HEADER VIRAL PROTEIN 11-JUL-25 9PIV TITLE HIV-1 BNAB 9-71 IN COMPLEX WITH BG505 MD39 SOSIP AND RM19R COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM19R LIGHT CHAIN FV; COMPND 3 CHAIN: G, I, K; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM19R HEAVY CHAIN FV; COMPND 7 CHAIN: J, O, P; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 9-71 HEAVY CHAIN FV; COMPND 11 CHAIN: H, M, N; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 9-71 LIGHT CHAIN FV; COMPND 15 CHAIN: L, Q, R; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 19 CHAIN: B, E, F; COMPND 20 SYNONYM: ENV POLYPROTEIN; COMPND 21 ENGINEERED: YES; COMPND 22 MUTATION: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: ENVELOPE GLYCOPROTEIN GP41 - BG505 MD39; COMPND 25 CHAIN: A, C, D; COMPND 26 SYNONYM: ENV POLYPROTEIN; COMPND 27 ENGINEERED: YES; COMPND 28 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 9 ORGANISM_TAXID: 9544; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 29 ORGANISM_TAXID: 11676; SOURCE 30 GENE: ENV; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 36 ORGANISM_TAXID: 11676; SOURCE 37 GENE: ENV; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, SOSIP, HUMAN, BROADLY NEUTRALIZING ANTIBODY, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR D.L.V.BADER,G.OZOROWSKI,A.B.WARD REVDAT 1 04-MAR-26 9PIV 0 JRNL AUTH D.L.V.BADER,C.T.FLYNN JRNL TITL STRUCTURAL AND IMMUNOGENETIC SIGNATURES GUIDE CD4-MIMETIC JRNL TITL 2 HIV VACCINE DEVELOPMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, LEGINON, GCTF, ROSETTA, REMARK 3 PHENIX, CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 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 : 230472 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 9PIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-25. REMARK 100 THE DEPOSITION ID IS D_1000297913. 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 BNAB 9-71 IN COMPLEX WITH REMARK 245 BG505 MD39 SOSIP AND RM19R REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.88 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 : 5300 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 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: 18-MERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 18-MERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, J, H, L, B, A, I, O, M, Q, REMARK 350 AND CHAINS: E, C, K, P, N, R, F, D, 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, j, k, l, m 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 G 1 REMARK 465 ILE G 2 REMARK 465 ILE G 106 REMARK 465 LYS G 107 REMARK 465 VAL J 111 REMARK 465 SER J 112 REMARK 465 SER J 113 REMARK 465 GLU L 1 REMARK 465 LYS L 107 REMARK 465 MET B 0 REMARK 465 GLY B 1 REMARK 465 ILE B 2 REMARK 465 LEU B 3 REMARK 465 PRO B 4 REMARK 465 SER B 5 REMARK 465 PRO B 6 REMARK 465 GLY B 7 REMARK 465 MET B 8 REMARK 465 PRO B 9 REMARK 465 ALA B 10 REMARK 465 LEU B 11 REMARK 465 LEU B 12 REMARK 465 SER B 13 REMARK 465 LEU B 14 REMARK 465 VAL B 15 REMARK 465 SER B 16 REMARK 465 LEU B 17 REMARK 465 LEU B 18 REMARK 465 SER B 19 REMARK 465 VAL B 20 REMARK 465 LEU B 21 REMARK 465 LEU B 22 REMARK 465 MET B 23 REMARK 465 GLY B 24 REMARK 465 CYS B 25 REMARK 465 VAL B 26 REMARK 465 ALA B 27 REMARK 465 GLU B 28 REMARK 465 THR B 29 REMARK 465 GLY B 30 REMARK 465 ALA B 31 REMARK 465 GLU B 185A REMARK 465 ASN B 185B REMARK 465 GLN B 185C REMARK 465 GLY B 185D REMARK 465 ASN B 185E REMARK 465 ARG B 185F REMARK 465 SER B 185G REMARK 465 ASN B 185H REMARK 465 ASN B 185I REMARK 465 SER B 185J REMARK 465 ASN B 185K REMARK 465 ASN B 399 REMARK 465 THR B 400 REMARK 465 SER B 401 REMARK 465 VAL B 402 REMARK 465 GLN B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 SER B 407 REMARK 465 THR B 408 REMARK 465 GLY B 409 REMARK 465 SER B 410 REMARK 465 VAL B 505 REMARK 465 VAL B 506 REMARK 465 GLY B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 REMARK 465 ARG B 512 REMARK 465 ARG B 513 REMARK 465 ALA A 512 REMARK 465 VAL A 513 REMARK 465 GLY A 514 REMARK 465 ILE A 515 REMARK 465 GLY A 516 REMARK 465 ALA A 517 REMARK 465 VAL A 518 REMARK 465 GLY A 547 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 PRO A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 ASP A 568 REMARK 465 ALA A 662 REMARK 465 LEU A 663 REMARK 465 ASP A 664 REMARK 465 GLY A 665 REMARK 465 THR A 666 REMARK 465 LYS A 667 REMARK 465 HIS A 668 REMARK 465 HIS A 669 REMARK 465 HIS A 670 REMARK 465 HIS A 671 REMARK 465 HIS A 672 REMARK 465 HIS A 673 REMARK 465 ALA I 1 REMARK 465 ILE I 2 REMARK 465 ILE I 106 REMARK 465 LYS I 107 REMARK 465 VAL O 111 REMARK 465 SER O 112 REMARK 465 SER O 113 REMARK 465 GLU Q 1 REMARK 465 LYS Q 107 REMARK 465 MET E 0 REMARK 465 GLY E 1 REMARK 465 ILE E 2 REMARK 465 LEU E 3 REMARK 465 PRO E 4 REMARK 465 SER E 5 REMARK 465 PRO E 6 REMARK 465 GLY E 7 REMARK 465 MET E 8 REMARK 465 PRO E 9 REMARK 465 ALA E 10 REMARK 465 LEU E 11 REMARK 465 LEU E 12 REMARK 465 SER E 13 REMARK 465 LEU E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 LEU E 17 REMARK 465 LEU E 18 REMARK 465 SER E 19 REMARK 465 VAL E 20 REMARK 465 LEU E 21 REMARK 465 LEU E 22 REMARK 465 MET E 23 REMARK 465 GLY E 24 REMARK 465 CYS E 25 REMARK 465 VAL E 26 REMARK 465 ALA E 27 REMARK 465 GLU E 28 REMARK 465 THR E 29 REMARK 465 GLY E 30 REMARK 465 ALA E 31 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 GLY E 185D REMARK 465 ASN E 185E REMARK 465 ARG E 185F REMARK 465 SER E 185G REMARK 465 ASN E 185H REMARK 465 ASN E 185I REMARK 465 SER E 185J REMARK 465 ASN E 185K REMARK 465 ASN E 399 REMARK 465 THR E 400 REMARK 465 SER E 401 REMARK 465 VAL E 402 REMARK 465 GLN E 403 REMARK 465 GLY E 404 REMARK 465 SER E 405 REMARK 465 ASN E 406 REMARK 465 SER E 407 REMARK 465 THR E 408 REMARK 465 GLY E 409 REMARK 465 SER E 410 REMARK 465 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 C 512 REMARK 465 VAL C 513 REMARK 465 GLY C 514 REMARK 465 ILE C 515 REMARK 465 GLY C 516 REMARK 465 ALA C 517 REMARK 465 VAL C 518 REMARK 465 GLY C 547 REMARK 465 ILE C 548 REMARK 465 VAL C 549 REMARK 465 GLN C 550 REMARK 465 GLN C 551 REMARK 465 GLN C 552 REMARK 465 SER C 553 REMARK 465 ASN C 554 REMARK 465 LEU C 555 REMARK 465 LEU C 556 REMARK 465 ARG C 557 REMARK 465 ALA C 558 REMARK 465 PRO C 559 REMARK 465 GLU C 560 REMARK 465 PRO C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 HIS C 564 REMARK 465 LEU C 565 REMARK 465 LEU C 566 REMARK 465 LYS C 567 REMARK 465 ASP C 568 REMARK 465 ALA C 662 REMARK 465 LEU C 663 REMARK 465 ASP C 664 REMARK 465 GLY C 665 REMARK 465 THR C 666 REMARK 465 LYS C 667 REMARK 465 HIS C 668 REMARK 465 HIS C 669 REMARK 465 HIS C 670 REMARK 465 HIS C 671 REMARK 465 HIS C 672 REMARK 465 HIS C 673 REMARK 465 ALA K 1 REMARK 465 ILE K 2 REMARK 465 ILE K 106 REMARK 465 LYS K 107 REMARK 465 VAL P 111 REMARK 465 SER P 112 REMARK 465 SER P 113 REMARK 465 GLU R 1 REMARK 465 LYS R 107 REMARK 465 MET F 0 REMARK 465 GLY F 1 REMARK 465 ILE F 2 REMARK 465 LEU F 3 REMARK 465 PRO F 4 REMARK 465 SER F 5 REMARK 465 PRO F 6 REMARK 465 GLY F 7 REMARK 465 MET F 8 REMARK 465 PRO F 9 REMARK 465 ALA F 10 REMARK 465 LEU F 11 REMARK 465 LEU F 12 REMARK 465 SER F 13 REMARK 465 LEU F 14 REMARK 465 VAL F 15 REMARK 465 SER F 16 REMARK 465 LEU F 17 REMARK 465 LEU F 18 REMARK 465 SER F 19 REMARK 465 VAL F 20 REMARK 465 LEU F 21 REMARK 465 LEU F 22 REMARK 465 MET F 23 REMARK 465 GLY F 24 REMARK 465 CYS F 25 REMARK 465 VAL F 26 REMARK 465 ALA F 27 REMARK 465 GLU F 28 REMARK 465 THR F 29 REMARK 465 GLY F 30 REMARK 465 ALA F 31 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 185K 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 VAL 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 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 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 ALA D 662 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 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 ASP G 30 -130.73 54.20 REMARK 500 VAL G 51 -57.15 71.66 REMARK 500 GLU G 91 17.07 -141.09 REMARK 500 SER J 15 -11.64 84.76 REMARK 500 PHE H 97 18.87 55.42 REMARK 500 ARG H 100B -49.61 70.26 REMARK 500 SER H 100D 4.51 81.75 REMARK 500 THR L 51 -47.27 71.35 REMARK 500 ILE L 94 -49.37 67.44 REMARK 500 ASN B 67 174.63 78.49 REMARK 500 MET B 150 34.24 -140.89 REMARK 500 GLN B 258 -57.14 64.19 REMARK 500 ASN B 276 -32.71 -136.10 REMARK 500 ILE B 277 -58.16 67.41 REMARK 500 SER B 460 164.79 73.45 REMARK 500 SER B 463 -6.11 -54.90 REMARK 500 THR B 464 -37.77 66.54 REMARK 500 GLU B 492 79.42 -119.54 REMARK 500 TYR A 638 -0.50 75.64 REMARK 500 ASP I 30 -130.72 54.17 REMARK 500 VAL I 51 -57.18 71.65 REMARK 500 GLU I 91 17.05 -141.08 REMARK 500 SER O 15 -11.63 84.72 REMARK 500 PHE M 97 18.93 55.42 REMARK 500 ARG M 100B -49.69 70.31 REMARK 500 SER M 100D 4.51 81.78 REMARK 500 THR Q 51 -47.25 71.28 REMARK 500 ILE Q 94 -49.38 67.45 REMARK 500 ASN E 67 174.63 78.50 REMARK 500 MET E 150 34.27 -140.93 REMARK 500 GLN E 258 -57.13 64.19 REMARK 500 ASN E 276 -32.73 -136.11 REMARK 500 ILE E 277 -58.09 67.41 REMARK 500 SER E 460 164.83 73.46 REMARK 500 SER E 463 -6.11 -54.91 REMARK 500 THR E 464 -37.73 66.52 REMARK 500 GLU E 492 79.45 -119.60 REMARK 500 TYR C 638 -0.48 75.62 REMARK 500 ASP K 30 -130.75 54.22 REMARK 500 VAL K 51 -57.19 71.65 REMARK 500 GLU K 91 17.10 -141.09 REMARK 500 SER P 15 -11.64 84.71 REMARK 500 PHE N 97 18.94 55.40 REMARK 500 ARG N 100B -49.63 70.31 REMARK 500 SER N 100D 4.50 81.77 REMARK 500 THR R 51 -47.25 71.31 REMARK 500 ILE R 94 -49.35 67.42 REMARK 500 ASN F 67 174.63 78.48 REMARK 500 MET F 150 34.31 -140.89 REMARK 500 GLN F 258 -57.13 64.19 REMARK 500 REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-71678 RELATED DB: EMDB REMARK 900 HIV-1 BNAB 9-71 IN COMPLEX WITH BG505 MD39 SOSIP AND RM19R DBREF 9PIV G 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV J 1 113 PDB 9PIV 9PIV 1 113 DBREF 9PIV H 3 113 PDB 9PIV 9PIV 3 113 DBREF 9PIV L 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV B 31 513 UNP Q2N0S5 Q2N0S5_HV1 30 510 DBREF 9PIV A 512 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 DBREF 9PIV I 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV O 1 113 PDB 9PIV 9PIV 1 113 DBREF 9PIV M 3 113 PDB 9PIV 9PIV 3 113 DBREF 9PIV Q 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV E 31 513 UNP Q2N0S5 Q2N0S5_HV1 30 510 DBREF 9PIV C 512 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 DBREF 9PIV K 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV P 1 113 PDB 9PIV 9PIV 1 113 DBREF 9PIV N 3 113 PDB 9PIV 9PIV 3 113 DBREF 9PIV R 1 107 PDB 9PIV 9PIV 1 107 DBREF 9PIV F 31 513 UNP Q2N0S5 Q2N0S5_HV1 30 510 DBREF 9PIV D 512 664 UNP Q2N0S8 Q2N0S8_9HIV1 511 663 SEQADV 9PIV MET B 0 UNP Q2N0S5 INITIATING METHIONINE SEQADV 9PIV GLY B 1 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ILE B 2 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 3 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO B 4 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER B 5 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO B 6 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY B 7 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET B 8 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO B 9 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA B 10 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 11 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 12 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER B 13 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 14 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL B 15 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER B 16 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 17 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 18 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER B 19 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL B 20 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 21 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU B 22 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET B 23 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY B 24 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV CYS B 25 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL B 26 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA B 27 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU B 28 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV THR B 29 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY B 30 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU B 106 UNP Q2N0S5 THR 105 ENGINEERED MUTATION SEQADV 9PIV ILE B 271 UNP Q2N0S5 MET 270 ENGINEERED MUTATION SEQADV 9PIV LEU B 288 UNP Q2N0S5 PHE 287 ENGINEERED MUTATION SEQADV 9PIV VAL B 304 UNP Q2N0S5 ARG 303 ENGINEERED MUTATION SEQADV 9PIV TYR B 319 UNP Q2N0S5 ALA 316 ENGINEERED MUTATION SEQADV 9PIV ASN B 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9PIV GLN B 363 UNP Q2N0S5 ASN 361 ENGINEERED MUTATION SEQADV 9PIV CYS B 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9PIV ARG B 509 UNP Q2N0S5 GLU 506 ENGINEERED MUTATION SEQADV 9PIV ARG B 510 UNP Q2N0S5 LYS 507 ENGINEERED MUTATION SEQADV 9PIV ARG B 512 UNP Q2N0S5 ALA 509 ENGINEERED MUTATION SEQADV 9PIV ARG B 513 UNP Q2N0S5 VAL 510 ENGINEERED MUTATION SEQADV 9PIV SER A 519 UNP Q2N0S8 PHE 518 ENGINEERED MUTATION SEQADV 9PIV PRO A 559 UNP Q2N0S8 ILE 558 ENGINEERED MUTATION SEQADV 9PIV PRO A 561 UNP Q2N0S8 ALA 560 ENGINEERED MUTATION SEQADV 9PIV ASP A 568 UNP Q2N0S8 LEU 567 ENGINEERED MUTATION SEQADV 9PIV HIS A 570 UNP Q2N0S8 VAL 569 ENGINEERED MUTATION SEQADV 9PIV HIS A 585 UNP Q2N0S8 ARG 584 ENGINEERED MUTATION SEQADV 9PIV CYS A 605 UNP Q2N0S8 THR 604 ENGINEERED MUTATION SEQADV 9PIV GLY A 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV THR A 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV LYS A 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS A 673 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV MET E 0 UNP Q2N0S5 INITIATING METHIONINE SEQADV 9PIV GLY E 1 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ILE E 2 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 3 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO E 4 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER E 5 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO E 6 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY E 7 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET E 8 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO E 9 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA E 10 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 11 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 12 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER E 13 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 14 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL E 15 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER E 16 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 17 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 18 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER E 19 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL E 20 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 21 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU E 22 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET E 23 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY E 24 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV CYS E 25 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL E 26 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA E 27 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU E 28 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV THR E 29 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY E 30 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU E 106 UNP Q2N0S5 THR 105 ENGINEERED MUTATION SEQADV 9PIV ILE E 271 UNP Q2N0S5 MET 270 ENGINEERED MUTATION SEQADV 9PIV LEU E 288 UNP Q2N0S5 PHE 287 ENGINEERED MUTATION SEQADV 9PIV VAL E 304 UNP Q2N0S5 ARG 303 ENGINEERED MUTATION SEQADV 9PIV TYR E 319 UNP Q2N0S5 ALA 316 ENGINEERED MUTATION SEQADV 9PIV ASN E 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9PIV GLN E 363 UNP Q2N0S5 ASN 361 ENGINEERED MUTATION SEQADV 9PIV CYS E 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9PIV ARG E 509 UNP Q2N0S5 GLU 506 ENGINEERED MUTATION SEQADV 9PIV ARG E 510 UNP Q2N0S5 LYS 507 ENGINEERED MUTATION SEQADV 9PIV ARG E 512 UNP Q2N0S5 ALA 509 ENGINEERED MUTATION SEQADV 9PIV ARG E 513 UNP Q2N0S5 VAL 510 ENGINEERED MUTATION SEQADV 9PIV SER C 519 UNP Q2N0S8 PHE 518 ENGINEERED MUTATION SEQADV 9PIV PRO C 559 UNP Q2N0S8 ILE 558 ENGINEERED MUTATION SEQADV 9PIV PRO C 561 UNP Q2N0S8 ALA 560 ENGINEERED MUTATION SEQADV 9PIV ASP C 568 UNP Q2N0S8 LEU 567 ENGINEERED MUTATION SEQADV 9PIV HIS C 570 UNP Q2N0S8 VAL 569 ENGINEERED MUTATION SEQADV 9PIV HIS C 585 UNP Q2N0S8 ARG 584 ENGINEERED MUTATION SEQADV 9PIV CYS C 605 UNP Q2N0S8 THR 604 ENGINEERED MUTATION SEQADV 9PIV GLY C 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV THR C 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV LYS C 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS C 673 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV MET F 0 UNP Q2N0S5 INITIATING METHIONINE SEQADV 9PIV GLY F 1 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ILE F 2 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 3 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO F 4 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER F 5 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO F 6 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY F 7 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET F 8 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV PRO F 9 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA F 10 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 11 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 12 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER F 13 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 14 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL F 15 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER F 16 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 17 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 18 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV SER F 19 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL F 20 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 21 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV LEU F 22 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV MET F 23 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY F 24 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV CYS F 25 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV VAL F 26 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV ALA F 27 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU F 28 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV THR F 29 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLY F 30 UNP Q2N0S5 EXPRESSION TAG SEQADV 9PIV GLU F 106 UNP Q2N0S5 THR 105 ENGINEERED MUTATION SEQADV 9PIV ILE F 271 UNP Q2N0S5 MET 270 ENGINEERED MUTATION SEQADV 9PIV LEU F 288 UNP Q2N0S5 PHE 287 ENGINEERED MUTATION SEQADV 9PIV VAL F 304 UNP Q2N0S5 ARG 303 ENGINEERED MUTATION SEQADV 9PIV TYR F 319 UNP Q2N0S5 ALA 316 ENGINEERED MUTATION SEQADV 9PIV ASN F 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9PIV GLN F 363 UNP Q2N0S5 ASN 361 ENGINEERED MUTATION SEQADV 9PIV CYS F 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9PIV ARG F 509 UNP Q2N0S5 GLU 506 ENGINEERED MUTATION SEQADV 9PIV ARG F 510 UNP Q2N0S5 LYS 507 ENGINEERED MUTATION SEQADV 9PIV ARG F 512 UNP Q2N0S5 ALA 509 ENGINEERED MUTATION SEQADV 9PIV ARG F 513 UNP Q2N0S5 VAL 510 ENGINEERED MUTATION SEQADV 9PIV SER D 519 UNP Q2N0S8 PHE 518 ENGINEERED MUTATION SEQADV 9PIV PRO D 559 UNP Q2N0S8 ILE 558 ENGINEERED MUTATION SEQADV 9PIV PRO D 561 UNP Q2N0S8 ALA 560 ENGINEERED MUTATION SEQADV 9PIV ASP D 568 UNP Q2N0S8 LEU 567 ENGINEERED MUTATION SEQADV 9PIV HIS D 570 UNP Q2N0S8 VAL 569 ENGINEERED MUTATION SEQADV 9PIV HIS D 585 UNP Q2N0S8 ARG 584 ENGINEERED MUTATION SEQADV 9PIV CYS D 605 UNP Q2N0S8 THR 604 ENGINEERED MUTATION SEQADV 9PIV GLY D 665 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV THR D 666 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV LYS D 667 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 668 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 669 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 670 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 671 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 672 UNP Q2N0S8 EXPRESSION TAG SEQADV 9PIV HIS D 673 UNP Q2N0S8 EXPRESSION TAG SEQRES 1 G 107 ALA ILE ARG MET THR GLN SER PRO ALA ILE LEU SER LEU SEQRES 2 G 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 G 107 GLN SER VAL ASP SER ARG LEU ALA TRP TYR GLN GLN LYS SEQRES 4 G 107 PRO GLY GLN SER PRO ARG LEU LEU ILE TYR ASP VAL SER SEQRES 5 G 107 SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER SEQRES 6 G 107 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 G 107 GLU PRO GLU ASP VAL ALA VAL TYR PHE CYS HIS GLN GLU SEQRES 8 G 107 ASN ASP TRP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 G 107 GLU ILE LYS SEQRES 1 J 121 GLU VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 J 121 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 J 121 ASP SER ILE SER THR ASN ASN GLY TRP SER TRP ILE ARG SEQRES 4 J 121 GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 J 121 ASN GLY ARG SER GLY SER THR ARG TYR ASN PRO SER LEU SEQRES 6 J 121 GLN SER ARG VAL THR ILE SER THR ASP THR SER GLY ASN SEQRES 7 J 121 GLN PHE SER LEU LYS VAL ASN SER VAL THR ALA ALA ASP SEQRES 8 J 121 THR ALA LYS TYR TYR CYS ALA PHE PHE TRP SER THR TYR SEQRES 9 J 121 TYR LYS ARG PHE ASP VAL TRP GLY PRO GLY VAL ARG VAL SEQRES 10 J 121 THR VAL SER SER SEQRES 1 H 126 GLN LEU ALA GLN SER GLY GLY GLY VAL LYS LYS PRO GLY SEQRES 2 H 126 ALA SER VAL LYS ILE SER CYS VAL THR PRO GLU SER THR SEQRES 3 H 126 PHE THR LYS TYR TRP LEU HIS TRP VAL ARG GLN ALA PRO SEQRES 4 H 126 GLY GLN GLY PHE GLU TRP LEU GLY VAL VAL SER PRO HIS SEQRES 5 H 126 GLY GLY ARG PRO MET PHE ALA ASN LYS PHE ARG ASP ARG SEQRES 6 H 126 LEU THR LEU THR ARG ASP ILE HIS THR THR THR HIS TYR SEQRES 7 H 126 MET GLU LEU ARG GLY LEU THR SER ASP ASP THR ALA ILE SEQRES 8 H 126 TYR TYR CYS ALA ARG ASP SER PHE GLY GLU THR PHE ARG SEQRES 9 H 126 HIS SER GLY ASP GLN PRO TYR GLN MET ASP VAL TRP GLY SEQRES 10 H 126 GLY GLY THR ASN ILE VAL VAL SER SER SEQRES 1 L 109 GLU PRO VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 109 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 109 GLN GLY PHE SER VAL ASP HIS LEU ALA TRP PHE GLN LYS SEQRES 4 L 109 ARG PRO GLY ARG PRO PRO ARG LEU LEU ILE PHE GLU THR SEQRES 5 L 109 SER ARG ARG ALA ASN GLY SER PRO ASP ARG PHE SER GLY SEQRES 6 L 109 SER ALA SER GLY ALA GLU TYR THR LEU THR ILE SER ASN SEQRES 7 L 109 VAL GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN SER SEQRES 8 L 109 TYR GLY SER ILE THR PRO LEU ILE PHE GLY GLY GLY THR SEQRES 9 L 109 ARG VAL ASP VAL LYS SEQRES 1 B 512 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 B 512 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 B 512 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 B 512 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 B 512 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 B 512 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 B 512 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 B 512 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 B 512 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 B 512 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 B 512 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 B 512 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 13 B 512 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 14 B 512 TYR ARG LEU ASP VAL VAL GLN ILE ASN GLU ASN GLN GLY SEQRES 15 B 512 ASN ARG SER ASN ASN SER ASN LYS GLU TYR ARG LEU ILE SEQRES 16 B 512 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 17 B 512 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 18 B 512 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 19 B 512 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 20 B 512 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 21 B 512 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 22 B 512 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 23 B 512 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 24 B 512 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 25 B 512 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 26 B 512 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 27 B 512 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 28 B 512 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 29 B 512 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 30 B 512 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 31 B 512 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 32 B 512 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 33 B 512 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 34 B 512 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 35 B 512 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 36 B 512 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 37 B 512 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 38 B 512 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 39 B 512 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 40 B 512 ARG ARG ARG ARG ARG SEQRES 1 A 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 A 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 A 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 A 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 A 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 A 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 A 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 A 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 A 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 A 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 A 162 HIS HIS HIS HIS HIS HIS SEQRES 1 I 107 ALA ILE ARG MET THR GLN SER PRO ALA ILE LEU SER LEU SEQRES 2 I 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 I 107 GLN SER VAL ASP SER ARG LEU ALA TRP TYR GLN GLN LYS SEQRES 4 I 107 PRO GLY GLN SER PRO ARG LEU LEU ILE TYR ASP VAL SER SEQRES 5 I 107 SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER SEQRES 6 I 107 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 I 107 GLU PRO GLU ASP VAL ALA VAL TYR PHE CYS HIS GLN GLU SEQRES 8 I 107 ASN ASP TRP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 I 107 GLU ILE LYS SEQRES 1 O 121 GLU VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 O 121 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 O 121 ASP SER ILE SER THR ASN ASN GLY TRP SER TRP ILE ARG SEQRES 4 O 121 GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 O 121 ASN GLY ARG SER GLY SER THR ARG TYR ASN PRO SER LEU SEQRES 6 O 121 GLN SER ARG VAL THR ILE SER THR ASP THR SER GLY ASN SEQRES 7 O 121 GLN PHE SER LEU LYS VAL ASN SER VAL THR ALA ALA ASP SEQRES 8 O 121 THR ALA LYS TYR TYR CYS ALA PHE PHE TRP SER THR TYR SEQRES 9 O 121 TYR LYS ARG PHE ASP VAL TRP GLY PRO GLY VAL ARG VAL SEQRES 10 O 121 THR VAL SER SER SEQRES 1 M 126 GLN LEU ALA GLN SER GLY GLY GLY VAL LYS LYS PRO GLY SEQRES 2 M 126 ALA SER VAL LYS ILE SER CYS VAL THR PRO GLU SER THR SEQRES 3 M 126 PHE THR LYS TYR TRP LEU HIS TRP VAL ARG GLN ALA PRO SEQRES 4 M 126 GLY GLN GLY PHE GLU TRP LEU GLY VAL VAL SER PRO HIS SEQRES 5 M 126 GLY GLY ARG PRO MET PHE ALA ASN LYS PHE ARG ASP ARG SEQRES 6 M 126 LEU THR LEU THR ARG ASP ILE HIS THR THR THR HIS TYR SEQRES 7 M 126 MET GLU LEU ARG GLY LEU THR SER ASP ASP THR ALA ILE SEQRES 8 M 126 TYR TYR CYS ALA ARG ASP SER PHE GLY GLU THR PHE ARG SEQRES 9 M 126 HIS SER GLY ASP GLN PRO TYR GLN MET ASP VAL TRP GLY SEQRES 10 M 126 GLY GLY THR ASN ILE VAL VAL SER SER SEQRES 1 Q 109 GLU PRO VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 Q 109 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 Q 109 GLN GLY PHE SER VAL ASP HIS LEU ALA TRP PHE GLN LYS SEQRES 4 Q 109 ARG PRO GLY ARG PRO PRO ARG LEU LEU ILE PHE GLU THR SEQRES 5 Q 109 SER ARG ARG ALA ASN GLY SER PRO ASP ARG PHE SER GLY SEQRES 6 Q 109 SER ALA SER GLY ALA GLU TYR THR LEU THR ILE SER ASN SEQRES 7 Q 109 VAL GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN SER SEQRES 8 Q 109 TYR GLY SER ILE THR PRO LEU ILE PHE GLY GLY GLY THR SEQRES 9 Q 109 ARG VAL ASP VAL LYS SEQRES 1 E 512 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 E 512 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 E 512 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 E 512 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 E 512 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 E 512 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 E 512 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 E 512 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 E 512 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 E 512 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 E 512 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 E 512 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 13 E 512 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 14 E 512 TYR ARG LEU ASP VAL VAL GLN ILE ASN GLU ASN GLN GLY SEQRES 15 E 512 ASN ARG SER ASN ASN SER ASN LYS GLU TYR ARG LEU ILE SEQRES 16 E 512 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 17 E 512 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 18 E 512 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 19 E 512 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 20 E 512 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 21 E 512 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 22 E 512 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 23 E 512 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 24 E 512 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 25 E 512 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 26 E 512 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 27 E 512 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 28 E 512 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 29 E 512 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 30 E 512 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 31 E 512 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 32 E 512 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 33 E 512 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 34 E 512 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 35 E 512 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 36 E 512 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 37 E 512 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 38 E 512 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 39 E 512 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 40 E 512 ARG ARG ARG ARG ARG SEQRES 1 C 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 C 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 C 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 C 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 C 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 C 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 C 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 C 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 C 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 C 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 C 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 C 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 C 162 HIS HIS HIS HIS HIS HIS SEQRES 1 K 107 ALA ILE ARG MET THR GLN SER PRO ALA ILE LEU SER LEU SEQRES 2 K 107 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 K 107 GLN SER VAL ASP SER ARG LEU ALA TRP TYR GLN GLN LYS SEQRES 4 K 107 PRO GLY GLN SER PRO ARG LEU LEU ILE TYR ASP VAL SER SEQRES 5 K 107 SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SER SEQRES 6 K 107 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 K 107 GLU PRO GLU ASP VAL ALA VAL TYR PHE CYS HIS GLN GLU SEQRES 8 K 107 ASN ASP TRP PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 K 107 GLU ILE LYS SEQRES 1 P 121 GLU VAL GLN LEU VAL GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 P 121 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 P 121 ASP SER ILE SER THR ASN ASN GLY TRP SER TRP ILE ARG SEQRES 4 P 121 GLN THR PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SEQRES 5 P 121 ASN GLY ARG SER GLY SER THR ARG TYR ASN PRO SER LEU SEQRES 6 P 121 GLN SER ARG VAL THR ILE SER THR ASP THR SER GLY ASN SEQRES 7 P 121 GLN PHE SER LEU LYS VAL ASN SER VAL THR ALA ALA ASP SEQRES 8 P 121 THR ALA LYS TYR TYR CYS ALA PHE PHE TRP SER THR TYR SEQRES 9 P 121 TYR LYS ARG PHE ASP VAL TRP GLY PRO GLY VAL ARG VAL SEQRES 10 P 121 THR VAL SER SER SEQRES 1 N 126 GLN LEU ALA GLN SER GLY GLY GLY VAL LYS LYS PRO GLY SEQRES 2 N 126 ALA SER VAL LYS ILE SER CYS VAL THR PRO GLU SER THR SEQRES 3 N 126 PHE THR LYS TYR TRP LEU HIS TRP VAL ARG GLN ALA PRO SEQRES 4 N 126 GLY GLN GLY PHE GLU TRP LEU GLY VAL VAL SER PRO HIS SEQRES 5 N 126 GLY GLY ARG PRO MET PHE ALA ASN LYS PHE ARG ASP ARG SEQRES 6 N 126 LEU THR LEU THR ARG ASP ILE HIS THR THR THR HIS TYR SEQRES 7 N 126 MET GLU LEU ARG GLY LEU THR SER ASP ASP THR ALA ILE SEQRES 8 N 126 TYR TYR CYS ALA ARG ASP SER PHE GLY GLU THR PHE ARG SEQRES 9 N 126 HIS SER GLY ASP GLN PRO TYR GLN MET ASP VAL TRP GLY SEQRES 10 N 126 GLY GLY THR ASN ILE VAL VAL SER SER SEQRES 1 R 109 GLU PRO VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 R 109 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 R 109 GLN GLY PHE SER VAL ASP HIS LEU ALA TRP PHE GLN LYS SEQRES 4 R 109 ARG PRO GLY ARG PRO PRO ARG LEU LEU ILE PHE GLU THR SEQRES 5 R 109 SER ARG ARG ALA ASN GLY SER PRO ASP ARG PHE SER GLY SEQRES 6 R 109 SER ALA SER GLY ALA GLU TYR THR LEU THR ILE SER ASN SEQRES 7 R 109 VAL GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN SER SEQRES 8 R 109 TYR GLY SER ILE THR PRO LEU ILE PHE GLY GLY GLY THR SEQRES 9 R 109 ARG VAL ASP VAL LYS SEQRES 1 F 512 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 F 512 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 F 512 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 F 512 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 F 512 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 F 512 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 F 512 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 F 512 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 F 512 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 F 512 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 F 512 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 F 512 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 13 F 512 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 14 F 512 TYR ARG LEU ASP VAL VAL GLN ILE ASN GLU ASN GLN GLY SEQRES 15 F 512 ASN ARG SER ASN ASN SER ASN LYS GLU TYR ARG LEU ILE SEQRES 16 F 512 ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS SEQRES 17 F 512 VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO SEQRES 18 F 512 ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE SEQRES 19 F 512 ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL GLN SEQRES 20 F 512 CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU SEQRES 21 F 512 LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL ILE ILE SEQRES 22 F 512 ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE LEU SEQRES 23 F 512 VAL GLN LEU ASN THR PRO VAL GLN ILE ASN CYS THR ARG SEQRES 24 F 512 PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO SEQRES 25 F 512 GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP SEQRES 26 F 512 ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR TRP SEQRES 27 F 512 ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS SEQRES 28 F 512 HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA GLN SER SEQRES 29 F 512 SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE ASN SEQRES 30 F 512 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 31 F 512 PHE ASN SER THR TRP ILE SER ASN THR SER VAL GLN GLY SEQRES 32 F 512 SER ASN SER THR GLY SER ASN ASP SER ILE THR LEU PRO SEQRES 33 F 512 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ILE SEQRES 34 F 512 GLY GLN ALA MET TYR ALA PRO PRO ILE GLN GLY VAL ILE SEQRES 35 F 512 ARG CYS VAL SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 36 F 512 ASP GLY GLY SER THR ASN SER THR THR GLU THR PHE ARG SEQRES 37 F 512 PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER GLU SEQRES 38 F 512 LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY SEQRES 39 F 512 VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 40 F 512 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 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 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 NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET MAN c 4 11 HET MAN c 5 11 HET MAN c 6 11 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET MAN d 4 11 HET MAN d 5 11 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 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 NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET MAN j 6 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET MAN k 4 11 HET MAN k 5 11 HET NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET NAG m 1 14 HET NAG m 2 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG B 603 14 HET NAG B 604 14 HET NAG B 605 14 HET NAG B 606 14 HET NAG B 607 14 HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 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 C 701 14 HET NAG C 702 14 HET NAG C 703 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 D 701 14 HET NAG D 702 14 HET NAG D 703 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 19 NAG 72(C8 H15 N O6) FORMUL 22 BMA 9(C6 H12 O6) FORMUL 22 MAN 15(C6 H12 O6) HELIX 1 AA1 GLU G 79 VAL G 83 5 5 HELIX 2 AA2 SER J 28 ASN J 32 5 5 HELIX 3 AA3 ASN J 60 GLN J 64 5 5 HELIX 4 AA4 THR J 83 THR J 87 5 5 HELIX 5 AA5 PRO H 25 THR H 30 1 6 HELIX 6 AA6 ASN H 61 ARG H 64 5 4 HELIX 7 AA7 ILE H 73 THR H 75 5 3 HELIX 8 AA8 THR H 83 THR H 87 5 5 HELIX 9 AA9 GLU L 79 PHE L 83 5 5 HELIX 10 AB1 ALA B 70 CYS B 74 5 5 HELIX 11 AB2 ASN B 98 LYS B 117 1 20 HELIX 12 AB3 LEU B 122 CYS B 126 5 5 HELIX 13 AB4 LYS B 335 GLY B 354 1 20 HELIX 14 AB5 ASP B 368 THR B 373 1 6 HELIX 15 AB6 MET B 475 ARG B 480 1 6 HELIX 16 AB7 SER B 481 TYR B 484 5 4 HELIX 17 AB8 THR A 529 SER A 534 1 6 HELIX 18 AB9 THR A 536 ARG A 542 1 7 HELIX 19 AC1 HIS A 570 TRP A 596 1 27 HELIX 20 AC2 ASN A 618 ASN A 625 1 8 HELIX 21 AC3 THR A 627 ILE A 635 1 9 HELIX 22 AC4 TYR A 638 GLN A 658 1 21 HELIX 23 AC5 GLU I 79 VAL I 83 5 5 HELIX 24 AC6 SER O 28 ASN O 32 5 5 HELIX 25 AC7 ASN O 60 GLN O 64 5 5 HELIX 26 AC8 THR O 83 THR O 87 5 5 HELIX 27 AC9 PRO M 25 THR M 30 1 6 HELIX 28 AD1 ASN M 61 ARG M 64 5 4 HELIX 29 AD2 ILE M 73 THR M 75 5 3 HELIX 30 AD3 THR M 83 THR M 87 5 5 HELIX 31 AD4 GLU Q 79 PHE Q 83 5 5 HELIX 32 AD5 ALA E 70 CYS E 74 5 5 HELIX 33 AD6 ASN E 98 LYS E 117 1 20 HELIX 34 AD7 LEU E 122 CYS E 126 5 5 HELIX 35 AD8 LYS E 335 GLY E 354 1 20 HELIX 36 AD9 ASP E 368 THR E 373 1 6 HELIX 37 AE1 MET E 475 ARG E 480 1 6 HELIX 38 AE2 SER E 481 TYR E 484 5 4 HELIX 39 AE3 THR C 529 SER C 534 1 6 HELIX 40 AE4 THR C 536 ARG C 542 1 7 HELIX 41 AE5 HIS C 570 TRP C 596 1 27 HELIX 42 AE6 ASN C 618 ASN C 625 1 8 HELIX 43 AE7 THR C 627 ILE C 635 1 9 HELIX 44 AE8 TYR C 638 GLN C 658 1 21 HELIX 45 AE9 GLU K 79 VAL K 83 5 5 HELIX 46 AF1 SER P 28 ASN P 32 5 5 HELIX 47 AF2 ASN P 60 GLN P 64 5 5 HELIX 48 AF3 THR P 83 THR P 87 5 5 HELIX 49 AF4 PRO N 25 THR N 30 1 6 HELIX 50 AF5 ASN N 61 ARG N 64 5 4 HELIX 51 AF6 ILE N 73 THR N 75 5 3 HELIX 52 AF7 THR N 83 THR N 87 5 5 HELIX 53 AF8 GLU R 79 PHE R 83 5 5 HELIX 54 AF9 ALA F 70 CYS F 74 5 5 HELIX 55 AG1 ASN F 98 LYS F 117 1 20 HELIX 56 AG2 LEU F 122 CYS F 126 5 5 HELIX 57 AG3 LYS F 335 GLY F 354 1 20 HELIX 58 AG4 ASP F 368 THR F 373 1 6 HELIX 59 AG5 MET F 475 ARG F 480 1 6 HELIX 60 AG6 SER F 481 TYR F 484 5 4 HELIX 61 AG7 THR D 529 SER D 534 1 6 HELIX 62 AG8 THR D 536 ARG D 542 1 7 HELIX 63 AG9 HIS D 570 TRP D 596 1 27 HELIX 64 AH1 ASN D 618 ASN D 625 1 8 HELIX 65 AH2 THR D 627 ILE D 635 1 9 HELIX 66 AH3 TYR D 638 GLN D 658 1 21 SHEET 1 AA1 4 MET G 4 SER G 7 0 SHEET 2 AA1 4 ALA G 19 ALA G 25 -1 O SER G 22 N SER G 7 SHEET 3 AA1 4 GLU G 70 ILE G 75 -1 O ILE G 75 N ALA G 19 SHEET 4 AA1 4 PHE G 62 SER G 67 -1 N SER G 63 O THR G 74 SHEET 1 AA2 6 ILE G 10 SER G 12 0 SHEET 2 AA2 6 THR G 102 GLU G 105 1 O LYS G 103 N LEU G 11 SHEET 3 AA2 6 ALA G 84 GLN G 90 -1 N ALA G 84 O VAL G 104 SHEET 4 AA2 6 LEU G 33 GLN G 38 -1 N ALA G 34 O HIS G 89 SHEET 5 AA2 6 ARG G 45 TYR G 49 -1 O ARG G 45 N GLN G 37 SHEET 6 AA2 6 SER G 53 ARG G 54 -1 O SER G 53 N TYR G 49 SHEET 1 AA3 4 ILE G 10 SER G 12 0 SHEET 2 AA3 4 THR G 102 GLU G 105 1 O LYS G 103 N LEU G 11 SHEET 3 AA3 4 ALA G 84 GLN G 90 -1 N ALA G 84 O VAL G 104 SHEET 4 AA3 4 THR G 97 PHE G 98 -1 O THR G 97 N GLN G 90 SHEET 1 AA4 4 GLN J 3 SER J 7 0 SHEET 2 AA4 4 SER J 19 SER J 25 -1 O ALA J 23 N VAL J 5 SHEET 3 AA4 4 GLN J 77 VAL J 82 -1 O PHE J 78 N CYS J 22 SHEET 4 AA4 4 VAL J 67 ASP J 72 -1 N THR J 68 O LYS J 81 SHEET 1 AA5 5 THR J 57 ARG J 58 0 SHEET 2 AA5 5 GLY J 44 ILE J 51 -1 N TYR J 50 O ARG J 58 SHEET 3 AA5 5 TRP J 35 THR J 40 -1 N TRP J 35 O ILE J 51 SHEET 4 AA5 5 ALA J 88 SER J 97 -1 O TYR J 91 N ILE J 37 SHEET 5 AA5 5 ARG J 100B TRP J 103 -1 O PHE J 100C N TRP J 96 SHEET 1 AA6 5 THR J 57 ARG J 58 0 SHEET 2 AA6 5 GLY J 44 ILE J 51 -1 N TYR J 50 O ARG J 58 SHEET 3 AA6 5 TRP J 35 THR J 40 -1 N TRP J 35 O ILE J 51 SHEET 4 AA6 5 ALA J 88 SER J 97 -1 O TYR J 91 N ILE J 37 SHEET 5 AA6 5 VAL J 107 VAL J 109 -1 O VAL J 107 N TYR J 90 SHEET 1 AA7 4 ALA H 5 SER H 7 0 SHEET 2 AA7 4 VAL H 18 VAL H 23 -1 O SER H 21 N SER H 7 SHEET 3 AA7 4 THR H 77 LEU H 82 -1 O HIS H 78 N CYS H 22 SHEET 4 AA7 4 LEU H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA8 6 GLY H 10 LYS H 12 0 SHEET 2 AA8 6 THR H 107 VAL H 111 1 O VAL H 110 N LYS H 12 SHEET 3 AA8 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 6 TRP H 33 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA8 6 PHE H 45 VAL H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA8 6 PRO H 57 PHE H 59 -1 O MET H 58 N VAL H 50 SHEET 1 AA9 4 GLY H 10 LYS H 12 0 SHEET 2 AA9 4 THR H 107 VAL H 111 1 O VAL H 110 N LYS H 12 SHEET 3 AA9 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AB1 4 LEU L 4 SER L 7 0 SHEET 2 AB1 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB1 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AB1 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AB2 6 THR L 10 SER L 12 0 SHEET 2 AB2 6 THR L 102 ASP L 105 1 O ARG L 103 N LEU L 11 SHEET 3 AB2 6 VAL L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AB2 6 ALA L 34 LYS L 38 -1 N LYS L 38 O VAL L 85 SHEET 5 AB2 6 ARG L 45 PHE L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB2 6 ARG L 53 ARG L 54 -1 O ARG L 53 N PHE L 49 SHEET 1 AB3 4 THR L 10 SER L 12 0 SHEET 2 AB3 4 THR L 102 ASP L 105 1 O ARG L 103 N LEU L 11 SHEET 3 AB3 4 VAL L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AB3 4 LEU L 96 PHE L 98 -1 O ILE L 97 N SER L 90 SHEET 1 AB4 3 LEU B 494 THR B 499 0 SHEET 2 AB4 3 TRP B 35 TYR B 40 -1 N TRP B 35 O THR B 499 SHEET 3 AB4 3 ILE A 603 PRO A 609 -1 O VAL A 608 N VAL B 36 SHEET 1 AB5 5 TRP B 45 ASP B 47 0 SHEET 2 AB5 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AB5 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AB5 5 VAL B 242 VAL B 245 -1 O VAL B 245 N ILE B 225 SHEET 5 AB5 5 ILE B 84 LEU B 86 -1 N ILE B 84 O THR B 244 SHEET 1 AB6 3 VAL B 75 PRO B 76 0 SHEET 2 AB6 3 PHE B 53 SER B 56 1 N CYS B 54 O VAL B 75 SHEET 3 AB6 3 HIS B 216 CYS B 218 -1 O CYS B 218 N PHE B 53 SHEET 1 AB7 2 GLU B 91 ASN B 94 0 SHEET 2 AB7 2 THR B 236 CYS B 239 -1 O GLY B 237 N PHE B 93 SHEET 1 AB8 5 LYS B 169 TYR B 177 0 SHEET 2 AB8 5 LEU B 154 THR B 162 -1 N CYS B 157 O SER B 174 SHEET 3 AB8 5 LEU B 129 ASN B 133 -1 N GLN B 130 O SER B 158 SHEET 4 AB8 5 GLU B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AB8 5 VAL B 181 GLN B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AB9 3 ALA B 200 GLN B 203 0 SHEET 2 AB9 3 GLN B 432 TYR B 435 1 O TYR B 435 N THR B 202 SHEET 3 AB9 3 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AC1 7 LEU B 259 LEU B 261 0 SHEET 2 AC1 7 ILE B 443 ARG B 456 -1 O GLY B 451 N LEU B 260 SHEET 3 AC1 7 ILE B 284 ARG B 298 -1 N CYS B 296 O CYS B 445 SHEET 4 AC1 7 ALA B 329 SER B 334 -1 O HIS B 330 N THR B 297 SHEET 5 AC1 7 SER B 413 LYS B 421 -1 O ILE B 414 N VAL B 333 SHEET 6 AC1 7 GLU B 381 CYS B 385 -1 N TYR B 384 O ARG B 419 SHEET 7 AC1 7 HIS B 374 CYS B 378 -1 N HIS B 374 O CYS B 385 SHEET 1 AC2 6 ILE B 271 SER B 274 0 SHEET 2 AC2 6 ILE B 284 ARG B 298 -1 O LEU B 285 N ARG B 273 SHEET 3 AC2 6 ILE B 443 ARG B 456 -1 O CYS B 445 N CYS B 296 SHEET 4 AC2 6 THR B 465 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 5 AC2 6 ILE B 358 PHE B 361 1 N ARG B 360 O PHE B 468 SHEET 6 AC2 6 THR B 394 TRP B 395 -1 O TRP B 395 N ILE B 359 SHEET 1 AC3 2 VAL B 304 GLY B 312 0 SHEET 2 AC3 2 GLN B 315 THR B 320 -1 O TYR B 319 N LYS B 305 SHEET 1 AC4 4 MET I 4 SER I 7 0 SHEET 2 AC4 4 ALA I 19 ALA I 25 -1 O SER I 22 N SER I 7 SHEET 3 AC4 4 GLU I 70 ILE I 75 -1 O ILE I 75 N ALA I 19 SHEET 4 AC4 4 PHE I 62 SER I 67 -1 N SER I 63 O THR I 74 SHEET 1 AC5 6 ILE I 10 SER I 12 0 SHEET 2 AC5 6 THR I 102 GLU I 105 1 O LYS I 103 N LEU I 11 SHEET 3 AC5 6 ALA I 84 GLN I 90 -1 N ALA I 84 O VAL I 104 SHEET 4 AC5 6 LEU I 33 GLN I 38 -1 N ALA I 34 O HIS I 89 SHEET 5 AC5 6 ARG I 45 TYR I 49 -1 O ARG I 45 N GLN I 37 SHEET 6 AC5 6 SER I 53 ARG I 54 -1 O SER I 53 N TYR I 49 SHEET 1 AC6 4 ILE I 10 SER I 12 0 SHEET 2 AC6 4 THR I 102 GLU I 105 1 O LYS I 103 N LEU I 11 SHEET 3 AC6 4 ALA I 84 GLN I 90 -1 N ALA I 84 O VAL I 104 SHEET 4 AC6 4 THR I 97 PHE I 98 -1 O THR I 97 N GLN I 90 SHEET 1 AC7 4 GLN O 3 SER O 7 0 SHEET 2 AC7 4 SER O 19 SER O 25 -1 O ALA O 23 N VAL O 5 SHEET 3 AC7 4 GLN O 77 VAL O 82 -1 O PHE O 78 N CYS O 22 SHEET 4 AC7 4 VAL O 67 ASP O 72 -1 N THR O 68 O LYS O 81 SHEET 1 AC8 5 THR O 57 ARG O 58 0 SHEET 2 AC8 5 GLY O 44 ILE O 51 -1 N TYR O 50 O ARG O 58 SHEET 3 AC8 5 TRP O 35 THR O 40 -1 N TRP O 35 O ILE O 51 SHEET 4 AC8 5 ALA O 88 SER O 97 -1 O TYR O 91 N ILE O 37 SHEET 5 AC8 5 ARG O 100B TRP O 103 -1 O PHE O 100C N TRP O 96 SHEET 1 AC9 5 THR O 57 ARG O 58 0 SHEET 2 AC9 5 GLY O 44 ILE O 51 -1 N TYR O 50 O ARG O 58 SHEET 3 AC9 5 TRP O 35 THR O 40 -1 N TRP O 35 O ILE O 51 SHEET 4 AC9 5 ALA O 88 SER O 97 -1 O TYR O 91 N ILE O 37 SHEET 5 AC9 5 VAL O 107 VAL O 109 -1 O VAL O 107 N TYR O 90 SHEET 1 AD1 4 ALA M 5 SER M 7 0 SHEET 2 AD1 4 VAL M 18 VAL M 23 -1 O SER M 21 N SER M 7 SHEET 3 AD1 4 THR M 77 LEU M 82 -1 O HIS M 78 N CYS M 22 SHEET 4 AD1 4 LEU M 67 ASP M 72 -1 N ASP M 72 O THR M 77 SHEET 1 AD2 6 GLY M 10 LYS M 12 0 SHEET 2 AD2 6 THR M 107 VAL M 111 1 O VAL M 110 N LYS M 12 SHEET 3 AD2 6 ALA M 88 ASP M 95 -1 N TYR M 90 O THR M 107 SHEET 4 AD2 6 TRP M 33 GLN M 39 -1 N HIS M 35 O ALA M 93 SHEET 5 AD2 6 PHE M 45 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AD2 6 PRO M 57 PHE M 59 -1 O MET M 58 N VAL M 50 SHEET 1 AD3 4 GLY M 10 LYS M 12 0 SHEET 2 AD3 4 THR M 107 VAL M 111 1 O VAL M 110 N LYS M 12 SHEET 3 AD3 4 ALA M 88 ASP M 95 -1 N TYR M 90 O THR M 107 SHEET 4 AD3 4 VAL M 102 TRP M 103 -1 O VAL M 102 N ARG M 94 SHEET 1 AD4 4 LEU Q 4 SER Q 7 0 SHEET 2 AD4 4 ALA Q 19 ALA Q 25 -1 O ARG Q 24 N THR Q 5 SHEET 3 AD4 4 GLU Q 70 ILE Q 75 -1 O LEU Q 73 N LEU Q 21 SHEET 4 AD4 4 PHE Q 62 SER Q 67 -1 N SER Q 65 O THR Q 72 SHEET 1 AD5 6 THR Q 10 SER Q 12 0 SHEET 2 AD5 6 THR Q 102 ASP Q 105 1 O ARG Q 103 N LEU Q 11 SHEET 3 AD5 6 VAL Q 85 TYR Q 91 -1 N TYR Q 86 O THR Q 102 SHEET 4 AD5 6 ALA Q 34 LYS Q 38 -1 N LYS Q 38 O VAL Q 85 SHEET 5 AD5 6 ARG Q 45 PHE Q 49 -1 O LEU Q 47 N TRP Q 35 SHEET 6 AD5 6 ARG Q 53 ARG Q 54 -1 O ARG Q 53 N PHE Q 49 SHEET 1 AD6 4 THR Q 10 SER Q 12 0 SHEET 2 AD6 4 THR Q 102 ASP Q 105 1 O ARG Q 103 N LEU Q 11 SHEET 3 AD6 4 VAL Q 85 TYR Q 91 -1 N TYR Q 86 O THR Q 102 SHEET 4 AD6 4 LEU Q 96 PHE Q 98 -1 O ILE Q 97 N SER Q 90 SHEET 1 AD7 3 LEU E 494 THR E 499 0 SHEET 2 AD7 3 TRP E 35 TYR E 40 -1 N TRP E 35 O THR E 499 SHEET 3 AD7 3 ILE C 603 PRO C 609 -1 O VAL C 608 N VAL E 36 SHEET 1 AD8 5 TRP E 45 ASP E 47 0 SHEET 2 AD8 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AD8 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AD8 5 VAL E 242 VAL E 245 -1 O VAL E 245 N ILE E 225 SHEET 5 AD8 5 ILE E 84 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AD9 3 VAL E 75 PRO E 76 0 SHEET 2 AD9 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AD9 3 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AE1 2 GLU E 91 ASN E 94 0 SHEET 2 AE1 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AE2 5 LYS E 169 TYR E 177 0 SHEET 2 AE2 5 LEU E 154 THR E 162 -1 N CYS E 157 O SER E 174 SHEET 3 AE2 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AE2 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AE2 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AE3 3 ALA E 200 GLN E 203 0 SHEET 2 AE3 3 GLN E 432 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AE3 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AE4 7 LEU E 259 LEU E 261 0 SHEET 2 AE4 7 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AE4 7 ILE E 284 ARG E 298 -1 N CYS E 296 O CYS E 445 SHEET 4 AE4 7 ALA E 329 SER E 334 -1 O HIS E 330 N THR E 297 SHEET 5 AE4 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AE4 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AE4 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AE5 6 ILE E 271 SER E 274 0 SHEET 2 AE5 6 ILE E 284 ARG E 298 -1 O LEU E 285 N ARG E 273 SHEET 3 AE5 6 ILE E 443 ARG E 456 -1 O CYS E 445 N CYS E 296 SHEET 4 AE5 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AE5 6 ILE E 358 PHE E 361 1 N ARG E 360 O PHE E 468 SHEET 6 AE5 6 THR E 394 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AE6 2 VAL E 304 GLY E 312 0 SHEET 2 AE6 2 GLN E 315 THR E 320 -1 O TYR E 319 N LYS E 305 SHEET 1 AE7 4 MET K 4 SER K 7 0 SHEET 2 AE7 4 ALA K 19 ALA K 25 -1 O SER K 22 N SER K 7 SHEET 3 AE7 4 GLU K 70 ILE K 75 -1 O ILE K 75 N ALA K 19 SHEET 4 AE7 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 AE8 6 ILE K 10 SER K 12 0 SHEET 2 AE8 6 THR K 102 GLU K 105 1 O LYS K 103 N LEU K 11 SHEET 3 AE8 6 ALA K 84 GLN K 90 -1 N ALA K 84 O VAL K 104 SHEET 4 AE8 6 LEU K 33 GLN K 38 -1 N ALA K 34 O HIS K 89 SHEET 5 AE8 6 ARG K 45 TYR K 49 -1 O ARG K 45 N GLN K 37 SHEET 6 AE8 6 SER K 53 ARG K 54 -1 O SER K 53 N TYR K 49 SHEET 1 AE9 4 ILE K 10 SER K 12 0 SHEET 2 AE9 4 THR K 102 GLU K 105 1 O LYS K 103 N LEU K 11 SHEET 3 AE9 4 ALA K 84 GLN K 90 -1 N ALA K 84 O VAL K 104 SHEET 4 AE9 4 THR K 97 PHE K 98 -1 O THR K 97 N GLN K 90 SHEET 1 AF1 4 GLN P 3 SER P 7 0 SHEET 2 AF1 4 SER P 19 SER P 25 -1 O ALA P 23 N VAL P 5 SHEET 3 AF1 4 GLN P 77 VAL P 82 -1 O PHE P 78 N CYS P 22 SHEET 4 AF1 4 VAL P 67 ASP P 72 -1 N THR P 68 O LYS P 81 SHEET 1 AF2 5 THR P 57 ARG P 58 0 SHEET 2 AF2 5 GLY P 44 ILE P 51 -1 N TYR P 50 O ARG P 58 SHEET 3 AF2 5 TRP P 35 THR P 40 -1 N TRP P 35 O ILE P 51 SHEET 4 AF2 5 ALA P 88 SER P 97 -1 O TYR P 91 N ILE P 37 SHEET 5 AF2 5 ARG P 100B TRP P 103 -1 O PHE P 100C N TRP P 96 SHEET 1 AF3 5 THR P 57 ARG P 58 0 SHEET 2 AF3 5 GLY P 44 ILE P 51 -1 N TYR P 50 O ARG P 58 SHEET 3 AF3 5 TRP P 35 THR P 40 -1 N TRP P 35 O ILE P 51 SHEET 4 AF3 5 ALA P 88 SER P 97 -1 O TYR P 91 N ILE P 37 SHEET 5 AF3 5 VAL P 107 VAL P 109 -1 O VAL P 107 N TYR P 90 SHEET 1 AF4 4 ALA N 5 SER N 7 0 SHEET 2 AF4 4 VAL N 18 VAL N 23 -1 O SER N 21 N SER N 7 SHEET 3 AF4 4 THR N 77 LEU N 82 -1 O HIS N 78 N CYS N 22 SHEET 4 AF4 4 LEU N 67 ASP N 72 -1 N ASP N 72 O THR N 77 SHEET 1 AF5 6 GLY N 10 LYS N 12 0 SHEET 2 AF5 6 THR N 107 VAL N 111 1 O VAL N 110 N LYS N 12 SHEET 3 AF5 6 ALA N 88 ASP N 95 -1 N TYR N 90 O THR N 107 SHEET 4 AF5 6 TRP N 33 GLN N 39 -1 N HIS N 35 O ALA N 93 SHEET 5 AF5 6 PHE N 45 VAL N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AF5 6 PRO N 57 PHE N 59 -1 O MET N 58 N VAL N 50 SHEET 1 AF6 4 GLY N 10 LYS N 12 0 SHEET 2 AF6 4 THR N 107 VAL N 111 1 O VAL N 110 N LYS N 12 SHEET 3 AF6 4 ALA N 88 ASP N 95 -1 N TYR N 90 O THR N 107 SHEET 4 AF6 4 VAL N 102 TRP N 103 -1 O VAL N 102 N ARG N 94 SHEET 1 AF7 4 LEU R 4 SER R 7 0 SHEET 2 AF7 4 ALA R 19 ALA R 25 -1 O ARG R 24 N THR R 5 SHEET 3 AF7 4 GLU R 70 ILE R 75 -1 O LEU R 73 N LEU R 21 SHEET 4 AF7 4 PHE R 62 SER R 67 -1 N SER R 65 O THR R 72 SHEET 1 AF8 6 THR R 10 SER R 12 0 SHEET 2 AF8 6 THR R 102 ASP R 105 1 O ARG R 103 N LEU R 11 SHEET 3 AF8 6 VAL R 85 TYR R 91 -1 N TYR R 86 O THR R 102 SHEET 4 AF8 6 ALA R 34 LYS R 38 -1 N LYS R 38 O VAL R 85 SHEET 5 AF8 6 ARG R 45 PHE R 49 -1 O LEU R 47 N TRP R 35 SHEET 6 AF8 6 ARG R 53 ARG R 54 -1 O ARG R 53 N PHE R 49 SHEET 1 AF9 4 THR R 10 SER R 12 0 SHEET 2 AF9 4 THR R 102 ASP R 105 1 O ARG R 103 N LEU R 11 SHEET 3 AF9 4 VAL R 85 TYR R 91 -1 N TYR R 86 O THR R 102 SHEET 4 AF9 4 LEU R 96 PHE R 98 -1 O ILE R 97 N SER R 90 SHEET 1 AG1 3 LEU F 494 THR F 499 0 SHEET 2 AG1 3 TRP F 35 TYR F 40 -1 N TRP F 35 O THR F 499 SHEET 3 AG1 3 ILE D 603 PRO D 609 -1 O VAL D 608 N VAL F 36 SHEET 1 AG2 5 TRP F 45 ASP F 47 0 SHEET 2 AG2 5 TYR F 486 ILE F 491 -1 O LYS F 490 N LYS F 46 SHEET 3 AG2 5 PHE F 223 CYS F 228 -1 N ALA F 224 O VAL F 489 SHEET 4 AG2 5 VAL F 242 VAL F 245 -1 O VAL F 245 N ILE F 225 SHEET 5 AG2 5 ILE F 84 LEU F 86 -1 N ILE F 84 O THR F 244 SHEET 1 AG3 3 VAL F 75 PRO F 76 0 SHEET 2 AG3 3 PHE F 53 SER F 56 1 N CYS F 54 O VAL F 75 SHEET 3 AG3 3 HIS F 216 CYS F 218 -1 O CYS F 218 N PHE F 53 SHEET 1 AG4 2 GLU F 91 ASN F 94 0 SHEET 2 AG4 2 THR F 236 CYS F 239 -1 O GLY F 237 N PHE F 93 SHEET 1 AG5 5 LYS F 169 TYR F 177 0 SHEET 2 AG5 5 LEU F 154 THR F 162 -1 N CYS F 157 O SER F 174 SHEET 3 AG5 5 LEU F 129 ASN F 133 -1 N GLN F 130 O SER F 158 SHEET 4 AG5 5 GLU F 190 LEU F 193 -1 O TYR F 191 N LEU F 129 SHEET 5 AG5 5 VAL F 181 GLN F 183 -1 N VAL F 182 O ARG F 192 SHEET 1 AG6 3 ALA F 200 GLN F 203 0 SHEET 2 AG6 3 GLN F 432 TYR F 435 1 O TYR F 435 N THR F 202 SHEET 3 AG6 3 ILE F 423 ILE F 424 -1 N ILE F 424 O MET F 434 SHEET 1 AG7 7 LEU F 259 LEU F 261 0 SHEET 2 AG7 7 ILE F 443 ARG F 456 -1 O GLY F 451 N LEU F 260 SHEET 3 AG7 7 ILE F 284 ARG F 298 -1 N CYS F 296 O CYS F 445 SHEET 4 AG7 7 ALA F 329 SER F 334 -1 O HIS F 330 N THR F 297 SHEET 5 AG7 7 SER F 413 LYS F 421 -1 O ILE F 414 N VAL F 333 SHEET 6 AG7 7 GLU F 381 CYS F 385 -1 N TYR F 384 O ARG F 419 SHEET 7 AG7 7 HIS F 374 CYS F 378 -1 N HIS F 374 O CYS F 385 SHEET 1 AG8 6 ILE F 271 SER F 274 0 SHEET 2 AG8 6 ILE F 284 ARG F 298 -1 O LEU F 285 N ARG F 273 SHEET 3 AG8 6 ILE F 443 ARG F 456 -1 O CYS F 445 N CYS F 296 SHEET 4 AG8 6 THR F 465 PRO F 470 -1 O ARG F 469 N THR F 455 SHEET 5 AG8 6 ILE F 358 PHE F 361 1 N ARG F 360 O PHE F 468 SHEET 6 AG8 6 THR F 394 TRP F 395 -1 O TRP F 395 N ILE F 359 SHEET 1 AG9 2 VAL F 304 GLY F 312 0 SHEET 2 AG9 2 GLN F 315 THR F 320 -1 O TYR F 319 N LYS F 305 SSBOND 1 CYS G 23 CYS G 88 1555 1555 2.04 SSBOND 2 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 5 CYS B 54 CYS B 74 1555 1555 2.03 SSBOND 6 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 7 CYS B 126 CYS B 196 1555 1555 2.03 SSBOND 8 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 9 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 10 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 11 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 12 CYS B 378 CYS B 445 1555 1555 2.04 SSBOND 13 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 14 CYS B 501 CYS A 605 1555 1555 2.03 SSBOND 15 CYS A 598 CYS A 604 1555 1555 2.03 SSBOND 16 CYS I 23 CYS I 88 1555 1555 2.04 SSBOND 17 CYS O 22 CYS O 92 1555 1555 2.03 SSBOND 18 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 19 CYS Q 23 CYS Q 88 1555 1555 2.04 SSBOND 20 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 21 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 22 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 23 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 24 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 25 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 26 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 27 CYS E 378 CYS E 445 1555 1555 2.04 SSBOND 28 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 29 CYS E 501 CYS C 605 1555 1555 2.03 SSBOND 30 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 31 CYS K 23 CYS K 88 1555 1555 2.05 SSBOND 32 CYS P 22 CYS P 92 1555 1555 2.03 SSBOND 33 CYS N 22 CYS N 92 1555 1555 2.03 SSBOND 34 CYS R 23 CYS R 88 1555 1555 2.04 SSBOND 35 CYS F 54 CYS F 74 1555 1555 2.03 SSBOND 36 CYS F 119 CYS F 205 1555 1555 2.03 SSBOND 37 CYS F 126 CYS F 196 1555 1555 2.03 SSBOND 38 CYS F 131 CYS F 157 1555 1555 2.03 SSBOND 39 CYS F 218 CYS F 247 1555 1555 2.03 SSBOND 40 CYS F 228 CYS F 239 1555 1555 2.03 SSBOND 41 CYS F 296 CYS F 331 1555 1555 2.03 SSBOND 42 CYS F 378 CYS F 445 1555 1555 2.04 SSBOND 43 CYS F 385 CYS F 418 1555 1555 2.03 SSBOND 44 CYS F 501 CYS D 605 1555 1555 2.03 SSBOND 45 CYS D 598 CYS D 604 1555 1555 2.03 LINK ND2 ASN B 88 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN B 133 C1 NAG B 607 1555 1555 1.44 LINK ND2 ASN B 156 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 160 C1 NAG B 602 1555 1555 1.44 LINK ND2 ASN B 197 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN B 234 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN B 262 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN B 276 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN B 295 C1 NAG B 603 1555 1555 1.44 LINK ND2 ASN B 332 C1 NAG B 604 1555 1555 1.44 LINK ND2 ASN B 339 C1 NAG B 605 1555 1555 1.44 LINK ND2 ASN B 386 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN B 392 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN B 448 C1 NAG B 606 1555 1555 1.44 LINK ND2 ASN A 611 C1 NAG A 702 1555 1555 1.44 LINK ND2 ASN A 618 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 637 C1 NAG A 703 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 607 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 606 1555 1555 1.44 LINK ND2 ASN C 611 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 618 C1 NAG C 701 1555 1555 1.44 LINK ND2 ASN C 637 C1 NAG C 703 1555 1555 1.44 LINK ND2 ASN F 88 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN F 133 C1 NAG F 607 1555 1555 1.44 LINK ND2 ASN F 156 C1 NAG F 601 1555 1555 1.44 LINK ND2 ASN F 160 C1 NAG F 602 1555 1555 1.44 LINK ND2 ASN F 197 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN F 234 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN F 262 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN F 276 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN F 295 C1 NAG F 603 1555 1555 1.44 LINK ND2 ASN F 332 C1 NAG F 604 1555 1555 1.44 LINK ND2 ASN F 339 C1 NAG F 605 1555 1555 1.44 LINK ND2 ASN F 386 C1 NAG l 1 1555 1555 1.44 LINK ND2 ASN F 392 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN F 448 C1 NAG F 606 1555 1555 1.44 LINK ND2 ASN D 611 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN D 618 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 637 C1 NAG D 703 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG 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 O6 BMA V 3 C1 MAN V 6 1555 1555 1.45 LINK O2 MAN V 4 C1 MAN V 5 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.43 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O3 BMA W 3 C1 MAN W 4 1555 1555 1.45 LINK O6 BMA W 3 C1 MAN W 5 1555 1555 1.46 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.45 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.44 LINK O3 BMA c 3 C1 MAN c 4 1555 1555 1.44 LINK O6 BMA c 3 C1 MAN c 6 1555 1555 1.45 LINK O2 MAN c 4 C1 MAN c 5 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.43 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.45 LINK O6 BMA d 3 C1 MAN d 5 1555 1555 1.46 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.45 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.44 LINK O3 BMA j 3 C1 MAN j 4 1555 1555 1.44 LINK O6 BMA j 3 C1 MAN j 6 1555 1555 1.45 LINK O2 MAN j 4 C1 MAN j 5 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.43 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O3 BMA k 3 C1 MAN k 4 1555 1555 1.45 LINK O6 BMA k 3 C1 MAN k 5 1555 1555 1.46 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.44 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.44 CISPEP 1 SER G 7 PRO G 8 0 -6.26 CISPEP 2 TRP G 94 PRO G 95 0 -1.67 CISPEP 3 SER L 7 PRO L 8 0 -7.10 CISPEP 4 THR L 95 PRO L 95A 0 4.28 CISPEP 5 SER I 7 PRO I 8 0 -6.25 CISPEP 6 TRP I 94 PRO I 95 0 -1.70 CISPEP 7 SER Q 7 PRO Q 8 0 -7.07 CISPEP 8 THR Q 95 PRO Q 95A 0 4.28 CISPEP 9 SER K 7 PRO K 8 0 -6.30 CISPEP 10 TRP K 94 PRO K 95 0 -1.66 CISPEP 11 SER R 7 PRO R 8 0 -7.11 CISPEP 12 THR R 95 PRO R 95A 0 4.30 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