HEADER VIRAL PROTEIN 17-MAY-23 8SW4 TITLE BG505 GT1.1 SOSIP IN COMPLEX WITH NHP FABS 21N13, 21M20 AND RM20A3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 21M20 HEAVY CHAIN VARIABLE REGION; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 21M20 LIGHT CHAIN VARIABLE REGION; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: BG505 GT1.1 SOSIP GP120; COMPND 11 CHAIN: A, C, D; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 16 CHAIN: B, G, I; COMPND 17 FRAGMENT: UNP RESIDUES 509-661; COMPND 18 SYNONYM: ENV POLYPROTEIN; COMPND 19 ENGINEERED: YES; COMPND 20 MUTATION: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: RM20A3 HEAVY CHAIN VARIABLE REGION; COMPND 23 CHAIN: E, J, K; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: RM20A3 LIGHT CHAIN VARIABLE REGION; COMPND 27 CHAIN: F, M, N; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 7; COMPND 30 MOLECULE: 21N13 HEAVY CHAIN VARIABLE REGION; COMPND 31 CHAIN: O, Q, S; COMPND 32 ENGINEERED: YES; COMPND 33 MOL_ID: 8; COMPND 34 MOLECULE: 21N13 LIGHT CHAIN VARIABLE REGION; COMPND 35 CHAIN: P, R, T; COMPND 36 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA; SOURCE 3 ORGANISM_TAXID: 9539; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA; SOURCE 9 ORGANISM_TAXID: 9539; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 15 ORGANISM_TAXID: 11676; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 21 ORGANISM_TAXID: 11676; SOURCE 22 CELL_LINE: HEK293F; SOURCE 23 GENE: ENV; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: MACACA; SOURCE 29 ORGANISM_TAXID: 9539; SOURCE 30 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: MACACA; SOURCE 35 ORGANISM_TAXID: 9539; SOURCE 36 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 39 MOL_ID: 7; SOURCE 40 ORGANISM_SCIENTIFIC: MACACA; SOURCE 41 ORGANISM_TAXID: 9539; SOURCE 42 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 43 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 44 EXPRESSION_SYSTEM_CELL_LINE: HEK293F; SOURCE 45 MOL_ID: 8; SOURCE 46 ORGANISM_SCIENTIFIC: MACACA; SOURCE 47 ORGANISM_TAXID: 9539; SOURCE 48 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 50 EXPRESSION_SYSTEM_CELL_LINE: HEK293F KEYWDS GERMLINE TARGETING, HIV-1 ENV, NEUTRALIZING ANTIBODY, NON-HUMAN KEYWDS 2 PRIMATE ANTIBODY, CD4 BINDING SITE, FUSION PEPTIDE, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR G.OZOROWSKI,J.L.TORRES,S.ZHANG,A.B.WARD JRNL AUTH T.CANIELS,G.OZOROWSKI,A.B.WARD,R.W.SANDERS JRNL TITL NEUTRALIZING ANTIBODIES INDUCED IN NON-HUMAN PRIMATES BY JRNL TITL 2 GERMLINE TARGETING ENV TRIMER JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, EPU, 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) : 2.850 REMARK 3 NUMBER OF PARTICLES : 242098 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 8SW4 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_1000273042. 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 : BG505 GT1.1 SOSIP IN COMPLEX REMARK 245 WITH 21N13 FAB, 21M20 FAB AND REMARK 245 RM20A3 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 6.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 48.50 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 190000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: EICOSAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, B, E, F, C, G, J, M, REMARK 350 AND CHAINS: D, I, K, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU H 1 REMARK 465 SER H 113 REMARK 465 ASP L 1 REMARK 465 MET A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 MET A -1 REMARK 465 LYS A 0 REMARK 465 ARG A 1 REMARK 465 GLY A 2 REMARK 465 LEU A 3 REMARK 465 CYS A 4 REMARK 465 CYS A 5 REMARK 465 VAL A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 LEU A 9 REMARK 465 CYS A 10 REMARK 465 GLY A 11 REMARK 465 ALA A 12 REMARK 465 VAL A 13 REMARK 465 PHE A 14 REMARK 465 VAL A 15 REMARK 465 SER A 16 REMARK 465 PRO A 17 REMARK 465 SER A 18 REMARK 465 GLN A 19 REMARK 465 GLU A 20 REMARK 465 ILE A 21 REMARK 465 HIS A 22 REMARK 465 ALA A 23 REMARK 465 ARG A 24 REMARK 465 PHE A 25 REMARK 465 ARG A 26 REMARK 465 ARG A 27 REMARK 465 GLY A 28 REMARK 465 ALA A 29 REMARK 465 ARG A 30 REMARK 465 ALA A 31 REMARK 465 GLU A 32 REMARK 465 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 LYS A 64 REMARK 465 LYS A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 VAL A 68 REMARK 465 TRP A 69 REMARK 465 ALA A 70 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 ASN A 399 REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 SER A 460 REMARK 465 THR A 461 REMARK 465 ASP A 462 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 GLU E 1 REMARK 465 SER E 112 REMARK 465 GLN F 1 REMARK 465 SER F 2 REMARK 465 LEU F 107 REMARK 465 MET C -4 REMARK 465 ASP C -3 REMARK 465 ALA C -2 REMARK 465 MET C -1 REMARK 465 LYS C 0 REMARK 465 ARG C 1 REMARK 465 GLY C 2 REMARK 465 LEU C 3 REMARK 465 CYS C 4 REMARK 465 CYS C 5 REMARK 465 VAL C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 LEU C 9 REMARK 465 CYS C 10 REMARK 465 GLY C 11 REMARK 465 ALA C 12 REMARK 465 VAL C 13 REMARK 465 PHE C 14 REMARK 465 VAL C 15 REMARK 465 SER C 16 REMARK 465 PRO C 17 REMARK 465 SER C 18 REMARK 465 GLN C 19 REMARK 465 GLU C 20 REMARK 465 ILE C 21 REMARK 465 HIS C 22 REMARK 465 ALA C 23 REMARK 465 ARG C 24 REMARK 465 PHE C 25 REMARK 465 ARG C 26 REMARK 465 ARG C 27 REMARK 465 GLY C 28 REMARK 465 ALA C 29 REMARK 465 ARG C 30 REMARK 465 ALA C 31 REMARK 465 GLU C 32 REMARK 465 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 LYS C 64 REMARK 465 LYS C 65 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 THR C 461 REMARK 465 ASP C 462 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 G 512 REMARK 465 VAL G 513 REMARK 465 GLY G 514 REMARK 465 ILE G 515 REMARK 465 GLY G 516 REMARK 465 ALA G 517 REMARK 465 VAL G 518 REMARK 465 PHE G 519 REMARK 465 GLY G 547 REMARK 465 ILE G 548 REMARK 465 VAL G 549 REMARK 465 GLN G 550 REMARK 465 GLN G 551 REMARK 465 GLN G 552 REMARK 465 SER G 553 REMARK 465 ASN G 554 REMARK 465 LEU G 555 REMARK 465 LEU G 556 REMARK 465 ARG G 557 REMARK 465 ALA G 558 REMARK 465 PRO G 559 REMARK 465 GLU G 560 REMARK 465 ALA G 561 REMARK 465 GLN G 562 REMARK 465 GLN G 563 REMARK 465 HIS G 564 REMARK 465 LEU G 565 REMARK 465 LEU G 566 REMARK 465 LYS G 567 REMARK 465 LEU G 568 REMARK 465 THR G 569 REMARK 465 GLU J 1 REMARK 465 GLN M 1 REMARK 465 SER M 2 REMARK 465 LEU M 107 REMARK 465 MET D -4 REMARK 465 ASP D -3 REMARK 465 ALA D -2 REMARK 465 MET D -1 REMARK 465 LYS D 0 REMARK 465 ARG D 1 REMARK 465 GLY D 2 REMARK 465 LEU D 3 REMARK 465 CYS D 4 REMARK 465 CYS D 5 REMARK 465 VAL D 6 REMARK 465 LEU D 7 REMARK 465 LEU D 8 REMARK 465 LEU D 9 REMARK 465 CYS D 10 REMARK 465 GLY D 11 REMARK 465 ALA D 12 REMARK 465 VAL D 13 REMARK 465 PHE D 14 REMARK 465 VAL D 15 REMARK 465 SER D 16 REMARK 465 PRO D 17 REMARK 465 SER D 18 REMARK 465 GLN D 19 REMARK 465 GLU D 20 REMARK 465 ILE D 21 REMARK 465 HIS D 22 REMARK 465 ALA D 23 REMARK 465 ARG D 24 REMARK 465 PHE D 25 REMARK 465 ARG D 26 REMARK 465 ARG D 27 REMARK 465 GLY D 28 REMARK 465 ALA D 29 REMARK 465 ARG D 30 REMARK 465 ALA D 31 REMARK 465 GLU D 32 REMARK 465 ALA D 58 REMARK 465 LYS D 59 REMARK 465 ALA D 60 REMARK 465 TYR D 61 REMARK 465 GLU D 62 REMARK 465 THR D 63 REMARK 465 LYS D 64 REMARK 465 LYS D 65 REMARK 465 HIS D 66 REMARK 465 GLU D 185A REMARK 465 ASN D 185B REMARK 465 GLN D 185C REMARK 465 THR D 400 REMARK 465 SER D 401 REMARK 465 VAL D 402 REMARK 465 GLN D 403 REMARK 465 GLY D 404 REMARK 465 SER D 405 REMARK 465 ASN D 406 REMARK 465 SER D 407 REMARK 465 THR D 408 REMARK 465 GLY D 409 REMARK 465 SER D 410 REMARK 465 SER D 460 REMARK 465 THR D 461 REMARK 465 ASP D 462 REMARK 465 SER D 463 REMARK 465 ARG D 504 REMARK 465 VAL D 505 REMARK 465 VAL D 506 REMARK 465 GLY D 507 REMARK 465 ARG D 508 REMARK 465 ARG D 509 REMARK 465 ARG D 510 REMARK 465 ARG D 511 REMARK 465 ARG D 512 REMARK 465 ARG D 513 REMARK 465 ALA I 512 REMARK 465 VAL I 513 REMARK 465 GLY I 514 REMARK 465 ILE I 515 REMARK 465 GLY I 516 REMARK 465 ALA I 517 REMARK 465 VAL I 518 REMARK 465 PHE I 519 REMARK 465 GLY I 547 REMARK 465 ILE I 548 REMARK 465 VAL I 549 REMARK 465 GLN I 550 REMARK 465 GLN I 551 REMARK 465 GLN I 552 REMARK 465 SER I 553 REMARK 465 ASN I 554 REMARK 465 LEU I 555 REMARK 465 LEU I 556 REMARK 465 ARG I 557 REMARK 465 ALA I 558 REMARK 465 PRO I 559 REMARK 465 GLU I 560 REMARK 465 ALA I 561 REMARK 465 GLN I 562 REMARK 465 GLN I 563 REMARK 465 HIS I 564 REMARK 465 LEU I 565 REMARK 465 LEU I 566 REMARK 465 LYS I 567 REMARK 465 LEU I 568 REMARK 465 GLU K 1 REMARK 465 GLN N 1 REMARK 465 SER N 2 REMARK 465 LEU N 107 REMARK 465 SER O 112 REMARK 465 PRO O 113 REMARK 465 SER O 114 REMARK 465 LYS P 107 REMARK 465 GLN Q 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 SG CYS D 218 SG CYS D 247 1.60 REMARK 500 SG CYS D 126 SG CYS D 196 1.80 REMARK 500 OG SER M 14 OE1 GLN M 17 2.01 REMARK 500 O SER S 32 OH TYR S 100C 2.03 REMARK 500 OD1 ASN A 99 NE2 GLN A 103 2.09 REMARK 500 NZ LYS C 207 OD2 ASP O 27 2.17 REMARK 500 OG SER N 12 OG1 THR N 105 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS J 92 CA - CB - SG ANGL. DEV. = 8.1 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 SER H 30 -14.46 -154.29 REMARK 500 ALA L 30 -122.00 51.85 REMARK 500 ALA L 51 -56.85 75.63 REMARK 500 THR A 77 4.18 90.11 REMARK 500 ASP A 78 155.60 72.79 REMARK 500 GLN A 258 -56.48 66.60 REMARK 500 GLU A 268 -57.55 -120.62 REMARK 500 PRO A 313 76.65 -68.12 REMARK 500 PHE A 391 69.58 -111.82 REMARK 500 THR A 464 -11.32 73.84 REMARK 500 GLN B 650 -71.04 -139.10 REMARK 500 ASN F 31 53.42 -92.03 REMARK 500 ASP F 50 -173.70 59.42 REMARK 500 THR C 163 -146.81 -119.85 REMARK 500 THR C 189 -1.98 72.37 REMARK 500 GLN C 258 -56.55 66.62 REMARK 500 ASN C 262 -178.70 61.54 REMARK 500 PRO C 313 96.92 -66.25 REMARK 500 PHE C 391 67.34 -107.27 REMARK 500 THR C 464 -13.55 72.54 REMARK 500 LEU C 483 55.05 -90.04 REMARK 500 GLU C 492 78.30 -118.14 REMARK 500 ASN G 651 -62.85 -145.89 REMARK 500 ASP M 50 -176.30 66.64 REMARK 500 THR D 189 -10.71 74.52 REMARK 500 HIS D 249 170.36 -56.20 REMARK 500 GLN D 258 -57.65 66.83 REMARK 500 ASN D 262 -174.86 60.61 REMARK 500 GLU D 268 -54.77 -125.36 REMARK 500 PHE D 391 76.85 -112.55 REMARK 500 ASN D 392 74.03 -154.20 REMARK 500 TRP I 571 -10.81 89.40 REMARK 500 SER I 636 -58.44 -131.68 REMARK 500 GLN I 652 -64.84 -129.23 REMARK 500 ASN N 31 57.80 -90.25 REMARK 500 ASP N 50 -124.87 56.32 REMARK 500 CYS P 32 40.47 -109.98 REMARK 500 THR P 51 -53.14 71.09 REMARK 500 CYS R 32 57.02 -97.60 REMARK 500 ARG R 50 -166.28 -121.50 REMARK 500 TYR S 33 18.78 59.85 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-40797 RELATED DB: EMDB REMARK 900 BG505 GT1.1 SOSIP IN COMPLEX WITH NHP FABS 21N13, 21M20 AND RM20A3 DBREF 8SW4 H 1 113 PDB 8SW4 8SW4 1 113 DBREF 8SW4 L 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 A -4 513 PDB 8SW4 8SW4 -4 513 DBREF 8SW4 B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8SW4 E 1 112 PDB 8SW4 8SW4 1 112 DBREF 8SW4 F 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 C -4 513 PDB 8SW4 8SW4 -4 513 DBREF 8SW4 G 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8SW4 J 1 112 PDB 8SW4 8SW4 1 112 DBREF 8SW4 M 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 D -4 513 PDB 8SW4 8SW4 -4 513 DBREF 8SW4 I 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8SW4 K 1 112 PDB 8SW4 8SW4 1 112 DBREF 8SW4 N 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 O 1 114 PDB 8SW4 8SW4 1 114 DBREF 8SW4 P 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 Q 1 114 PDB 8SW4 8SW4 1 114 DBREF 8SW4 R 1 107 PDB 8SW4 8SW4 1 107 DBREF 8SW4 S 1 114 PDB 8SW4 8SW4 1 114 DBREF 8SW4 T 1 107 PDB 8SW4 8SW4 1 107 SEQADV 8SW4 PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 8SW4 CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 8SW4 PRO G 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 8SW4 CYS G 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQADV 8SW4 PRO I 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 8SW4 CYS I 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQRES 1 H 125 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU ALA LYS SEQRES 2 H 125 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 125 PHE THR PHE SER ARG SER ILE MET HIS TRP VAL ARG GLN SEQRES 4 H 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER THR ILE ASN SEQRES 5 H 125 TYR ALA GLY SER THR TYR TYR ALA ASP SER VAL ARG GLY SEQRES 6 H 125 ARG PHE VAL ILE SER ARG ASP ASN SER LYS ASN THR LEU SEQRES 7 H 125 SER LEU GLN MET ASN SER VAL ARG PRO GLU ASP ARG ALA SEQRES 8 H 125 VAL TYR HIS CYS ALA LYS ASP LYS GLU GLY TYR TYR SER SEQRES 9 H 125 GLY GLY TYR PRO LEU TRP TYR PHE ASP LEU TRP GLY PRO SEQRES 10 H 125 GLY THR PRO VAL THR ILE SER SER SEQRES 1 L 107 ASP VAL GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 107 SER VAL GLY ASP LYS VAL SER ILE THR CYS ARG ALA SER SEQRES 3 L 107 GLN GLY ILE ALA ASP ALA LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 107 ASN LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE SER LEU THR ILE SER SER LEU SEQRES 7 L 107 GLN ALA GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 107 ASN SER HIS PRO PRO THR PHE GLY GLN GLY THR ARG VAL SEQRES 9 L 107 GLU VAL LYS SEQRES 1 A 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 A 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 A 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 A 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 A 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 A 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 A 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 A 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 A 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 A 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 A 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 A 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 A 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 A 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 A 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 A 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 A 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 A 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 A 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 A 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 A 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 A 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 A 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 A 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 A 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 A 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 A 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 A 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 A 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 A 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 A 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 A 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 A 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 A 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 A 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 A 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 A 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 A 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 A 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 A 509 ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 124 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 E 124 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 E 124 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 E 124 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 E 124 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 E 124 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 E 124 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 E 124 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 E 124 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 E 124 GLY ALA LEU VAL THR VAL SER SEQRES 1 F 111 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY SER SEQRES 2 F 111 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 F 111 SER ASP ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 F 111 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 F 111 VAL THR GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER SEQRES 6 F 111 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 F 111 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 F 111 ALA TYR ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY SEQRES 9 F 111 GLY THR ARG LEU THR VAL LEU SEQRES 1 C 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 C 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 C 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 C 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 C 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 C 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 C 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 C 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 C 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 C 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 C 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 C 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 C 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 C 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 C 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 C 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 C 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 C 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 C 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 C 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 C 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 C 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 C 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 C 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 C 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 C 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 C 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 C 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 C 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 C 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 C 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 C 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 C 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 C 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 C 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 C 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 C 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 C 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 C 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 C 509 ARG ARG SEQRES 1 G 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 G 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 G 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 G 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 G 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 G 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 G 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 G 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 G 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 G 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 G 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 G 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 J 124 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 J 124 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 J 124 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 J 124 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 J 124 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 J 124 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 J 124 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 J 124 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 J 124 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 J 124 GLY ALA LEU VAL THR VAL SER SEQRES 1 M 111 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY SER SEQRES 2 M 111 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 M 111 SER ASP ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 M 111 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 M 111 VAL THR GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER SEQRES 6 M 111 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 M 111 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 M 111 ALA TYR ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY SEQRES 9 M 111 GLY THR ARG LEU THR VAL LEU SEQRES 1 D 509 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 D 509 LEU CYS GLY ALA VAL PHE VAL SER PRO SER GLN GLU ILE SEQRES 3 D 509 HIS ALA ARG PHE ARG ARG GLY ALA ARG ALA GLU ASN LEU SEQRES 4 D 509 TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP LYS ASP SEQRES 5 D 509 ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA LYS ALA SEQRES 6 D 509 TYR GLU THR LYS LYS HIS ASN VAL TRP ALA THR HIS ALA SEQRES 7 D 509 CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE HIS LEU SEQRES 8 D 509 GLU ASN VAL THR GLU GLU PHE ASN MET TRP LYS ASN ASN SEQRES 9 D 509 MET VAL GLU GLN MET HIS THR ASP ILE ILE SER LEU TRP SEQRES 10 D 509 ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR PRO LEU SEQRES 11 D 509 CYS VAL THR LEU GLN CYS THR ASN VAL THR ASN ASN ILE SEQRES 12 D 509 THR ASP ASP MET ARG GLY GLU LEU LYS ASN CYS SER PHE SEQRES 13 D 509 ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN LYS VAL SEQRES 14 D 509 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE ASN SEQRES 15 D 509 GLU ASN GLN ASN THR SER TYR ARG LEU ILE ASN CYS ASN SEQRES 16 D 509 THR ALA ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE SEQRES 17 D 509 GLU PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE SEQRES 18 D 509 ALA ILE LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR SEQRES 19 D 509 GLY PRO CYS PRO SER VAL SER THR VAL GLN CYS THR HIS SEQRES 20 D 509 GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN SEQRES 21 D 509 GLY SER LEU ALA GLU GLU GLU VAL MET ILE ARG SER LYS SEQRES 22 D 509 ASP ILE ARG ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE SEQRES 23 D 509 ASN THR PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN SEQRES 24 D 509 ASN THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN TRP SEQRES 25 D 509 PHE TYR ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN SEQRES 26 D 509 ALA HIS CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR SEQRES 27 D 509 LEU GLY LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY SEQRES 28 D 509 ASN ASN THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY SEQRES 29 D 509 ASP LEU GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 30 D 509 GLU PHE PHE TYR CYS ASP THR SER GLY LEU PHE ASN SER SEQRES 31 D 509 THR TRP ILE SER ASN THR SER VAL GLN GLY SER ASN SER SEQRES 32 D 509 THR GLY SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE SEQRES 33 D 509 LYS GLN ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA SEQRES 34 D 509 MET TYR ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SEQRES 35 D 509 SER ASN ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SEQRES 36 D 509 SER THR ASP SER THR THR GLU THR PHE ARG PRO SER GLY SEQRES 37 D 509 GLY ASP MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS SEQRES 38 D 509 TYR LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO SEQRES 39 D 509 THR ARG CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG SEQRES 40 D 509 ARG ARG SEQRES 1 I 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 I 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 I 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 I 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 I 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 I 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 I 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 I 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 I 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 I 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 I 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 I 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 K 124 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 K 124 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 K 124 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 K 124 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 K 124 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 K 124 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 K 124 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 K 124 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 K 124 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 K 124 GLY ALA LEU VAL THR VAL SER SEQRES 1 N 111 GLN SER ALA LEU THR GLN PRO PRO SER VAL SER GLY SER SEQRES 2 N 111 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 N 111 SER ASP ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 N 111 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP SEQRES 5 N 111 VAL THR GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER SEQRES 6 N 111 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 N 111 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 N 111 ALA TYR ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY SEQRES 9 N 111 GLY THR ARG LEU THR VAL LEU SEQRES 1 O 130 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY ARG VAL LYS SEQRES 2 O 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER ASP SEQRES 3 O 130 ASP SER PHE GLY SER SER TYR PHE TYR TRP SER TRP ILE SEQRES 4 O 130 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 O 130 ILE ALA TYR SER GLY GLY VAL ARG TYR ASN PRO SER LEU SEQRES 6 O 130 SER SER ARG VAL THR ILE SER ARG ASN ILE HIS GLU ARG SEQRES 7 O 130 GLN PHE TYR LEU ARG LEU THR SER MET THR ALA ALA ASP SEQRES 8 O 130 THR ALA VAL TYR TYR CYS ALA ARG HIS CYS GLU ASP ASP SEQRES 9 O 130 TYR GLY TYR TYR SER ALA ALA GLN SER TYR GLY LEU ASP SEQRES 10 O 130 SER TRP GLY GLN GLY ILE ALA VAL THR VAL SER PRO SER SEQRES 1 P 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 P 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER SEQRES 3 P 107 GLU ASN VAL ASN ASN CYS LEU ASN TRP TYR GLN GLN LYS SEQRES 4 P 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SER SEQRES 5 P 107 THR LEU GLN ARG GLY VAL PRO SER ARG PHE SER GLY THR SEQRES 6 P 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 P 107 GLN SER GLU ASP PHE GLY THR TYR TYR CYS GLN HIS TYR SEQRES 8 P 107 TYR GLY THR PRO LEU THR PHE GLY GLY GLY THR MET VAL SEQRES 9 P 107 ASP ILE LYS SEQRES 1 Q 130 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY ARG VAL LYS SEQRES 2 Q 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER ASP SEQRES 3 Q 130 ASP SER PHE GLY SER SER TYR PHE TYR TRP SER TRP ILE SEQRES 4 Q 130 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 Q 130 ILE ALA TYR SER GLY GLY VAL ARG TYR ASN PRO SER LEU SEQRES 6 Q 130 SER SER ARG VAL THR ILE SER ARG ASN ILE HIS GLU ARG SEQRES 7 Q 130 GLN PHE TYR LEU ARG LEU THR SER MET THR ALA ALA ASP SEQRES 8 Q 130 THR ALA VAL TYR TYR CYS ALA ARG HIS CYS GLU ASP ASP SEQRES 9 Q 130 TYR GLY TYR TYR SER ALA ALA GLN SER TYR GLY LEU ASP SEQRES 10 Q 130 SER TRP GLY GLN GLY ILE ALA VAL THR VAL SER PRO SER SEQRES 1 R 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 R 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER SEQRES 3 R 107 GLU ASN VAL ASN ASN CYS LEU ASN TRP TYR GLN GLN LYS SEQRES 4 R 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SER SEQRES 5 R 107 THR LEU GLN ARG GLY VAL PRO SER ARG PHE SER GLY THR SEQRES 6 R 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 R 107 GLN SER GLU ASP PHE GLY THR TYR TYR CYS GLN HIS TYR SEQRES 8 R 107 TYR GLY THR PRO LEU THR PHE GLY GLY GLY THR MET VAL SEQRES 9 R 107 ASP ILE LYS SEQRES 1 S 130 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY ARG VAL LYS SEQRES 2 S 130 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER ASP SEQRES 3 S 130 ASP SER PHE GLY SER SER TYR PHE TYR TRP SER TRP ILE SEQRES 4 S 130 ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR SEQRES 5 S 130 ILE ALA TYR SER GLY GLY VAL ARG TYR ASN PRO SER LEU SEQRES 6 S 130 SER SER ARG VAL THR ILE SER ARG ASN ILE HIS GLU ARG SEQRES 7 S 130 GLN PHE TYR LEU ARG LEU THR SER MET THR ALA ALA ASP SEQRES 8 S 130 THR ALA VAL TYR TYR CYS ALA ARG HIS CYS GLU ASP ASP SEQRES 9 S 130 TYR GLY TYR TYR SER ALA ALA GLN SER TYR GLY LEU ASP SEQRES 10 S 130 SER TRP GLY GLN GLY ILE ALA VAL THR VAL SER PRO SER SEQRES 1 T 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 T 107 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG THR SER SEQRES 3 T 107 GLU ASN VAL ASN ASN CYS LEU ASN TRP TYR GLN GLN LYS SEQRES 4 T 107 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ARG THR SER SEQRES 5 T 107 THR LEU GLN ARG GLY VAL PRO SER ARG PHE SER GLY THR SEQRES 6 T 107 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 T 107 GLN SER GLU ASP PHE GLY THR TYR TYR CYS GLN HIS TYR SEQRES 8 T 107 TYR GLY THR PRO LEU THR PHE GLY GLY GLY THR MET VAL SEQRES 9 T 107 ASP ILE LYS HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 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 G 701 14 HET NAG G 702 14 HET NAG D 601 14 HET NAG D 602 14 HET NAG D 603 14 HET NAG D 604 14 HET NAG D 605 14 HET NAG D 606 14 HET NAG D 607 14 HET NAG D 608 14 HET NAG D 609 14 HET NAG I 701 14 HET NAG I 702 14 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET MAN U 4 11 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET BMA W 3 11 HET MAN W 4 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET MAN X 4 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 21 NAG 41(C8 H15 N O6) FORMUL 54 BMA 3(C6 H12 O6) FORMUL 54 MAN 3(C6 H12 O6) HELIX 1 AA1 ASN H 73 LYS H 75 5 3 HELIX 2 AA2 ARG H 83 ARG H 87 5 5 HELIX 3 AA3 GLN L 79 PHE L 83 5 5 HELIX 4 AA4 ASN A 98 LYS A 117 1 20 HELIX 5 AA5 LYS A 335 GLY A 354 1 20 HELIX 6 AA6 ASP A 368 THR A 373 1 6 HELIX 7 AA7 THR A 387 LEU A 390 5 4 HELIX 8 AA8 ASN A 425 ARG A 429 5 5 HELIX 9 AA9 MET A 475 ARG A 480 1 6 HELIX 10 AB1 LEU B 523 SER B 528 5 6 HELIX 11 AB2 THR B 529 SER B 534 1 6 HELIX 12 AB3 MET B 535 LEU B 537 5 3 HELIX 13 AB4 VAL B 570 TRP B 596 1 27 HELIX 14 AB5 ASN B 618 ASP B 624 1 7 HELIX 15 AB6 THR B 627 SER B 636 1 10 HELIX 16 AB7 TYR B 638 SER B 649 1 12 HELIX 17 AB8 GLN B 650 ALA B 662 1 13 HELIX 18 AB9 THR E 28 PHE E 32 5 5 HELIX 19 AC1 ASP E 61 LYS E 64 5 4 HELIX 20 AC2 ARG E 83 THR E 87 5 5 HELIX 21 AC3 GLN F 79 GLU F 83 5 5 HELIX 22 AC4 ALA C 70 CYS C 74 5 5 HELIX 23 AC5 ASN C 98 LYS C 117 1 20 HELIX 24 AC6 LEU C 122 CYS C 126 5 5 HELIX 25 AC7 LYS C 335 GLY C 354 1 20 HELIX 26 AC8 ASP C 368 THR C 373 1 6 HELIX 27 AC9 THR C 387 LEU C 390 5 4 HELIX 28 AD1 ASN C 425 ARG C 429 5 5 HELIX 29 AD2 MET C 475 SER C 481 1 7 HELIX 30 AD3 LEU G 523 SER G 528 5 6 HELIX 31 AD4 THR G 529 SER G 534 1 6 HELIX 32 AD5 THR G 536 ARG G 542 1 7 HELIX 33 AD6 GLY G 572 TRP G 596 1 25 HELIX 34 AD7 LEU G 619 ASP G 624 1 6 HELIX 35 AD8 THR G 627 ILE G 635 1 9 HELIX 36 AD9 TYR G 638 GLN G 650 1 13 HELIX 37 AE1 ASN G 651 ALA G 662 1 12 HELIX 38 AE2 THR J 28 PHE J 32 5 5 HELIX 39 AE3 ASP J 61 LYS J 64 5 4 HELIX 40 AE4 ARG J 83 THR J 87 5 5 HELIX 41 AE5 GLN M 79 GLU M 83 5 5 HELIX 42 AE6 ALA D 70 CYS D 74 5 5 HELIX 43 AE7 ASN D 98 LYS D 117 1 20 HELIX 44 AE8 LEU D 122 CYS D 126 5 5 HELIX 45 AE9 THR D 139 ARG D 151 5 5 HELIX 46 AF1 LYS D 335 ARG D 350 1 16 HELIX 47 AF2 ASP D 368 THR D 373 1 6 HELIX 48 AF3 THR D 387 LEU D 390 5 4 HELIX 49 AF4 ASN D 425 ARG D 429 5 5 HELIX 50 AF5 MET D 475 TYR D 484 1 10 HELIX 51 AF6 LEU I 523 SER I 528 5 6 HELIX 52 AF7 THR I 529 SER I 534 1 6 HELIX 53 AF8 THR I 536 ARG I 542 1 7 HELIX 54 AF9 GLY I 572 TRP I 596 1 25 HELIX 55 AG1 ASN I 618 ILE I 622 5 5 HELIX 56 AG2 THR I 627 ILE I 635 1 9 HELIX 57 AG3 TYR I 638 GLN I 650 1 13 HELIX 58 AG4 GLN I 652 ALA I 662 1 11 HELIX 59 AG5 THR K 28 PHE K 32 5 5 HELIX 60 AG6 ASP K 61 LYS K 64 5 4 HELIX 61 AG7 ARG K 83 THR K 87 5 5 HELIX 62 AG8 GLN N 79 GLU N 83 5 5 HELIX 63 AG9 ASP O 26 SER O 31 5 6 HELIX 64 AH1 THR O 83 THR O 87 5 5 HELIX 65 AH2 ASP Q 27 SER Q 31 5 5 HELIX 66 AH3 THR Q 83 THR Q 87 5 5 HELIX 67 AH4 ASP S 26 SER S 31 5 6 HELIX 68 AH5 LEU S 63 SER S 65 5 3 HELIX 69 AH6 THR S 83 THR S 87 5 5 SHEET 1 AA1 4 LEU H 4 GLY H 8 0 SHEET 2 AA1 4 SER H 17 ALA H 24 -1 O ALA H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 ASN H 82A-1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N VAL H 68 O GLN H 81 SHEET 1 AA2 7 GLY H 10 ALA H 12 0 SHEET 2 AA2 7 MET H 34 ALA H 40 0 SHEET 3 AA2 7 GLY H 44 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 4 AA2 7 THR H 57 TYR H 59 -1 O TYR H 58 N THR H 50 SHEET 5 AA2 7 ALA H 88 ASP H 95 -1 O HIS H 91 N VAL H 37 SHEET 6 AA2 7 PHE H 100I TRP H 103 -1 O LEU H 102 N LYS H 94 SHEET 7 AA2 7 THR H 107 ILE H 111 -1 O THR H 107 N TYR H 90 SHEET 1 AA3 4 MET L 4 SER L 7 0 SHEET 2 AA3 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA4 2 SER L 12 ALA L 13 0 SHEET 2 AA4 2 GLU L 105 VAL L 106 1 O GLU L 105 N ALA L 13 SHEET 1 AA5 6 LEU L 33 GLN L 38 0 SHEET 2 AA5 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 3 AA5 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 4 AA5 6 VAL L 85 GLN L 90 -1 O GLN L 89 N ALA L 34 SHEET 5 AA5 6 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 6 AA5 6 THR L 102 ARG L 103 -1 O THR L 102 N TYR L 86 SHEET 1 AA6 3 LEU A 494 THR A 499 0 SHEET 2 AA6 3 TRP A 35 TYR A 40 -1 N TRP A 35 O THR A 499 SHEET 3 AA6 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA7 5 TRP A 45 ASP A 47 0 SHEET 2 AA7 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA7 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA7 5 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 5 AA7 5 ILE A 84 LEU A 86 -1 N ILE A 84 O THR A 244 SHEET 1 AA8 2 PHE A 53 ALA A 55 0 SHEET 2 AA8 2 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA9 2 GLU A 91 ASN A 94 0 SHEET 2 AA9 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AB1 5 ARG A 169 TYR A 177 0 SHEET 2 AB1 5 LEU A 154 THR A 162 -1 N PHE A 159 O VAL A 172 SHEET 3 AB1 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AB1 5 SER A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AB1 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AB2 3 ALA A 200 GLN A 203 0 SHEET 2 AB2 3 GLN A 432 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AB2 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AB312 LEU A 259 LEU A 261 0 SHEET 2 AB312 MET A 271 SER A 274 0 SHEET 3 AB312 ILE A 284 ARG A 308 -1 O LEU A 285 N ARG A 273 SHEET 4 AB312 TRP A 316 ILE A 323 -1 O ILE A 323 N ASN A 301 SHEET 5 AB312 ALA A 329 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 6 AB312 ILE A 358 PHE A 361 0 SHEET 7 AB312 HIS A 374 CYS A 378 0 SHEET 8 AB312 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 9 AB312 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 10 AB312 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 11 AB312 GLY A 441 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 12 AB312 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AB4 4 GLN E 3 GLU E 6 0 SHEET 2 AB4 4 LEU E 18 SER E 25 -1 O ARG E 23 N VAL E 5 SHEET 3 AB4 4 THR E 77 MET E 82 -1 O LEU E 80 N LEU E 20 SHEET 4 AB4 4 PHE E 67 ASP E 72 -1 N SER E 70 O SER E 79 SHEET 1 AB5 6 MET E 34 GLN E 39 0 SHEET 2 AB5 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 3 AB5 6 THR E 57 TYR E 59 -1 O PHE E 58 N LEU E 50 SHEET 4 AB5 6 ALA E 88 GLY E 95 -1 O TYR E 91 N VAL E 37 SHEET 5 AB5 6 PHE E 100H TRP E 103 -1 O PHE E 102 N THR E 94 SHEET 6 AB5 6 ALA E 107 VAL E 109 -1 O ALA E 107 N TYR E 90 SHEET 1 AB6 6 VAL F 11 SER F 12 0 SHEET 2 AB6 6 VAL F 33 GLN F 38 0 SHEET 3 AB6 6 LYS F 45 ILE F 48 -1 O MET F 47 N TRP F 35 SHEET 4 AB6 6 ASP F 85 ALA F 92 -1 O ASP F 85 N GLN F 38 SHEET 5 AB6 6 THR F 95A PHE F 98 -1 O ILE F 97 N ALA F 90 SHEET 6 AB6 6 THR F 102 THR F 105 -1 O THR F 102 N TYR F 86 SHEET 1 AB7 3 SER F 18 THR F 24 0 SHEET 2 AB7 3 THR F 70 SER F 76 -1 O ALA F 71 N CYS F 23 SHEET 3 AB7 3 PHE F 62 SER F 67 -1 N SER F 67 O THR F 70 SHEET 1 AB8 3 LEU C 494 THR C 499 0 SHEET 2 AB8 3 TRP C 35 TYR C 40 -1 N TRP C 35 O THR C 499 SHEET 3 AB8 3 ILE G 603 PRO G 609 -1 O VAL G 608 N VAL C 36 SHEET 1 AB9 5 TRP C 45 ASP C 47 0 SHEET 2 AB9 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB9 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB9 5 VAL C 242 VAL C 245 -1 O VAL C 245 N ILE C 225 SHEET 5 AB9 5 ILE C 84 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AC1 2 PHE C 53 ALA C 55 0 SHEET 2 AC1 2 HIS C 216 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AC2 2 GLU C 91 ASN C 94 0 SHEET 2 AC2 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AC3 5 ARG C 169 TYR C 177 0 SHEET 2 AC3 5 LEU C 154 THR C 162 -1 N LYS C 155 O PHE C 176 SHEET 3 AC3 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AC3 5 SER C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AC3 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AC4 3 ALA C 200 GLN C 203 0 SHEET 2 AC4 3 GLN C 432 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AC4 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC512 LEU C 259 LEU C 261 0 SHEET 2 AC512 MET C 271 SER C 274 0 SHEET 3 AC512 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 4 AC512 ILE C 322 ILE C 323 -1 O ILE C 323 N ASN C 301 SHEET 5 AC512 ALA C 329 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 6 AC512 ILE C 358 PHE C 361 0 SHEET 7 AC512 HIS C 374 CYS C 378 0 SHEET 8 AC512 GLU C 381 CYS C 385 -1 O CYS C 385 N HIS C 374 SHEET 9 AC512 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 10 AC512 SER C 413 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 11 AC512 GLY C 441 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 12 AC512 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AC6 2 LYS C 305 GLY C 312 0 SHEET 2 AC6 2 GLN C 315 ALA C 319 -1 O PHE C 317 N ILE C 307 SHEET 1 AC7 4 GLN J 3 GLY J 8 0 SHEET 2 AC7 4 LEU J 18 SER J 25 -1 O SER J 21 N THR J 7 SHEET 3 AC7 4 THR J 77 MET J 82 -1 O MET J 82 N LEU J 18 SHEET 4 AC7 4 PHE J 67 ASP J 72 -1 N SER J 70 O SER J 79 SHEET 1 AC8 7 LEU J 11 VAL J 12 0 SHEET 2 AC8 7 MET J 34 GLN J 39 0 SHEET 3 AC8 7 LEU J 45 ILE J 51 -1 O ILE J 51 N MET J 34 SHEET 4 AC8 7 THR J 57 TYR J 59 -1 O PHE J 58 N LEU J 50 SHEET 5 AC8 7 ALA J 88 GLY J 95 -1 O VAL J 89 N GLN J 39 SHEET 6 AC8 7 PHE J 100H TRP J 103 -1 O PHE J 102 N THR J 94 SHEET 7 AC8 7 ALA J 107 VAL J 111 -1 O VAL J 109 N ALA J 88 SHEET 1 AC9 3 VAL M 19 THR M 24 0 SHEET 2 AC9 3 THR M 70 ILE M 75 -1 O ALA M 71 N CYS M 23 SHEET 3 AC9 3 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74 SHEET 1 AD1 5 VAL M 33 GLN M 38 0 SHEET 2 AD1 5 LYS M 45 ILE M 48 -1 O MET M 47 N TRP M 35 SHEET 3 AD1 5 ALA M 84 TYR M 91 -1 O ASP M 85 N GLN M 38 SHEET 4 AD1 5 TYR M 96 PHE M 98 -1 O ILE M 97 N ALA M 90 SHEET 5 AD1 5 THR M 102 LEU M 104 -1 O LEU M 104 N ALA M 84 SHEET 1 AD2 3 LEU D 494 THR D 499 0 SHEET 2 AD2 3 TRP D 35 TYR D 40 -1 N TRP D 35 O THR D 499 SHEET 3 AD2 3 ILE I 603 PRO I 609 -1 O CYS I 604 N VAL D 38 SHEET 1 AD3 5 TRP D 45 ASP D 47 0 SHEET 2 AD3 5 TYR D 486 ILE D 491 -1 O LYS D 490 N LYS D 46 SHEET 3 AD3 5 PHE D 223 CYS D 228 -1 N ALA D 224 O VAL D 489 SHEET 4 AD3 5 VAL D 242 VAL D 245 -1 O VAL D 245 N ILE D 225 SHEET 5 AD3 5 ILE D 84 LEU D 86 -1 N ILE D 84 O THR D 244 SHEET 1 AD4 3 VAL D 75 PRO D 76 0 SHEET 2 AD4 3 PHE D 53 SER D 56 1 N SER D 56 O VAL D 75 SHEET 3 AD4 3 HIS D 216 CYS D 218 -1 O CYS D 218 N PHE D 53 SHEET 1 AD5 2 GLU D 91 ASN D 94 0 SHEET 2 AD5 2 THR D 236 CYS D 239 -1 O GLY D 237 N PHE D 93 SHEET 1 AD6 5 ARG D 169 TYR D 177 0 SHEET 2 AD6 5 LEU D 154 THR D 162 -1 N MET D 161 O GLN D 170 SHEET 3 AD6 5 LEU D 129 ASN D 133 -1 N GLN D 130 O SER D 158 SHEET 4 AD6 5 SER D 190 LEU D 193 -1 O TYR D 191 N LEU D 129 SHEET 5 AD6 5 ILE D 181 PRO D 183 -1 N VAL D 182 O ARG D 192 SHEET 1 AD7 3 ALA D 200 GLN D 203 0 SHEET 2 AD7 3 GLN D 432 TYR D 435 1 O TYR D 435 N THR D 202 SHEET 3 AD7 3 ILE D 423 ILE D 424 -1 N ILE D 424 O MET D 434 SHEET 1 AD812 LEU D 259 LEU D 261 0 SHEET 2 AD812 MET D 271 SER D 274 0 SHEET 3 AD812 ILE D 284 ASN D 302 -1 O LEU D 285 N ARG D 273 SHEET 4 AD812 ILE D 322 ILE D 323 -1 O ILE D 323 N ASN D 301 SHEET 5 AD812 HIS D 330 SER D 334 -1 O HIS D 330 N THR D 297 SHEET 6 AD812 ILE D 358 PHE D 361 0 SHEET 7 AD812 HIS D 374 CYS D 378 0 SHEET 8 AD812 GLU D 381 CYS D 385 -1 O GLU D 381 N CYS D 378 SHEET 9 AD812 SER D 393 TRP D 395 -1 O TRP D 395 N ILE D 359 SHEET 10 AD812 SER D 413 ILE D 420 -1 O ARG D 419 N TYR D 384 SHEET 11 AD812 GLY D 441 ARG D 456 -1 O LEU D 454 N ILE D 284 SHEET 12 AD812 THR D 465 PRO D 470 -1 O ARG D 469 N THR D 455 SHEET 1 AD9 2 LYS D 305 GLY D 312 0 SHEET 2 AD9 2 GLN D 315 ALA D 319 -1 O PHE D 317 N ILE D 307 SHEET 1 AE1 4 GLN K 3 GLU K 6 0 SHEET 2 AE1 4 LEU K 18 SER K 25 -1 O ARG K 23 N VAL K 5 SHEET 3 AE1 4 THR K 77 MET K 82 -1 O MET K 82 N LEU K 18 SHEET 4 AE1 4 PHE K 67 ASP K 72 -1 N ASP K 72 O THR K 77 SHEET 1 AE2 6 LEU K 11 VAL K 12 0 SHEET 2 AE2 6 ALA K 107 VAL K 111 1 O THR K 110 N VAL K 12 SHEET 3 AE2 6 ALA K 88 TYR K 91 -1 N TYR K 90 O ALA K 107 SHEET 4 AE2 6 MET K 34 GLN K 39 -1 N VAL K 37 O TYR K 91 SHEET 5 AE2 6 LEU K 45 ILE K 51 -1 O GLU K 46 N ARG K 38 SHEET 6 AE2 6 THR K 57 TYR K 59 -1 O PHE K 58 N LEU K 50 SHEET 1 AE3 2 THR K 94 GLY K 95 0 SHEET 2 AE3 2 PHE K 100H PHE K 102 -1 O PHE K 102 N THR K 94 SHEET 1 AE4 3 VAL N 19 THR N 24 0 SHEET 2 AE4 3 THR N 70 ILE N 75 -1 O ALA N 71 N CYS N 23 SHEET 3 AE4 3 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AE5 5 VAL N 33 GLN N 38 0 SHEET 2 AE5 5 LYS N 45 ILE N 48 -1 O MET N 47 N TRP N 35 SHEET 3 AE5 5 ASP N 85 TYR N 91 -1 O ASP N 85 N GLN N 38 SHEET 4 AE5 5 TYR N 96 PHE N 98 -1 O ILE N 97 N ALA N 90 SHEET 5 AE5 5 THR N 102 ARG N 103 -1 O THR N 102 N TYR N 86 SHEET 1 AE6 4 LEU O 4 SER O 7 0 SHEET 2 AE6 4 LEU O 18 VAL O 24 -1 O ALA O 23 N GLN O 5 SHEET 3 AE6 4 GLN O 77 LEU O 82 -1 O PHE O 78 N CYS O 22 SHEET 4 AE6 4 VAL O 67 ASN O 72 -1 N ASN O 72 O GLN O 77 SHEET 1 AE7 6 PHE O 34 GLN O 39 0 SHEET 2 AE7 6 LEU O 45 ALA O 52 -1 O GLU O 46 N ARG O 38 SHEET 3 AE7 6 VAL O 57 TYR O 59 -1 O ARG O 58 N TYR O 50 SHEET 4 AE7 6 ALA O 88 CYS O 96 -1 O TYR O 91 N ILE O 37 SHEET 5 AE7 6 SER O 102 TRP O 103 -1 O SER O 102 N ARG O 94 SHEET 6 AE7 6 ILE O 107 VAL O 109 -1 O VAL O 109 N ALA O 88 SHEET 1 AE8 4 MET P 4 SER P 7 0 SHEET 2 AE8 4 VAL P 19 THR P 25 -1 O ARG P 24 N THR P 5 SHEET 3 AE8 4 ASP P 70 ILE P 75 -1 O ILE P 75 N VAL P 19 SHEET 4 AE8 4 PHE P 62 SER P 67 -1 N SER P 63 O THR P 74 SHEET 1 AE9 7 SER P 10 SER P 12 0 SHEET 2 AE9 7 LEU P 33 GLN P 38 0 SHEET 3 AE9 7 LYS P 45 TYR P 49 -1 O LEU P 47 N TRP P 35 SHEET 4 AE9 7 THR P 53 LEU P 54 -1 O THR P 53 N TYR P 49 SHEET 5 AE9 7 GLY P 84 HIS P 90 -1 O THR P 85 N GLN P 38 SHEET 6 AE9 7 THR P 97 PHE P 98 -1 O THR P 97 N HIS P 90 SHEET 7 AE9 7 THR P 102 ASP P 105 -1 O THR P 102 N TYR P 86 SHEET 1 AF1 4 LEU Q 4 SER Q 7 0 SHEET 2 AF1 4 LEU Q 18 VAL Q 24 -1 O THR Q 21 N SER Q 7 SHEET 3 AF1 4 GLN Q 77 LEU Q 82 -1 O LEU Q 82 N LEU Q 18 SHEET 4 AF1 4 VAL Q 67 ASN Q 72 -1 N SER Q 70 O TYR Q 79 SHEET 1 AF2 7 ARG Q 11 VAL Q 12 0 SHEET 2 AF2 7 PHE Q 34 GLN Q 39 0 SHEET 3 AF2 7 LEU Q 45 ALA Q 52 -1 O GLU Q 46 N ARG Q 38 SHEET 4 AF2 7 VAL Q 57 TYR Q 59 -1 O ARG Q 58 N TYR Q 50 SHEET 5 AF2 7 ALA Q 88 CYS Q 96 -1 O TYR Q 91 N ILE Q 37 SHEET 6 AF2 7 SER Q 102 TRP Q 103 -1 O SER Q 102 N ARG Q 94 SHEET 7 AF2 7 ILE Q 107 VAL Q 111 -1 O VAL Q 109 N ALA Q 88 SHEET 1 AF3 4 MET R 4 SER R 7 0 SHEET 2 AF3 4 VAL R 19 THR R 25 -1 O THR R 22 N SER R 7 SHEET 3 AF3 4 ASP R 70 ILE R 75 -1 O TYR R 71 N CYS R 23 SHEET 4 AF3 4 PHE R 62 SER R 67 -1 N SER R 63 O THR R 74 SHEET 1 AF4 6 SER R 10 ALA R 13 0 SHEET 2 AF4 6 LEU R 33 GLN R 38 0 SHEET 3 AF4 6 LYS R 45 ILE R 48 -1 O LEU R 47 N TRP R 35 SHEET 4 AF4 6 GLY R 84 HIS R 90 -1 O THR R 85 N GLN R 38 SHEET 5 AF4 6 THR R 97 PHE R 98 -1 O THR R 97 N HIS R 90 SHEET 6 AF4 6 THR R 102 ILE R 106 -1 O VAL R 104 N GLY R 84 SHEET 1 AF5 4 LEU S 4 SER S 7 0 SHEET 2 AF5 4 LEU S 18 VAL S 24 -1 O THR S 21 N SER S 7 SHEET 3 AF5 4 GLN S 77 LEU S 82 -1 O LEU S 82 N LEU S 18 SHEET 4 AF5 4 VAL S 67 ASN S 72 -1 N SER S 70 O TYR S 79 SHEET 1 AF6 6 ARG S 11 VAL S 12 0 SHEET 2 AF6 6 PHE S 34 GLN S 39 0 SHEET 3 AF6 6 LEU S 45 ALA S 52 -1 O GLU S 46 N ARG S 38 SHEET 4 AF6 6 ALA S 88 CYS S 96 -1 O TYR S 91 N ILE S 37 SHEET 5 AF6 6 SER S 102 TRP S 103 -1 O SER S 102 N ARG S 94 SHEET 6 AF6 6 ILE S 107 VAL S 111 -1 O VAL S 109 N ALA S 88 SHEET 1 AF7 4 MET T 4 SER T 7 0 SHEET 2 AF7 4 VAL T 19 THR T 25 -1 O ARG T 24 N THR T 5 SHEET 3 AF7 4 ASP T 70 ILE T 75 -1 O LEU T 73 N ILE T 21 SHEET 4 AF7 4 PHE T 62 SER T 67 -1 N SER T 63 O THR T 74 SHEET 1 AF8 5 SER T 10 ALA T 13 0 SHEET 2 AF8 5 THR T 102 ILE T 106 1 O MET T 103 N LEU T 11 SHEET 3 AF8 5 GLY T 84 HIS T 90 -1 N TYR T 86 O THR T 102 SHEET 4 AF8 5 LEU T 33 GLN T 38 -1 N GLN T 38 O THR T 85 SHEET 5 AF8 5 LYS T 45 ILE T 48 -1 O LEU T 47 N TRP T 35 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 3 CYS A 54 CYS A 74 1555 1555 2.01 SSBOND 4 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 5 CYS A 126 CYS A 196 1555 1555 2.04 SSBOND 6 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 7 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 8 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 9 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 10 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 11 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 12 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 13 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 14 CYS E 22 CYS E 92 1555 1555 2.04 SSBOND 15 CYS F 23 CYS F 88 1555 1555 2.03 SSBOND 16 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 17 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 18 CYS C 126 CYS C 196 1555 1555 2.04 SSBOND 19 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 20 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 21 CYS C 228 CYS C 239 1555 1555 2.04 SSBOND 22 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 23 CYS C 378 CYS C 445 1555 1555 2.04 SSBOND 24 CYS C 385 CYS C 418 1555 1555 2.02 SSBOND 25 CYS C 501 CYS G 605 1555 1555 2.04 SSBOND 26 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 27 CYS J 22 CYS J 92 1555 1555 2.04 SSBOND 28 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 29 CYS D 54 CYS D 74 1555 1555 2.03 SSBOND 30 CYS D 119 CYS D 205 1555 1555 2.04 SSBOND 31 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 32 CYS D 228 CYS D 239 1555 1555 2.04 SSBOND 33 CYS D 296 CYS D 331 1555 1555 2.03 SSBOND 34 CYS D 378 CYS D 445 1555 1555 2.03 SSBOND 35 CYS D 385 CYS D 418 1555 1555 2.03 SSBOND 36 CYS D 501 CYS I 605 1555 1555 2.02 SSBOND 37 CYS I 598 CYS I 604 1555 1555 2.03 SSBOND 38 CYS K 22 CYS K 92 1555 1555 2.04 SSBOND 39 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 40 CYS O 22 CYS O 92 1555 1555 2.04 SSBOND 41 CYS P 23 CYS P 88 1555 1555 2.05 SSBOND 42 CYS Q 22 CYS Q 92 1555 1555 2.04 SSBOND 43 CYS R 23 CYS R 88 1555 1555 2.05 SSBOND 44 CYS S 22 CYS S 92 1555 1555 2.02 SSBOND 45 CYS T 23 CYS T 88 1555 1555 2.04 LINK ND2 ASN A 88 C1 NAG V 1 1555 1555 1.43 LINK ND2 ASN A 156 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG A 603 1555 1555 1.43 LINK ND2 ASN A 301 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 605 1555 1555 1.43 LINK ND2 ASN A 363 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 618 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG C 601 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG W 1 1555 1555 1.46 LINK ND2 ASN C 295 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 605 1555 1555 1.43 LINK ND2 ASN C 363 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN G 611 C1 NAG G 701 1555 1555 1.44 LINK ND2 ASN G 618 C1 NAG G 702 1555 1555 1.44 LINK ND2 ASN D 88 C1 NAG D 608 1555 1555 1.43 LINK ND2 ASN D 156 C1 NAG D 601 1555 1555 1.44 LINK ND2 ASN D 234 C1 NAG D 602 1555 1555 1.44 LINK ND2 ASN D 262 C1 NAG X 1 1555 1555 1.46 LINK ND2 ASN D 295 C1 NAG D 603 1555 1555 1.44 LINK ND2 ASN D 301 C1 NAG D 604 1555 1555 1.44 LINK ND2 ASN D 332 C1 NAG D 605 1555 1555 1.44 LINK ND2 ASN D 363 C1 NAG D 606 1555 1555 1.44 LINK ND2 ASN D 392 C1 NAG D 609 1555 1555 1.44 LINK ND2 ASN D 448 C1 NAG D 607 1555 1555 1.44 LINK ND2 ASN I 618 C1 NAG I 701 1555 1555 1.44 LINK ND2 ASN I 637 C1 NAG I 702 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.44 LINK O3 BMA U 3 C1 MAN U 4 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 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 O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -6.90 CISPEP 2 HIS L 94 PRO L 95 0 -0.95 CISPEP 3 SER P 7 PRO P 8 0 0.73 CISPEP 4 THR P 94 PRO P 95 0 -2.99 CISPEP 5 SER R 7 PRO R 8 0 1.50 CISPEP 6 THR R 94 PRO R 95 0 -1.28 CISPEP 7 SER T 7 PRO T 8 0 -2.68 CISPEP 8 THR T 94 PRO T 95 0 -0.62 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