HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-DEC-21 7T9A TITLE APEXGT2 IN COMPLEX WITH GT2-D42.16 AND RM20A3 FABS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV ENVELOPE APEXGT2 GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIV ENVELOPE APEXGT2 GP41; COMPND 7 CHAIN: B, D, F; COMPND 8 SYNONYM: ENV POLYPROTEIN; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: RM20A3 FAB HEAVY CHAIN; COMPND 12 CHAIN: J, M, O; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: RM20A3 FAB LIGHT CHAIN; COMPND 16 CHAIN: K, N, P; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 5; COMPND 19 MOLECULE: GT2-D42.16 FAB HEAVY CHAIN; COMPND 20 CHAIN: H; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 6; COMPND 23 MOLECULE: GT2-D42.16 FAB LIGHT CHAIN; COMPND 24 CHAIN: L; COMPND 25 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_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 17 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 18 ORGANISM_TAXID: 9544; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 25 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 26 ORGANISM_TAXID: 9544; SOURCE 27 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 28 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 30 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 31 MOL_ID: 5; SOURCE 32 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 33 ORGANISM_COMMON: MOUSE; SOURCE 34 ORGANISM_TAXID: 10090; SOURCE 35 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 36 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 39 MOL_ID: 6; SOURCE 40 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 41 ORGANISM_COMMON: MOUSE; SOURCE 42 ORGANISM_TAXID: 10090; SOURCE 43 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 44 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 45 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 46 EXPRESSION_SYSTEM_CELL_LINE: HEK KEYWDS HIV, GERMLINE TARGETING, VACCINE, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.T.BERNDSEN JRNL AUTH E.MELZI,J.WILLIS,K.MA,Y.LIN,S.KRATOCHVIL,Z.T.BERNDSEN, JRNL AUTH 2 U.NAIR,J.WARNER,J.STEICHEN,S.PECETTA,M.PEREZ,K.KIRSCH, JRNL AUTH 3 A.B.WARD,W.SCHIEF,F.D.BATISTA JRNL TITL PRIMING HIV ENVELOPE V2 APEX-DIRECTED BROADLY NEUTRALIZING JRNL TITL 2 ANTIBODY RESPONSES WITH PROTEIN OR MRNA IMMUNOGENS JRNL REF IMMUNITY 2022 JRNL REFN ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 3.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.540 REMARK 3 NUMBER OF PARTICLES : 62971 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 7T9A 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_1000259277. 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 : HIV-1 ENVELOPE APEXGT2 IN REMARK 245 COMPLEX WITH PCT64_LMCA.HL_GT2_ REMARK 245 D42.16 FAB AND RM20A3 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 50.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J, K, C, D, M, N, E, F, REMARK 350 AND CHAINS: O, P, H, L, G, I, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i 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 HIS A 66 REMARK 465 ASN A 397A REMARK 465 THR A 397B REMARK 465 SER A 397C REMARK 465 VAL A 397D REMARK 465 GLN A 397E REMARK 465 GLY A 397F REMARK 465 SER A 397G REMARK 465 ASN A 397H REMARK 465 SER A 397I REMARK 465 THR A 397J REMARK 465 GLY A 397K REMARK 465 SER A 397L 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 SER A 463 REMARK 465 ARG A 504 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 510 REMARK 465 VAL B 511 REMARK 465 GLY B 512 REMARK 465 ILE B 513 REMARK 465 GLY B 514 REMARK 465 ALA B 515 REMARK 465 VAL B 516 REMARK 465 SER 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 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 LEU B 663 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 THR B 666 REMARK 465 LYS B 667 REMARK 465 HIS B 668 REMARK 465 HIS B 669 REMARK 465 HIS B 670 REMARK 465 HIS B 671 REMARK 465 HIS B 672 REMARK 465 HIS B 673 REMARK 465 SER J 113 REMARK 465 GLY K 108 REMARK 465 GLN K 109 REMARK 465 PRO K 110 REMARK 465 LYS K 111 REMARK 465 ALA K 112 REMARK 465 SER K 113 REMARK 465 PRO K 114 REMARK 465 THR K 115 REMARK 465 VAL K 116 REMARK 465 THR K 117 REMARK 465 LEU K 118 REMARK 465 PHE K 119 REMARK 465 PRO K 120 REMARK 465 PRO K 121 REMARK 465 SER K 122 REMARK 465 SER K 123 REMARK 465 GLU K 124 REMARK 465 GLU K 125 REMARK 465 LEU K 126 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 ALA C 58 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 ASN C 67 REMARK 465 ASN C 397A REMARK 465 THR C 397B REMARK 465 SER C 397C REMARK 465 VAL C 397D REMARK 465 GLN C 397E REMARK 465 GLY C 397F REMARK 465 SER C 397G REMARK 465 ASN C 397H REMARK 465 SER C 397I REMARK 465 THR C 397J REMARK 465 GLY C 397K REMARK 465 SER C 397L REMARK 465 GLY C 458 REMARK 465 GLY C 459 REMARK 465 SER C 460 REMARK 465 THR C 461 REMARK 465 ASN C 462 REMARK 465 SER C 463 REMARK 465 ARG C 504 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 510 REMARK 465 VAL D 511 REMARK 465 GLY D 512 REMARK 465 ILE D 513 REMARK 465 GLY D 514 REMARK 465 ALA D 515 REMARK 465 VAL D 516 REMARK 465 SER 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 PRO 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 ASP D 568 REMARK 465 THR D 569 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 GLY D 665 REMARK 465 THR D 666 REMARK 465 LYS D 667 REMARK 465 HIS D 668 REMARK 465 HIS D 669 REMARK 465 HIS D 670 REMARK 465 HIS D 671 REMARK 465 HIS D 672 REMARK 465 HIS D 673 REMARK 465 SER M 113 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 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 HIS E 66 REMARK 465 ASN E 397A REMARK 465 THR E 397B REMARK 465 SER E 397C REMARK 465 VAL E 397D REMARK 465 GLN E 397E REMARK 465 GLY E 397F REMARK 465 SER E 397G REMARK 465 ASN E 397H REMARK 465 SER E 397I REMARK 465 THR E 397J REMARK 465 GLY E 397K REMARK 465 SER E 397L 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 SER E 463 REMARK 465 ARG E 504 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 510 REMARK 465 VAL F 511 REMARK 465 GLY F 512 REMARK 465 ILE F 513 REMARK 465 GLY F 514 REMARK 465 ALA F 515 REMARK 465 VAL F 516 REMARK 465 SER 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 PRO F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 ASP F 568 REMARK 465 THR F 569 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 GLY F 665 REMARK 465 THR F 666 REMARK 465 LYS F 667 REMARK 465 HIS F 668 REMARK 465 HIS F 669 REMARK 465 HIS F 670 REMARK 465 HIS F 671 REMARK 465 HIS F 672 REMARK 465 HIS F 673 REMARK 465 SER O 113 REMARK 465 GLY P 108 REMARK 465 GLN P 109 REMARK 465 PRO P 110 REMARK 465 LYS P 111 REMARK 465 ALA P 112 REMARK 465 SER P 113 REMARK 465 PRO P 114 REMARK 465 THR P 115 REMARK 465 VAL P 116 REMARK 465 THR P 117 REMARK 465 LEU P 118 REMARK 465 PHE P 119 REMARK 465 PRO P 120 REMARK 465 PRO P 121 REMARK 465 SER P 122 REMARK 465 SER P 123 REMARK 465 GLU P 124 REMARK 465 GLU P 125 REMARK 465 LEU P 126 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 LYS L 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 PHE B 520 CB PHE B 520 CG -0.102 REMARK 500 ASP K 27B CB ASP K 27B CG -0.162 REMARK 500 TYR K 96 CB TYR K 96 CG -0.094 REMARK 500 PHE D 520 CB PHE D 520 CG -0.111 REMARK 500 ASP N 27B CB ASP N 27B CG -0.139 REMARK 500 TYR N 96 CB TYR N 96 CG -0.091 REMARK 500 PHE F 520 CB PHE F 520 CG -0.109 REMARK 500 ASP P 27B CB ASP P 27B CG -0.131 REMARK 500 VAL H 111 CB VAL H 111 CG2 0.135 REMARK 500 GLU L 1 CB GLU L 1 CG 0.131 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 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ARG A 327 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG A 456 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG A 469 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 ARG A 476 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ASP J 86 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 ASP K 27B CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 ARG K 54 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 TYR C 40 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG C 151 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG C 166 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 ARG C 166 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ARG C 327 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG C 469 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG C 476 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 ARG N 54 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 ARG E 151 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG E 151 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ARG E 469 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ARG E 503 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG P 54 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 ARG H 19 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG H 50 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 ARG L 54 NE - CZ - NH2 ANGL. DEV. = -3.8 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 CYS A 54 -169.62 -79.56 REMARK 500 ALA A 55 112.18 177.37 REMARK 500 THR A 71 -54.56 63.58 REMARK 500 PRO A 76 35.73 -92.69 REMARK 500 THR A 77 -166.36 79.00 REMARK 500 ASP A 78 118.04 -39.00 REMARK 500 TRP A 96 -20.40 84.90 REMARK 500 LEU A 122 56.26 -91.55 REMARK 500 GLU A 186 147.25 77.41 REMARK 500 ASN A 195 69.47 -103.09 REMARK 500 THR A 198 -50.10 -125.39 REMARK 500 THR A 257 -100.60 -97.78 REMARK 500 PHE A 391 68.80 -118.54 REMARK 500 MET A 426 -76.48 57.36 REMARK 500 THR A 465 114.33 93.07 REMARK 500 ASN B 625 -56.56 -121.67 REMARK 500 LEU J 82C 94.47 11.85 REMARK 500 ALA J 100 -28.41 71.22 REMARK 500 LYS J 100E -91.78 -115.24 REMARK 500 ASP K 27B -107.73 -164.76 REMARK 500 ASN K 31 57.43 -90.67 REMARK 500 VAL K 51 -57.68 70.56 REMARK 500 SER K 76 -89.47 -88.94 REMARK 500 ASP C 78 80.74 57.61 REMARK 500 TRP C 96 -20.34 83.93 REMARK 500 ASN C 195 65.32 -113.72 REMARK 500 THR C 198 -143.72 -100.18 REMARK 500 THR C 257 -100.34 -96.35 REMARK 500 PHE C 391 68.56 -115.38 REMARK 500 MET C 426 -68.09 57.32 REMARK 500 THR C 465 125.36 76.68 REMARK 500 ASP D 624 -2.60 -159.92 REMARK 500 ASN D 625 -66.71 -122.80 REMARK 500 ILE D 635 44.03 -86.69 REMARK 500 TYR D 638 56.82 -98.16 REMARK 500 LEU M 82C 93.23 11.03 REMARK 500 ALA M 100 -21.05 66.49 REMARK 500 LYS M 100E -88.41 -116.71 REMARK 500 ASP N 27B -109.35 -162.49 REMARK 500 ASN N 31 56.52 -90.76 REMARK 500 VAL N 51 -58.16 69.99 REMARK 500 SER N 76 -90.25 -88.35 REMARK 500 THR E 77 -94.06 -143.10 REMARK 500 ASP E 78 73.14 42.96 REMARK 500 PRO E 79 -84.86 -77.92 REMARK 500 PRO E 81 103.01 -45.58 REMARK 500 GLU E 87 -116.34 52.78 REMARK 500 ASN E 88 38.23 -80.96 REMARK 500 LYS E 97 -25.78 -148.56 REMARK 500 LEU E 122 58.77 -90.50 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25754 RELATED DB: EMDB REMARK 900 APEXGT2 IN COMPLEX WITH GT2-D42.16 AND RM20A3 FABS DBREF 7T9A A 31 513 PDB 7T9A 7T9A 31 513 DBREF 7T9A B 510 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 DBREF 7T9A J 1 113 PDB 7T9A 7T9A 1 113 DBREF 7T9A K 3 126 PDB 7T9A 7T9A 3 126 DBREF 7T9A C 31 513 PDB 7T9A 7T9A 31 513 DBREF 7T9A D 510 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 DBREF 7T9A M 1 113 PDB 7T9A 7T9A 1 113 DBREF 7T9A N 3 126 PDB 7T9A 7T9A 3 126 DBREF 7T9A E 31 513 PDB 7T9A 7T9A 31 513 DBREF 7T9A F 510 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 DBREF 7T9A O 1 113 PDB 7T9A 7T9A 1 113 DBREF 7T9A P 3 126 PDB 7T9A 7T9A 3 126 DBREF 7T9A H 1 113 PDB 7T9A 7T9A 1 113 DBREF 7T9A L 1 107 PDB 7T9A 7T9A 1 107 SEQADV 7T9A SER B 517 UNP Q2N0S8 PHE 518 CONFLICT SEQADV 7T9A PRO B 559 UNP Q2N0S8 ILE 558 CONFLICT SEQADV 7T9A PRO B 561 UNP Q2N0S8 ALA 560 CONFLICT SEQADV 7T9A ASP B 568 UNP Q2N0S8 LEU 567 CONFLICT SEQADV 7T9A HIS B 570 UNP Q2N0S8 VAL 569 CONFLICT SEQADV 7T9A HIS B 585 UNP Q2N0S8 ARG 584 CONFLICT SEQADV 7T9A CYS B 605 UNP Q2N0S8 THR 604 CONFLICT SEQADV 7T9A GLY B 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A THR B 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A LYS B 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS B 673 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A SER D 517 UNP Q2N0S8 PHE 518 CONFLICT SEQADV 7T9A PRO D 559 UNP Q2N0S8 ILE 558 CONFLICT SEQADV 7T9A PRO D 561 UNP Q2N0S8 ALA 560 CONFLICT SEQADV 7T9A ASP D 568 UNP Q2N0S8 LEU 567 CONFLICT SEQADV 7T9A HIS D 570 UNP Q2N0S8 VAL 569 CONFLICT SEQADV 7T9A HIS D 585 UNP Q2N0S8 ARG 584 CONFLICT SEQADV 7T9A CYS D 605 UNP Q2N0S8 THR 604 CONFLICT SEQADV 7T9A GLY D 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A THR D 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A LYS D 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS D 673 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A SER F 517 UNP Q2N0S8 PHE 518 CONFLICT SEQADV 7T9A PRO F 559 UNP Q2N0S8 ILE 558 CONFLICT SEQADV 7T9A PRO F 561 UNP Q2N0S8 ALA 560 CONFLICT SEQADV 7T9A ASP F 568 UNP Q2N0S8 LEU 567 CONFLICT SEQADV 7T9A HIS F 570 UNP Q2N0S8 VAL 569 CONFLICT SEQADV 7T9A HIS F 585 UNP Q2N0S8 ARG 584 CONFLICT SEQADV 7T9A CYS F 605 UNP Q2N0S8 THR 604 CONFLICT SEQADV 7T9A GLY F 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A THR F 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A LYS F 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 7T9A HIS F 673 UNP Q2N0S8 EXPRESSION TAG SEQRES 1 A 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 A 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 473 ASN CYS SER PHE ASN ALA THR THR GLU LEU ARG ASN LYS SEQRES 11 A 473 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 A 473 VAL PRO MET GLY GLU ASN SER THR ASN TYR ARG LEU ILE SEQRES 13 A 473 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 14 A 473 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 A 473 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 16 A 473 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 17 A 473 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 18 A 473 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 19 A 473 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 20 A 473 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 21 A 473 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 22 A 473 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 23 A 473 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 24 A 473 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 25 A 473 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 26 A 473 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 27 A 473 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 A 473 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 29 A 473 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 30 A 473 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 31 A 473 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 32 A 473 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 33 A 473 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 34 A 473 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 35 A 473 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 36 A 473 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 37 A 473 ARG ARG ARG ARG ARG SEQRES 1 B 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 B 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 B 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 B 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 B 162 HIS HIS HIS HIS HIS HIS 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 K 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 K 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 K 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 K 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 K 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 K 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 K 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 K 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 K 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 K 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 C 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 C 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 473 ASN CYS SER PHE ASN ALA THR THR GLU LEU ARG ASN LYS SEQRES 11 C 473 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 C 473 VAL PRO MET GLY GLU ASN SER THR ASN TYR ARG LEU ILE SEQRES 13 C 473 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 14 C 473 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 C 473 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 16 C 473 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 17 C 473 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 18 C 473 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 19 C 473 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 20 C 473 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 21 C 473 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 22 C 473 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 23 C 473 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 24 C 473 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 25 C 473 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 26 C 473 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 27 C 473 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 C 473 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 29 C 473 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 30 C 473 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 31 C 473 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 32 C 473 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 33 C 473 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 34 C 473 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 35 C 473 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 36 C 473 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 37 C 473 ARG ARG ARG ARG ARG SEQRES 1 D 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 D 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 D 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 D 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 D 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 D 162 HIS HIS HIS HIS HIS HIS SEQRES 1 M 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 M 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 M 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 M 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 M 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 M 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 M 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 M 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 M 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 M 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 N 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 N 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 N 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 N 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 N 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 N 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 N 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 N 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 N 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 N 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 E 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 E 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 E 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 E 473 ASN CYS SER PHE ASN ALA THR THR GLU LEU ARG ASN LYS SEQRES 11 E 473 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 E 473 VAL PRO MET GLY GLU ASN SER THR ASN TYR ARG LEU ILE SEQRES 13 E 473 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 14 E 473 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 15 E 473 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 16 E 473 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 17 E 473 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 18 E 473 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 19 E 473 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 20 E 473 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 21 E 473 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 22 E 473 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 23 E 473 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 24 E 473 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 25 E 473 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 26 E 473 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 27 E 473 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 E 473 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 29 E 473 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 30 E 473 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 31 E 473 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 32 E 473 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 33 E 473 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 34 E 473 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 35 E 473 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 36 E 473 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 37 E 473 ARG ARG ARG ARG ARG SEQRES 1 F 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 F 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 F 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 F 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 F 162 HIS HIS HIS HIS HIS HIS 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 P 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 P 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 P 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 P 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 P 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 P 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 P 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 P 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 P 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 P 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 1 H 134 GLU VAL GLN LEU VAL GLU SER GLY GLY ASP LEU VAL LYS SEQRES 2 H 134 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 134 PHE THR PHE SER ASP ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 H 134 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 H 134 SER ASN ILE ASP GLY GLY THR THR ASP TYR VAL ALA PRO SEQRES 6 H 134 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 134 ASN THR LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 H 134 ASP THR ALA VAL TYR TYR CYS THR THR GLY VAL GLU THR SEQRES 9 H 134 TYR ASP PHE TRP SER GLY TYS ASP ASP HIS TYS TYR ASP SEQRES 10 H 134 TYR TYR PHE ARG ASP VAL TRP GLY LYS GLY THR THR VAL SEQRES 11 H 134 THR VAL SER SER SEQRES 1 L 107 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 107 SER ALA GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 107 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 107 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 107 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 107 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 107 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 107 TYR GLY SER SER PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 107 ASP ILE LYS HET TYS H 100E 16 HET TYS H 100I 16 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 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 C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET NAG C 611 14 HET NAG C 612 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 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 F 701 14 HET NAG F 702 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET MAN Q 4 11 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 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 MAN S 6 11 HET MAN S 7 11 HET NAG T 1 14 HET FUC T 2 10 HET NAG U 1 14 HET FUC U 2 10 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 BMA Y 3 11 HET MAN Y 4 11 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET FUC a 2 10 HET NAG b 1 14 HET FUC b 2 10 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 h 1 14 HET FUC h 2 10 HET NAG i 1 14 HET FUC i 2 10 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM FUC ALPHA-L-FUCOSE FORMUL 13 TYS 2(C9 H11 N O6 S) FORMUL 15 NAG 78(C8 H15 N O6) FORMUL 59 BMA 5(C6 H12 O6) FORMUL 59 MAN 7(C6 H12 O6) FORMUL 62 FUC 6(C6 H12 O5) HELIX 1 AA1 ASN A 98 LYS A 117 1 20 HELIX 2 AA2 THR A 139 ARG A 151 5 5 HELIX 3 AA3 LYS A 335 ARG A 350 1 16 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 MET A 475 TYR A 484 1 10 HELIX 6 AA6 LEU B 521 SER B 526 5 6 HELIX 7 AA7 THR B 527 SER B 532 1 6 HELIX 8 AA8 THR B 534 ARG B 540 1 7 HELIX 9 AA9 GLY B 572 TRP B 596 1 25 HELIX 10 AB1 ASN B 618 TRP B 623 1 6 HELIX 11 AB2 THR B 627 ILE B 635 1 9 HELIX 12 AB3 TYR B 638 ALA B 662 1 25 HELIX 13 AB4 THR J 28 PHE J 32 5 5 HELIX 14 AB5 ASP J 61 LYS J 64 5 4 HELIX 15 AB6 ARG J 83 THR J 87 5 5 HELIX 16 AB7 GLN K 79 GLU K 83 5 5 HELIX 17 AB8 ASN C 99 SER C 115 1 17 HELIX 18 AB9 THR C 139 ARG C 151 5 5 HELIX 19 AC1 LYS C 335 ARG C 350 1 16 HELIX 20 AC2 ASP C 368 THR C 373 1 6 HELIX 21 AC3 MET C 475 TYR C 484 1 10 HELIX 22 AC4 LEU D 521 SER D 526 5 6 HELIX 23 AC5 THR D 527 SER D 532 1 6 HELIX 24 AC6 THR D 534 ARG D 540 1 7 HELIX 25 AC7 GLY D 572 TRP D 596 1 25 HELIX 26 AC8 ASN D 618 ASN D 625 1 8 HELIX 27 AC9 THR D 627 ILE D 635 1 9 HELIX 28 AD1 THR D 639 ALA D 662 1 24 HELIX 29 AD2 THR M 28 PHE M 32 5 5 HELIX 30 AD3 ASP M 61 LYS M 64 5 4 HELIX 31 AD4 ARG M 83 THR M 87 5 5 HELIX 32 AD5 GLN N 79 GLU N 83 5 5 HELIX 33 AD6 ASN E 99 SER E 115 1 17 HELIX 34 AD7 THR E 139 ARG E 151 5 5 HELIX 35 AD8 ASN E 195 ASN E 197 5 3 HELIX 36 AD9 LYS E 335 ARG E 350 1 16 HELIX 37 AE1 ASP E 368 THR E 373 1 6 HELIX 38 AE2 MET E 475 TYR E 484 1 10 HELIX 39 AE3 THR F 527 SER F 532 1 6 HELIX 40 AE4 THR F 534 ARG F 540 1 7 HELIX 41 AE5 GLY F 572 TRP F 596 1 25 HELIX 42 AE6 ASN F 618 TRP F 623 1 6 HELIX 43 AE7 THR F 627 LYS F 633 1 7 HELIX 44 AE8 ILE F 635 ASN F 637 5 3 HELIX 45 AE9 TYR F 638 ALA F 662 1 25 HELIX 46 AF1 THR O 28 PHE O 32 5 5 HELIX 47 AF2 ASP O 61 LYS O 64 5 4 HELIX 48 AF3 ARG O 83 THR O 87 5 5 HELIX 49 AF4 GLN P 79 GLU P 83 5 5 HELIX 50 AF5 SER H 52A GLY H 54 5 5 HELIX 51 AF6 ALA H 61 LYS H 64 5 4 HELIX 52 AF7 LYS H 83 THR H 87 5 5 HELIX 53 AF8 SER L 29 SER L 31 5 3 HELIX 54 AF9 GLU L 79 PHE L 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 TYR A 39 O GLY A 495 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 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 ILE A 84 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 GLU A 91 ASN A 94 0 SHEET 2 AA3 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA4 5 ARG A 169 TYR A 177 0 SHEET 2 AA4 5 LEU A 154 THR A 162 -1 N ALA A 161 O GLN A 170 SHEET 3 AA4 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AA4 5 ASN A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA4 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA5 3 ILE A 201 GLN A 203 0 SHEET 2 AA5 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA5 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA612 LEU A 259 LEU A 261 0 SHEET 2 AA612 ILE A 271 ARG A 273 0 SHEET 3 AA612 ILE A 284 GLY A 312 -1 O LEU A 285 N ARG A 273 SHEET 4 AA612 GLN A 315 ILE A 323A-1 O GLY A 321 N THR A 303 SHEET 5 AA612 ALA A 329 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 6 AA612 ILE A 358 PHE A 361 0 SHEET 7 AA612 HIS A 374 CYS A 378 0 SHEET 8 AA612 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 9 AA612 SER A 393 ILE A 396 -1 O TRP A 395 N ILE A 359 SHEET 10 AA612 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 11 AA612 GLY A 441 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 12 AA612 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA7 4 GLN J 3 GLU J 6 0 SHEET 2 AA7 4 SER J 17 SER J 25 -1 O ARG J 23 N VAL J 5 SHEET 3 AA7 4 THR J 77 HIS J 82A-1 O LEU J 80 N LEU J 20 SHEET 4 AA7 4 PHE J 67 ASP J 72 -1 N THR J 68 O GLN J 81 SHEET 1 AA8 7 LEU J 11 VAL J 12 0 SHEET 2 AA8 7 MET J 34 GLN J 39 0 SHEET 3 AA8 7 LEU J 45 ILE J 51 -1 O ILE J 51 N MET J 34 SHEET 4 AA8 7 THR J 57 TYR J 59 -1 O PHE J 58 N LEU J 50 SHEET 5 AA8 7 ALA J 88 GLY J 95 -1 O TYR J 91 N VAL J 37 SHEET 6 AA8 7 PHE J 100H TRP J 103 -1 O PHE J 102 N THR J 94 SHEET 7 AA8 7 ALA J 107 VAL J 111 -1 O ALA J 107 N TYR J 90 SHEET 1 AA9 6 SER K 12 GLY K 13 0 SHEET 2 AA9 6 VAL K 33 GLN K 38 0 SHEET 3 AA9 6 LYS K 45 ILE K 48 -1 O MET K 47 N TRP K 35 SHEET 4 AA9 6 ALA K 84 TYR K 91 -1 O ASP K 85 N GLN K 38 SHEET 5 AA9 6 TYR K 96 PHE K 98 -1 O ILE K 97 N ALA K 90 SHEET 6 AA9 6 THR K 102 VAL K 106 -1 O THR K 102 N TYR K 86 SHEET 1 AB1 3 VAL K 19 THR K 24 0 SHEET 2 AB1 3 THR K 70 ILE K 75 -1 O ALA K 71 N CYS K 23 SHEET 3 AB1 3 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AB2 3 LEU C 494 THR C 499 0 SHEET 2 AB2 3 TRP C 35 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AB2 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL C 36 SHEET 1 AB3 5 TRP C 45 ASP C 47 0 SHEET 2 AB3 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB3 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB3 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB3 5 GLU C 83 ILE C 84 -1 N ILE C 84 O THR C 244 SHEET 1 AB4 3 VAL C 75 PRO C 76 0 SHEET 2 AB4 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AB4 3 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AB5 2 GLU C 91 ASN C 94 0 SHEET 2 AB5 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB6 5 ARG C 169 TYR C 177 0 SHEET 2 AB6 5 LEU C 154 THR C 162 -1 N PHE C 159 O VAL C 172 SHEET 3 AB6 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AB6 5 ASN C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB6 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB7 3 ILE C 201 GLN C 203 0 SHEET 2 AB7 3 ALA C 433 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AB7 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB812 LEU C 259 LEU C 261 0 SHEET 2 AB812 ILE C 271 SER C 274 0 SHEET 3 AB812 ILE C 284 GLY C 312 -1 O LEU C 285 N ARG C 273 SHEET 4 AB812 GLN C 315 ILE C 323A-1 O GLN C 315 N ILE C 309 SHEET 5 AB812 ALA C 329 SER C 334 -1 O ASN C 332 N ASN C 295 SHEET 6 AB812 ILE C 358 PHE C 361 0 SHEET 7 AB812 HIS C 374 CYS C 378 0 SHEET 8 AB812 GLU C 381 CYS C 385 -1 O CYS C 385 N HIS C 374 SHEET 9 AB812 SER C 393 ILE C 396 -1 O TRP C 395 N ILE C 359 SHEET 10 AB812 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 11 AB812 GLY C 441 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 12 AB812 GLU C 466 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AB9 4 GLN M 3 GLU M 6 0 SHEET 2 AB9 4 SER M 17 SER M 25 -1 O ARG M 23 N VAL M 5 SHEET 3 AB9 4 THR M 77 HIS M 82A-1 O LEU M 80 N LEU M 20 SHEET 4 AB9 4 PHE M 67 ASP M 72 -1 N THR M 68 O GLN M 81 SHEET 1 AC1 7 LEU M 11 VAL M 12 0 SHEET 2 AC1 7 MET M 34 GLN M 39 0 SHEET 3 AC1 7 GLU M 46 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 4 AC1 7 THR M 57 TYR M 59 -1 O PHE M 58 N LEU M 50 SHEET 5 AC1 7 ALA M 88 GLY M 95 -1 O TYR M 91 N VAL M 37 SHEET 6 AC1 7 PHE M 100H TRP M 103 -1 O ASP M 101 N THR M 94 SHEET 7 AC1 7 ALA M 107 VAL M 111 -1 O ALA M 107 N TYR M 90 SHEET 1 AC2 6 SER N 12 GLY N 13 0 SHEET 2 AC2 6 VAL N 33 GLN N 38 0 SHEET 3 AC2 6 LYS N 45 ILE N 48 -1 O MET N 47 N TRP N 35 SHEET 4 AC2 6 ALA N 84 TYR N 91 -1 O ASP N 85 N GLN N 38 SHEET 5 AC2 6 TYR N 96 PHE N 98 -1 O ILE N 97 N ALA N 90 SHEET 6 AC2 6 THR N 102 VAL N 106 -1 O THR N 102 N TYR N 86 SHEET 1 AC3 3 VAL N 19 THR N 24 0 SHEET 2 AC3 3 THR N 70 ILE N 75 -1 O ALA N 71 N CYS N 23 SHEET 3 AC3 3 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AC4 3 LEU E 494 THR E 499 0 SHEET 2 AC4 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AC4 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AC5 5 TRP E 45 ASP E 47 0 SHEET 2 AC5 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AC5 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AC5 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC5 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC6 2 PHE E 53 ALA E 55 0 SHEET 2 AC6 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AC7 2 GLU E 91 ASN E 94 0 SHEET 2 AC7 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AC8 5 ARG E 169 TYR E 177 0 SHEET 2 AC8 5 LEU E 154 THR E 162 -1 N PHE E 159 O VAL E 172 SHEET 3 AC8 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AC8 5 ASN E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC8 5 ILE E 181 PRO E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC9 3 ILE E 201 GLN E 203 0 SHEET 2 AC9 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC9 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AD112 LEU E 259 LEU E 261 0 SHEET 2 AD112 ILE E 271 SER E 274 0 SHEET 3 AD112 ILE E 284 GLY E 312 -1 O LEU E 285 N ARG E 273 SHEET 4 AD112 GLN E 315 ILE E 323A-1 O ILE E 323A N ASN E 301 SHEET 5 AD112 ALA E 329 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 6 AD112 ILE E 358 PHE E 361 0 SHEET 7 AD112 HIS E 374 CYS E 378 0 SHEET 8 AD112 GLU E 381 CYS E 385 -1 O PHE E 383 N PHE E 376 SHEET 9 AD112 SER E 393 ILE E 396 -1 O TRP E 395 N ILE E 359 SHEET 10 AD112 SER E 413 LYS E 421 -1 O ARG E 419 N TYR E 384 SHEET 11 AD112 GLY E 441 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 12 AD112 GLU E 466 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 1 AD2 4 GLN O 3 GLU O 6 0 SHEET 2 AD2 4 SER O 17 SER O 25 -1 O ARG O 23 N VAL O 5 SHEET 3 AD2 4 THR O 77 HIS O 82A-1 O LEU O 80 N LEU O 20 SHEET 4 AD2 4 PHE O 67 ASP O 72 -1 N THR O 68 O GLN O 81 SHEET 1 AD3 7 LEU O 11 VAL O 12 0 SHEET 2 AD3 7 MET O 34 GLN O 39 0 SHEET 3 AD3 7 GLU O 46 ILE O 51 -1 O ILE O 51 N MET O 34 SHEET 4 AD3 7 THR O 57 TYR O 59 -1 O PHE O 58 N LEU O 50 SHEET 5 AD3 7 ALA O 88 GLY O 95 -1 O TYR O 91 N VAL O 37 SHEET 6 AD3 7 PHE O 100H TRP O 103 -1 O ASP O 101 N THR O 94 SHEET 7 AD3 7 ALA O 107 VAL O 111 -1 O ALA O 107 N TYR O 90 SHEET 1 AD4 6 SER P 12 GLY P 13 0 SHEET 2 AD4 6 VAL P 33 GLN P 38 0 SHEET 3 AD4 6 LYS P 45 ILE P 48 -1 O MET P 47 N TRP P 35 SHEET 4 AD4 6 ALA P 84 TYR P 91 -1 O ASP P 85 N GLN P 38 SHEET 5 AD4 6 TYR P 96 PHE P 98 -1 O ILE P 97 N ALA P 90 SHEET 6 AD4 6 THR P 102 VAL P 106 -1 O THR P 102 N TYR P 86 SHEET 1 AD5 3 VAL P 19 THR P 24 0 SHEET 2 AD5 3 THR P 70 ILE P 75 -1 O ALA P 71 N CYS P 23 SHEET 3 AD5 3 PHE P 62 SER P 67 -1 N SER P 65 O SER P 72 SHEET 1 AD6 4 GLN H 3 SER H 7 0 SHEET 2 AD6 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AD6 4 THR H 77 ASN H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AD6 4 PHE H 67 ARG H 71 -1 N SER H 70 O TYR H 79 SHEET 1 AD7 6 MET H 34 GLN H 39 0 SHEET 2 AD7 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 3 AD7 6 THR H 57 TYR H 59 -1 O ASP H 58 N ARG H 50 SHEET 4 AD7 6 ALA H 88 PHE H 100A-1 O TYR H 91 N VAL H 37 SHEET 5 AD7 6 TYR H 100J TRP H 103 -1 O ARG H 100O N VAL H 96 SHEET 6 AD7 6 THR H 107 VAL H 109 -1 O THR H 107 N TYR H 90 SHEET 1 AD8 4 LEU L 4 SER L 7 0 SHEET 2 AD8 4 LEU L 21 ALA L 25 -1 O SER L 22 N SER L 7 SHEET 3 AD8 4 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AD8 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AD9 6 LEU L 11 SER L 12 0 SHEET 2 AD9 6 THR L 102 ASP L 105 1 O ASP L 105 N LEU L 11 SHEET 3 AD9 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD9 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AD9 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AD9 6 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49 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 2.05 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.02 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.02 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 13 CYS K 23 CYS K 88 1555 1555 2.02 SSBOND 14 CYS C 119 CYS C 205 1555 1555 2.05 SSBOND 15 CYS C 126 CYS C 196 1555 1555 2.05 SSBOND 16 CYS C 131 CYS C 157 1555 1555 2.02 SSBOND 17 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 18 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 19 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 20 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 21 CYS C 385 CYS C 418 1555 1555 2.02 SSBOND 22 CYS C 501 CYS D 605 1555 1555 2.02 SSBOND 23 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 24 CYS M 22 CYS M 92 1555 1555 2.05 SSBOND 25 CYS N 23 CYS N 88 1555 1555 2.02 SSBOND 26 CYS E 119 CYS E 205 1555 1555 2.06 SSBOND 27 CYS E 126 CYS E 196 1555 1555 2.05 SSBOND 28 CYS E 131 CYS E 157 1555 1555 2.04 SSBOND 29 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 30 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 31 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 32 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 33 CYS E 385 CYS E 418 1555 1555 2.02 SSBOND 34 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 35 CYS O 22 CYS O 92 1555 1555 2.04 SSBOND 36 CYS P 23 CYS P 88 1555 1555 2.02 SSBOND 37 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 38 CYS L 23 CYS L 88 1555 1555 2.08 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.51 LINK ND2 ASN A 133 C1 NAG A 612 1555 1555 1.52 LINK ND2 ASN A 137 C1 NAG A 603 1555 1555 1.52 LINK ND2 ASN A 156 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN A 160 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 611 1555 1555 1.45 LINK ND2 ASN A 234 C1 NAG A 602 1555 1555 1.51 LINK ND2 ASN A 262 C1 NAG Q 1 1555 1555 1.52 LINK ND2 ASN A 276 C1 NAG A 605 1555 1555 1.52 LINK ND2 ASN A 295 C1 NAG A 608 1555 1555 1.52 LINK ND2 ASN A 301 C1 NAG A 610 1555 1555 1.53 LINK ND2 ASN A 332 C1 NAG I 1 1555 1555 1.49 LINK ND2 ASN A 339 C1 NAG A 607 1555 1555 1.53 LINK ND2 ASN A 355 C1 NAG A 604 1555 1555 1.51 LINK ND2 ASN A 386 C1 NAG G 1 1555 1555 1.53 LINK ND2 ASN A 392 C1 NAG A 606 1555 1555 1.52 LINK ND2 ASN A 448 C1 NAG A 609 1555 1555 1.53 LINK ND2 ASN B 611 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN B 618 C1 NAG T 1 1555 1555 1.46 LINK ND2 ASN B 625 C1 NAG B 702 1555 1555 1.43 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.43 LINK ND2 ASN C 88 C1 NAG C 601 1555 1555 1.51 LINK ND2 ASN C 133 C1 NAG C 612 1555 1555 1.51 LINK ND2 ASN C 137 C1 NAG C 603 1555 1555 1.52 LINK ND2 ASN C 156 C1 NAG Z 1 1555 1555 1.51 LINK ND2 ASN C 160 C1 NAG V 1 1555 1555 1.43 LINK ND2 ASN C 197 C1 NAG C 611 1555 1555 1.43 LINK ND2 ASN C 234 C1 NAG C 602 1555 1555 1.51 LINK ND2 ASN C 262 C1 NAG Y 1 1555 1555 1.51 LINK ND2 ASN C 276 C1 NAG C 605 1555 1555 1.52 LINK ND2 ASN C 295 C1 NAG C 608 1555 1555 1.51 LINK ND2 ASN C 301 C1 NAG C 610 1555 1555 1.53 LINK ND2 ASN C 332 C1 NAG X 1 1555 1555 1.49 LINK ND2 ASN C 339 C1 NAG C 607 1555 1555 1.52 LINK ND2 ASN C 355 C1 NAG C 604 1555 1555 1.51 LINK ND2 ASN C 386 C1 NAG W 1 1555 1555 1.52 LINK ND2 ASN C 392 C1 NAG C 606 1555 1555 1.52 LINK ND2 ASN C 448 C1 NAG C 609 1555 1555 1.52 LINK ND2 ASN D 611 C1 NAG b 1 1555 1555 1.43 LINK ND2 ASN D 618 C1 NAG a 1 1555 1555 1.43 LINK ND2 ASN D 625 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 637 C1 NAG D 702 1555 1555 1.43 LINK ND2 ASN E 88 C1 NAG E 601 1555 1555 1.46 LINK ND2 ASN E 133 C1 NAG E 612 1555 1555 1.52 LINK ND2 ASN E 137 C1 NAG E 603 1555 1555 1.52 LINK ND2 ASN E 156 C1 NAG f 1 1555 1555 1.52 LINK ND2 ASN E 160 C1 NAG g 1 1555 1555 1.43 LINK ND2 ASN E 197 C1 NAG E 611 1555 1555 1.45 LINK ND2 ASN E 234 C1 NAG E 602 1555 1555 1.51 LINK ND2 ASN E 262 C1 NAG e 1 1555 1555 1.52 LINK ND2 ASN E 276 C1 NAG E 605 1555 1555 1.53 LINK ND2 ASN E 295 C1 NAG E 608 1555 1555 1.52 LINK ND2 ASN E 301 C1 NAG E 610 1555 1555 1.53 LINK ND2 ASN E 332 C1 NAG d 1 1555 1555 1.49 LINK ND2 ASN E 339 C1 NAG E 607 1555 1555 1.52 LINK ND2 ASN E 355 C1 NAG E 604 1555 1555 1.51 LINK ND2 ASN E 386 C1 NAG c 1 1555 1555 1.52 LINK ND2 ASN E 392 C1 NAG E 606 1555 1555 1.52 LINK ND2 ASN E 448 C1 NAG E 609 1555 1555 1.53 LINK ND2 ASN F 611 C1 NAG i 1 1555 1555 1.43 LINK ND2 ASN F 618 C1 NAG h 1 1555 1555 1.48 LINK ND2 ASN F 625 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 701 1555 1555 1.43 LINK C GLY H 100D N TYS H 100E 1555 1555 1.35 LINK C TYS H 100E N ASP H 100F 1555 1555 1.35 LINK C HIS H 100H N TYS H 100I 1555 1555 1.33 LINK C TYS H 100I N TYR H 100J 1555 1555 1.34 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.50 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.51 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.51 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.51 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.52 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.43 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 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 O6 BMA S 3 C1 MAN S 4 1555 1555 1.44 LINK O3 BMA S 3 C1 MAN S 7 1555 1555 1.44 LINK O3 MAN S 4 C1 MAN S 5 1555 1555 1.44 LINK O6 MAN S 4 C1 MAN S 6 1555 1555 1.45 LINK O6 NAG T 1 C1 FUC T 2 1555 1555 1.44 LINK O6 NAG U 1 C1 FUC U 2 1555 1555 1.43 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.50 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.52 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.51 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.52 LINK O3 BMA Y 3 C1 MAN Y 4 1555 1555 1.52 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.51 LINK O6 NAG a 1 C1 FUC a 2 1555 1555 1.44 LINK O6 NAG b 1 C1 FUC b 2 1555 1555 1.45 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.50 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.52 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.52 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.51 LINK O3 BMA e 3 C1 MAN e 4 1555 1555 1.52 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.50 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O6 NAG h 1 C1 FUC h 2 1555 1555 1.48 LINK O6 NAG i 1 C1 FUC i 2 1555 1555 1.46 CISPEP 1 SER L 7 PRO L 8 0 1.48 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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