 605 1555 1555 2.03 SSBOND 41 CYS K 22 CYS K 92 1555 1555 2.03 SSBOND 42 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 43 CYS I 598 CYS I 604 1555 1555 2.03 SSBOND 44 CYS P 22 CYS P 92 1555 1555 2.04 SSBOND 45 CYS R 23 CYS R 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 606 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG A 613 1555 1555 1.45 LINK ND2 ASN A 262 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 289 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG A 609 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 610 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG A 611 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 612 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.45 LINK ND2 ASN E 88 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 606 1555 1555 1.43 LINK ND2 ASN E 234 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 241 C1 NAG E 613 1555 1555 1.45 LINK ND2 ASN E 262 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 608 1555 1555 1.44 LINK ND2 ASN E 289 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 609 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 610 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG E 611 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 612 1555 1555 1.44 LINK ND2 ASN G 611 C1 NAG G 701 1555 1555 1.45 LINK ND2 ASN F 88 C1 NAG F 603 1555 1555 1.44 LINK ND2 ASN F 156 C1 NAG F 604 1555 1555 1.44 LINK ND2 ASN F 160 C1 NAG F 605 1555 1555 1.44 LINK ND2 ASN F 197 C1 NAG F 606 1555 1555 1.43 LINK ND2 ASN F 234 C1 NAG F 607 1555 1555 1.44 LINK ND2 ASN F 241 C1 NAG F 613 1555 1555 1.45 LINK ND2 ASN F 262 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN F 276 C1 NAG F 608 1555 1555 1.44 LINK ND2 ASN F 289 C1 NAG F 601 1555 1555 1.44 LINK ND2 ASN F 295 C1 NAG F 609 1555 1555 1.44 LINK ND2 ASN F 301 C1 NAG F 602 1555 1555 1.44 LINK ND2 ASN F 332 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN F 339 C1 NAG F 610 1555 1555 1.44 LINK ND2 ASN F 386 C1 NAG F 611 1555 1555 1.44 LINK ND2 ASN F 448 C1 NAG F 612 1555 1555 1.44 LINK ND2 ASN I 611 C1 NAG I 701 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.44 LINK O6 BMA S 3 C1 MAN S 5 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O3 BMA T 3 C1 MAN T 4 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 5 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.44 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.44 LINK O6 BMA W 3 C1 MAN W 5 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -2.55 CISPEP 2 LEU L 94 PRO L 95 0 5.19 CISPEP 3 SER Q 7 PRO Q 8 0 -2.49 CISPEP 4 LEU Q 94 PRO Q 95 0 5.18 CISPEP 5 SER R 7 PRO R 8 0 -2.49 CISPEP 6 LEU R 94 PRO R 95 0 5.17 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