HEADER VIRAL PROTEIN/IMMUNE SYSTEM 23-NOV-24 9EHM TITLE STRUCTURE OF HIV-1 BG505 SOSIP.664 ENV TRIMER IN COMPLEX WITH IOMAMIN5 TITLE 2 AND 10-1074 BROADLY NEUTRALIZING ANTIBODIES - CLASS II CAVEAT 9EHM NAG E 1 HAS WRONG CHIRALITY AT ATOM C1 NAG K 2 HAS WRONG CAVEAT 2 9EHM CHIRALITY AT ATOM C1 NAG N 1 HAS WRONG CHIRALITY AT ATOM C1 CAVEAT 3 9EHM RESIDUES GLY L 94 AND VAL L 96 THAT ARE NEXT TO EACH OTHER CAVEAT 4 9EHM IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED. COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 BG505 SOSIP GP120,ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: UNP RESIDUES 32-505; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HIV-1 BG505 SOSIP GP41; COMPND 9 CHAIN: D, E, F; COMPND 10 FRAGMENT: UNP RESIDUES 509-661; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: IOMAMIN5 FAB HEAVY CHAIN; COMPND 14 CHAIN: H, I; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: IOMAMIN5 FAB LIGHT CHAIN; COMPND 18 CHAIN: K, L; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: 10-1074 FAB HEAVY CHAIN; COMPND 22 CHAIN: M, N, O; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 6; COMPND 25 MOLECULE: 10-1074 FAB LIGHT CHAIN; COMPND 26 CHAIN: P, Q, R; COMPND 27 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 41 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, ENV, BNAB, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.A.DAM,Z.YANG,P.J.BJORKMAN REVDAT 1 21-MAY-25 9EHM 0 JRNL AUTH K.M.A.DAM,H.B.GRISTICK,Y.E.LI,Z.YANG,P.N.GNANAPRAGASAM, JRNL AUTH 2 A.P.WEST,M.S.SEAMAN,P.J.BJORKMAN JRNL TITL MAPPING ESSENTIAL SOMATIC HYPERMUTATIONS IN A CD4-BINDING JRNL TITL 2 SITE BNAB INFORMS HIV-1 VACCINE DESIGN JRNL REF CELL REP V. 44 15713 2025 JRNL REFN ESSN 2211-1247 JRNL DOI 10.1016/J.CELREP.2025.115713 REMARK 2 REMARK 2 RESOLUTION. 4.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : RELION, SERIALEM, RELION, UCSF REMARK 3 CHIMERAX, PHENIX, RELION, RELION, REMARK 3 RELION, RELION REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT 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) : 4.200 REMARK 3 NUMBER OF PARTICLES : 60493 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 9EHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1000287998. 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 : STRUCTURE OF HIV-1 BG505 REMARK 245 SOSIP.664 ENV TRIMER IN COMPLEX REMARK 245 WITH IOMAMIN5 AND 10-1074 REMARK 245 BROADLY NEUTRALIZING ANTIBODIES REMARK 245 - CLASS II REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 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 KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00 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) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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: HEXADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, K, L, REMARK 350 AND CHAINS: M, N, O, P, Q, R, G, J, 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, REMARK 350 AND CHAINS: m, n, o 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 MET A 6 REMARK 465 ASP A 7 REMARK 465 ALA A 8 REMARK 465 MET A 9 REMARK 465 LYS A 10 REMARK 465 ARG A 11 REMARK 465 GLY A 12 REMARK 465 LEU A 13 REMARK 465 CYS A 14 REMARK 465 CYS A 15 REMARK 465 VAL A 16 REMARK 465 LEU A 17 REMARK 465 LEU A 18 REMARK 465 LEU A 19 REMARK 465 CYS A 20 REMARK 465 GLY A 21 REMARK 465 ALA A 22 REMARK 465 VAL A 23 REMARK 465 PHE A 24 REMARK 465 VAL A 25 REMARK 465 SER A 26 REMARK 465 PRO A 27 REMARK 465 ALA A 28 REMARK 465 GLY A 29 REMARK 465 ALA A 30 REMARK 465 GLY A 31 REMARK 465 SER A 32 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 ASN A 145 REMARK 465 ILE A 146 REMARK 465 THR A 147 REMARK 465 ASP A 148 REMARK 465 ASP A 149 REMARK 465 MET A 150 REMARK 465 ARG A 151 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 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 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 MET B 6 REMARK 465 ASP B 7 REMARK 465 ALA B 8 REMARK 465 MET B 9 REMARK 465 LYS B 10 REMARK 465 ARG B 11 REMARK 465 GLY B 12 REMARK 465 LEU B 13 REMARK 465 CYS B 14 REMARK 465 CYS B 15 REMARK 465 VAL B 16 REMARK 465 LEU B 17 REMARK 465 LEU B 18 REMARK 465 LEU B 19 REMARK 465 CYS B 20 REMARK 465 GLY B 21 REMARK 465 ALA B 22 REMARK 465 VAL B 23 REMARK 465 PHE B 24 REMARK 465 VAL B 25 REMARK 465 SER B 26 REMARK 465 PRO B 27 REMARK 465 ALA B 28 REMARK 465 GLY B 29 REMARK 465 ALA B 30 REMARK 465 GLY B 31 REMARK 465 SER B 32 REMARK 465 THR B 147 REMARK 465 ASP B 148 REMARK 465 ASP B 149 REMARK 465 MET B 150 REMARK 465 ARG B 151 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 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 GLY B 459 REMARK 465 SER B 460 REMARK 465 THR B 461 REMARK 465 ASN B 462 REMARK 465 SER B 463 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 MET C 6 REMARK 465 ASP C 7 REMARK 465 ALA C 8 REMARK 465 MET C 9 REMARK 465 LYS C 10 REMARK 465 ARG C 11 REMARK 465 GLY C 12 REMARK 465 LEU C 13 REMARK 465 CYS C 14 REMARK 465 CYS C 15 REMARK 465 VAL C 16 REMARK 465 LEU C 17 REMARK 465 LEU C 18 REMARK 465 LEU C 19 REMARK 465 CYS C 20 REMARK 465 GLY C 21 REMARK 465 ALA C 22 REMARK 465 VAL C 23 REMARK 465 PHE C 24 REMARK 465 VAL C 25 REMARK 465 SER C 26 REMARK 465 PRO C 27 REMARK 465 ALA C 28 REMARK 465 GLY C 29 REMARK 465 ALA C 30 REMARK 465 GLY C 31 REMARK 465 SER C 32 REMARK 465 ASN C 33 REMARK 465 LEU C 34 REMARK 465 TRP C 35 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 MET C 150 REMARK 465 ARG C 151 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 SER C 185J REMARK 465 ASN C 185K 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 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 REMARK 465 ALA D 512 REMARK 465 VAL D 513 REMARK 465 GLY D 514 REMARK 465 ILE D 515 REMARK 465 GLY D 516 REMARK 465 ALA D 517 REMARK 465 VAL D 518 REMARK 465 PHE D 519 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 PRO D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 ALA E 512 REMARK 465 VAL E 513 REMARK 465 GLY E 514 REMARK 465 ILE E 515 REMARK 465 GLY E 516 REMARK 465 ALA E 517 REMARK 465 VAL E 518 REMARK 465 PHE E 519 REMARK 465 ILE E 548 REMARK 465 VAL E 549 REMARK 465 GLN E 550 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 PRO E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 LEU E 565 REMARK 465 LEU E 566 REMARK 465 LYS E 567 REMARK 465 LEU E 568 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 PHE F 519 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 GLN H 1 REMARK 465 GLN K 1 REMARK 465 GLN L 1 REMARK 465 TYR P 7 REMARK 465 TYR Q 7 REMARK 465 TYR R 7 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 OE1 GLN B 258 OG1 THR B 387 1.87 REMARK 500 NE2 GLN B 258 O THR B 372 1.88 REMARK 500 NE ARG A 503 O CYS D 605 2.09 REMARK 500 OD2 ASP L 27B OG SER L 90 2.13 REMARK 500 O GLY I 100H OH TYR L 36 2.14 REMARK 500 O LEU A 369 OG1 THR A 373 2.15 REMARK 500 ND2 ASN F 637 O5 NAG F 702 2.16 REMARK 500 O ILE E 595 ND2 ASN E 651 2.17 REMARK 500 NH2 ARG P 54 O PRO P 59 2.17 REMARK 500 OG1 THR A 37 O CYS D 604 2.17 REMARK 500 O GLY C 41 NE2 GLN F 540 2.18 REMARK 500 O THR A 278 NH2 ARG A 456 2.18 REMARK 500 OG SER C 199 O ILE C 430 2.19 REMARK 500 O GLN D 650 N GLU D 654 2.19 REMARK 500 OG SER Q 63 OG1 THR Q 74 2.19 REMARK 500 OD1 ASN O 60 OG SER O 62 2.19 REMARK 500 OG SER L 67 OG1 THR L 70 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLY L 94 C VAL L 96 N -0.225 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 296 CA - CB - SG ANGL. DEV. = 8.4 DEGREES REMARK 500 CYS C 385 CB - CA - C ANGL. DEV. = 7.7 DEGREES REMARK 500 LYS K 53 O - C - N ANGL. DEV. = -10.9 DEGREES REMARK 500 GLY L 94 O - C - N ANGL. DEV. = 11.1 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 LYS A 65 -76.93 -95.01 REMARK 500 VAL A 75 131.98 -38.88 REMARK 500 THR A 163 -167.52 -78.98 REMARK 500 CYS A 247 -179.03 -173.44 REMARK 500 THR A 248 -178.49 -68.51 REMARK 500 GLN A 258 -7.98 76.58 REMARK 500 ASN A 262 15.31 58.04 REMARK 500 HIS A 330 129.83 -174.18 REMARK 500 THR A 387 27.28 48.68 REMARK 500 ASN A 392 9.72 -153.06 REMARK 500 PRO A 493 4.48 -69.41 REMARK 500 THR B 132 -165.06 -124.19 REMARK 500 GLU B 153 -1.18 63.55 REMARK 500 THR B 257 -79.53 -111.91 REMARK 500 ARG B 327 -162.47 -120.08 REMARK 500 ASN B 392 16.42 -154.22 REMARK 500 SER B 397 -35.23 -133.02 REMARK 500 PRO B 493 0.20 -65.87 REMARK 500 PRO C 81 85.07 -68.81 REMARK 500 CYS C 126 98.12 -69.60 REMARK 500 GLN C 258 -8.88 72.97 REMARK 500 GLU C 267 99.18 -67.14 REMARK 500 THR C 387 43.35 39.44 REMARK 500 ASN C 392 -2.59 -150.30 REMARK 500 ILE C 396 -63.08 -90.19 REMARK 500 LYS C 502 116.51 -160.11 REMARK 500 LEU D 523 27.73 49.76 REMARK 500 ALA D 525 51.02 -90.44 REMARK 500 TRP D 571 -5.33 76.47 REMARK 500 LEU D 602 -9.10 69.98 REMARK 500 CYS D 604 146.57 -174.99 REMARK 500 GLN D 650 -50.67 -120.30 REMARK 500 TRP E 571 -5.11 69.29 REMARK 500 SER E 599 -1.28 64.99 REMARK 500 LEU E 602 -10.00 68.63 REMARK 500 ALA F 525 52.33 -94.23 REMARK 500 TRP F 571 -6.68 73.96 REMARK 500 LEU F 602 -12.36 73.42 REMARK 500 PRO F 609 -176.62 -69.96 REMARK 500 SER F 636 1.16 -67.04 REMARK 500 GLN F 653 -71.78 -128.86 REMARK 500 THR H 30 35.59 -98.47 REMARK 500 ARG H 54 -0.32 68.14 REMARK 500 MET I 48 -61.23 -90.04 REMARK 500 GLU K 50 -158.85 -144.25 REMARK 500 SER K 52 24.69 -153.95 REMARK 500 ASP K 82 3.70 -69.33 REMARK 500 LEU K 107 29.52 46.68 REMARK 500 GLU L 83 98.56 -68.56 REMARK 500 ASP L 93 -127.79 55.31 REMARK 500 REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG B 298 0.11 SIDE CHAIN REMARK 500 ARG B 304 0.14 SIDE CHAIN REMARK 500 ARG B 308 0.08 SIDE CHAIN REMARK 500 ARG K 54 0.08 SIDE CHAIN REMARK 500 ARG M 38 0.12 SIDE CHAIN REMARK 500 ARG Q 94 0.19 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 LYS K 53 -20.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48060 RELATED DB: EMDB REMARK 900 STRUCTURE OF HIV-1 BG505 SOSIP.664 ENV TRIMER IN COMPLEX WITH REMARK 900 IOMAMIN5 AND 10-1074 BROADLY NEUTRALIZING ANTIBODIES - CLASS II DBREF 9EHM A 6 32 PDB 9EHM 9EHM 6 32 DBREF 9EHM A 33 508 UNP Q2N0S5 Q2N0S5_HV1 32 505 DBREF 9EHM B 6 32 PDB 9EHM 9EHM 6 32 DBREF 9EHM B 33 508 UNP Q2N0S5 Q2N0S5_HV1 32 505 DBREF 9EHM C 6 32 PDB 9EHM 9EHM 6 32 DBREF 9EHM C 33 508 UNP Q2N0S5 Q2N0S5_HV1 32 505 DBREF 9EHM D 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 9EHM E 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 9EHM F 512 664 UNP Q2N0S5 Q2N0S5_9HIV1 509 661 DBREF 9EHM H 1 115 PDB 9EHM 9EHM 1 115 DBREF 9EHM I 1 115 PDB 9EHM 9EHM 1 115 DBREF 9EHM K 1 110 PDB 9EHM 9EHM 1 110 DBREF 9EHM L 1 110 PDB 9EHM 9EHM 1 110 DBREF 9EHM M 1 115 PDB 9EHM 9EHM 1 115 DBREF 9EHM N 1 115 PDB 9EHM 9EHM 1 115 DBREF 9EHM O 1 115 PDB 9EHM 9EHM 1 115 DBREF 9EHM P 7 110 PDB 9EHM 9EHM 7 110 DBREF 9EHM Q 7 110 PDB 9EHM 9EHM 7 110 DBREF 9EHM R 7 110 PDB 9EHM 9EHM 7 110 SEQADV 9EHM ASN A 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9EHM CYS A 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9EHM ARG A 509 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG A 510 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG A 511 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG A 512 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG A 513 UNP Q2N0S5 INSERTION SEQADV 9EHM ASN B 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9EHM CYS B 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9EHM ARG B 509 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG B 510 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG B 511 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG B 512 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG B 513 UNP Q2N0S5 INSERTION SEQADV 9EHM ASN C 332 UNP Q2N0S5 THR 330 ENGINEERED MUTATION SEQADV 9EHM CYS C 501 UNP Q2N0S5 ALA 498 ENGINEERED MUTATION SEQADV 9EHM ARG C 509 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG C 510 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG C 511 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG C 512 UNP Q2N0S5 INSERTION SEQADV 9EHM ARG C 513 UNP Q2N0S5 INSERTION SEQADV 9EHM PRO D 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 9EHM CYS D 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 9EHM PRO E 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 9EHM CYS E 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQADV 9EHM PRO F 559 UNP Q2N0S5 ILE 556 ENGINEERED MUTATION SEQADV 9EHM CYS F 605 UNP Q2N0S5 THR 602 ENGINEERED MUTATION SEQRES 1 A 506 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 A 506 LEU CYS GLY ALA VAL PHE VAL SER PRO ALA GLY ALA GLY SEQRES 3 A 506 SER ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 4 A 506 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 5 A 506 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 6 A 506 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 7 A 506 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 8 A 506 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 9 A 506 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 10 A 506 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 11 A 506 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 12 A 506 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 13 A 506 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 14 A 506 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 15 A 506 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 A 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 A 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 A 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 A 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 A 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 A 506 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 22 A 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 23 A 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 24 A 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 25 A 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 A 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 A 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 A 506 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 29 A 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 A 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 A 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 A 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 A 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 A 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 A 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 A 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 A 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 A 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 A 506 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 506 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 B 506 LEU CYS GLY ALA VAL PHE VAL SER PRO ALA GLY ALA GLY SEQRES 3 B 506 SER ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 4 B 506 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 5 B 506 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 6 B 506 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 7 B 506 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 8 B 506 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 9 B 506 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 10 B 506 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 11 B 506 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 12 B 506 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 13 B 506 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 14 B 506 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 15 B 506 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 B 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 B 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 B 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 B 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 B 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 B 506 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 22 B 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 23 B 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 24 B 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 25 B 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 B 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 B 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 B 506 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 29 B 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 B 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 B 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 B 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 B 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 B 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 B 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 B 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 B 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 B 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 B 506 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 C 506 MET ASP ALA MET LYS ARG GLY LEU CYS CYS VAL LEU LEU SEQRES 2 C 506 LEU CYS GLY ALA VAL PHE VAL SER PRO ALA GLY ALA GLY SEQRES 3 C 506 SER ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 4 C 506 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 5 C 506 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 6 C 506 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 7 C 506 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 8 C 506 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 9 C 506 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 10 C 506 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 11 C 506 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 12 C 506 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 13 C 506 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 14 C 506 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 15 C 506 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER ALA SEQRES 16 C 506 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 17 C 506 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 18 C 506 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 19 C 506 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 20 C 506 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 21 C 506 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE THR SEQRES 22 C 506 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 23 C 506 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 24 C 506 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 25 C 506 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 26 C 506 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 27 C 506 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 28 C 506 ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU GLU SEQRES 29 C 506 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 30 C 506 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 31 C 506 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 32 C 506 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 33 C 506 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 34 C 506 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 35 C 506 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 36 C 506 SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 37 C 506 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 38 C 506 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 39 C 506 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 E 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 E 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 E 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 E 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 E 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 128 GLN VAL GLN LEU VAL GLN SER GLY ALA GLN VAL LYS LYS SEQRES 2 H 128 PRO GLY ALA SER VAL THR VAL SER CYS THR ALA SER GLY SEQRES 3 H 128 TYR THR PHE THR GLY TYR HIS MET HIS TRP VAL ARG GLN SEQRES 4 H 128 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 128 PRO PHE ARG GLY ALA VAL LYS TYR ALA GLN LYS PHE ARG SEQRES 6 H 128 GLY ARG VAL SER MET THR ARG ASP THR SER ILE GLU ILE SEQRES 7 H 128 PHE TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 128 ALA VAL TYR TYR CYS ALA ARG GLU MET PHE ASP SER SER SEQRES 9 H 128 ALA ASP TRP SER PRO TRP ARG GLY MET VAL ALA TRP GLY SEQRES 10 H 128 GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 1 I 128 GLN VAL GLN LEU VAL GLN SER GLY ALA GLN VAL LYS LYS SEQRES 2 I 128 PRO GLY ALA SER VAL THR VAL SER CYS THR ALA SER GLY SEQRES 3 I 128 TYR THR PHE THR GLY TYR HIS MET HIS TRP VAL ARG GLN SEQRES 4 I 128 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 I 128 PRO PHE ARG GLY ALA VAL LYS TYR ALA GLN LYS PHE ARG SEQRES 6 I 128 GLY ARG VAL SER MET THR ARG ASP THR SER ILE GLU ILE SEQRES 7 I 128 PHE TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 I 128 ALA VAL TYR TYR CYS ALA ARG GLU MET PHE ASP SER SER SEQRES 9 I 128 ALA ASP TRP SER PRO TRP ARG GLY MET VAL ALA TRP GLY SEQRES 10 I 128 GLN GLY THR LEU VAL THR VAL SER SER ALA SER SEQRES 1 K 111 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 K 111 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY SER SER SEQRES 3 K 111 ARG ASP VAL GLY GLY PHE ASP LEU VAL SER TRP TYR GLN SEQRES 4 K 111 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLU SEQRES 5 K 111 VAL SER LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 K 111 ALA SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 K 111 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS TYR SEQRES 8 K 111 SER TYR ALA ASP GLY VAL ALA PHE GLY GLY GLY THR LYS SEQRES 9 K 111 LEU THR VAL LEU GLY GLN PRO SEQRES 1 L 111 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 111 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY SER SER SEQRES 3 L 111 ARG ASP VAL GLY GLY PHE ASP LEU VAL SER TRP TYR GLN SEQRES 4 L 111 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLU SEQRES 5 L 111 VAL SER LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 111 ALA SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 111 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS TYR SEQRES 8 L 111 SER TYR ALA ASP GLY VAL ALA PHE GLY GLY GLY THR LYS SEQRES 9 L 111 LEU THR VAL LEU GLY GLN PRO SEQRES 1 M 134 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 134 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 M 134 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 M 134 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 M 134 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 M 134 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 M 134 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 M 134 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 M 134 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 M 134 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 M 134 SER SER ALA SER SEQRES 1 N 134 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 N 134 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 N 134 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 N 134 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 N 134 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 N 134 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 N 134 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 N 134 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 N 134 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 N 134 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 N 134 SER SER ALA SER SEQRES 1 O 134 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 O 134 PRO SER GLU THR LEU SER VAL THR CYS SER VAL SER GLY SEQRES 3 O 134 ASP SER MET ASN ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 O 134 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 O 134 ASP ARG GLU SER ALA THR TYR ASN PRO SER LEU ASN SER SEQRES 6 O 134 ARG VAL VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 O 134 SER LEU LYS LEU ASN SER VAL THR PRO ALA ASP THR ALA SEQRES 8 O 134 VAL TYR TYR CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 O 134 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 O 134 SER MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 O 134 SER SER ALA SER SEQRES 1 P 110 TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR ALA SEQRES 2 P 110 ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG ALA SEQRES 3 P 110 VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO ILE SEQRES 4 P 110 LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY ILE SEQRES 5 P 110 PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE GLY SEQRES 6 P 110 THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA GLY SEQRES 7 P 110 ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER ARG SEQRES 8 P 110 SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG LEU SEQRES 9 P 110 THR VAL LEU GLY GLN PRO SEQRES 1 Q 110 TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR ALA SEQRES 2 Q 110 ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG ALA SEQRES 3 Q 110 VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO ILE SEQRES 4 Q 110 LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY ILE SEQRES 5 Q 110 PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE GLY SEQRES 6 Q 110 THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA GLY SEQRES 7 Q 110 ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER ARG SEQRES 8 Q 110 SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG LEU SEQRES 9 Q 110 THR VAL LEU GLY GLN PRO SEQRES 1 R 110 TYR VAL ARG PRO LEU SER VAL ALA LEU GLY GLU THR ALA SEQRES 2 R 110 ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG ALA SEQRES 3 R 110 VAL GLN TRP TYR GLN HIS ARG PRO GLY GLN ALA PRO ILE SEQRES 4 R 110 LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY ILE SEQRES 5 R 110 PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE GLY SEQRES 6 R 110 THR ARG ALA THR LEU THR ILE SER GLY VAL GLU ALA GLY SEQRES 7 R 110 ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER ARG SEQRES 8 R 110 SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG LEU SEQRES 9 R 110 THR VAL LEU GLY GLN PRO HET NAG G 1 14 HET NAG G 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET MAN T 3 11 HET BMA T 4 11 HET NAG U 1 14 HET NAG U 2 14 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 BMA W 4 11 HET NAG X 1 14 HET NAG X 2 14 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET MAN Z 4 11 HET NAG a 1 14 HET NAG a 2 14 HET MAN a 3 11 HET BMA a 4 11 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET MAN d 4 11 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 14 HET MAN g 3 11 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET MAN i 4 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET BMA j 4 11 HET NAG k 1 14 HET NAG k 2 14 HET MAN k 3 11 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET NAG n 1 14 HET NAG n 2 14 HET NAG o 1 14 HET NAG o 2 14 HET BMA o 3 11 HET MAN o 4 11 HET BMA o 5 11 HET BMA o 6 11 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG A 609 14 HET NAG 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 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 D 701 14 HET NAG D 702 14 HET NAG E 701 14 HET NAG E 702 14 HET NAG F 701 14 HET NAG F 702 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM BMA BETA-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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 17 NAG 79(C8 H15 N O6) FORMUL 20 MAN 8(C6 H12 O6) FORMUL 20 BMA 12(C6 H12 O6) HELIX 1 AA1 ASN A 98 LYS A 117 1 20 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 TYR A 177 LEU A 179 5 3 HELIX 4 AA4 LYS A 335 ARG A 350 1 16 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 ASN A 425 ARG A 429 5 5 HELIX 7 AA7 MET A 475 SER A 481 1 7 HELIX 8 AA8 ASP B 57 THR B 63 5 7 HELIX 9 AA9 ASN B 99 LYS B 117 1 19 HELIX 10 AB1 LEU B 122 CYS B 126 5 5 HELIX 11 AB2 TYR B 177 LEU B 179 5 3 HELIX 12 AB3 LYS B 335 PHE B 353 1 19 HELIX 13 AB4 ASP B 368 THR B 373 1 6 HELIX 14 AB5 ASN B 425 ARG B 429 5 5 HELIX 15 AB6 MET B 475 SER B 481 1 7 HELIX 16 AB7 GLU B 482 TYR B 484 5 3 HELIX 17 AB8 ASN C 99 LYS C 117 1 19 HELIX 18 AB9 LEU C 122 CYS C 126 5 5 HELIX 19 AC1 TYR C 177 LEU C 179 5 3 HELIX 20 AC2 LYS C 335 ARG C 350 1 16 HELIX 21 AC3 ASP C 368 THR C 373 1 6 HELIX 22 AC4 ASN C 425 ARG C 429 5 5 HELIX 23 AC5 MET C 475 SER C 481 1 7 HELIX 24 AC6 THR D 529 SER D 534 1 6 HELIX 25 AC7 THR D 536 ASN D 543 1 8 HELIX 26 AC8 GLY D 572 TRP D 596 1 25 HELIX 27 AC9 LEU D 619 ASP D 624 1 6 HELIX 28 AD1 THR D 627 SER D 636 1 10 HELIX 29 AD2 TYR D 638 GLN D 652 1 15 HELIX 30 AD3 GLN D 653 LEU D 663 1 11 HELIX 31 AD4 THR E 529 SER E 534 1 6 HELIX 32 AD5 THR E 536 ARG E 542 1 7 HELIX 33 AD6 ASN E 543 LEU E 545 5 3 HELIX 34 AD7 GLY E 572 TRP E 596 1 25 HELIX 35 AD8 ASN E 611 ASN E 616 1 6 HELIX 36 AD9 ASN E 618 ASP E 624 1 7 HELIX 37 AE1 THR E 627 SER E 636 1 10 HELIX 38 AE2 TYR E 638 ASP E 664 1 27 HELIX 39 AE3 THR F 529 SER F 534 1 6 HELIX 40 AE4 THR F 536 ASN F 543 1 8 HELIX 41 AE5 GLY F 572 TRP F 596 1 25 HELIX 42 AE6 LEU F 619 ASP F 624 1 6 HELIX 43 AE7 THR F 627 GLU F 634 1 8 HELIX 44 AE8 TYR F 638 GLN F 652 1 15 HELIX 45 AE9 GLN F 653 ASP F 664 1 12 HELIX 46 AF1 THR H 28 TYR H 32 5 5 HELIX 47 AF2 GLN H 61 ARG H 64 5 4 HELIX 48 AF3 ARG H 83 THR H 87 5 5 HELIX 49 AF4 TRP H 100C ARG H 100G 5 5 HELIX 50 AF5 GLN I 61 ARG I 64 5 4 HELIX 51 AF6 ARG I 83 THR I 87 5 5 HELIX 52 AF7 TRP I 100C ARG I 100G 5 5 HELIX 53 AF8 GLN K 79 GLU K 83 5 5 HELIX 54 AF9 GLN L 79 GLU L 83 5 5 HELIX 55 AG1 THR M 83 THR M 87 5 5 HELIX 56 AG2 ASN N 60 ASN N 64 5 5 HELIX 57 AG3 ASN O 60 ASN O 64 5 5 HELIX 58 AG4 THR O 83 THR O 87 5 5 HELIX 59 AG5 VAL O 100D GLY O 100H 5 5 HELIX 60 AG6 GLU P 79 GLU P 83 5 5 HELIX 61 AG7 GLU Q 79 GLU Q 83 5 5 SHEET 1 AA1 2 TRP A 35 TYR A 40 0 SHEET 2 AA1 2 LEU A 494 THR A 499 -1 O THR A 499 N TRP A 35 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 SER A 56 0 SHEET 2 AA3 2 ILE A 215 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 ASN A 67 VAL A 68 0 SHEET 2 AA4 2 VAL A 208 SER A 209 1 O SER A 209 N ASN A 67 SHEET 1 AA5 2 GLU A 92 ASN A 94 0 SHEET 2 AA5 2 THR A 236 PRO A 238 -1 O GLY A 237 N PHE A 93 SHEET 1 AA6 5 LYS A 169 PHE A 176 0 SHEET 2 AA6 5 LYS A 155 THR A 162 -1 N LYS A 155 O PHE A 176 SHEET 3 AA6 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AA6 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA6 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA7 3 ALA A 200 GLN A 203 0 SHEET 2 AA7 3 GLN A 432 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA7 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA8 6 MET A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 284 ASN A 302 -1 O LEU A 285 N ARG A 273 SHEET 3 AA8 6 HIS A 330 SER A 334 -1 O ASN A 332 N ASN A 295 SHEET 4 AA8 6 SER A 413 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 5 AA8 6 PHE A 382 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 6 AA8 6 HIS A 374 ASN A 377 -1 N HIS A 374 O CYS A 385 SHEET 1 AA9 6 MET A 271 ARG A 273 0 SHEET 2 AA9 6 ILE A 284 ASN A 302 -1 O LEU A 285 N ARG A 273 SHEET 3 AA9 6 GLY A 441 ARG A 456 -1 O SER A 447 N ILE A 294 SHEET 4 AA9 6 THR A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA9 6 ILE A 358 PHE A 361 1 N ILE A 358 O GLU A 466 SHEET 6 AA9 6 THR A 394 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AB1 2 ARG A 304 ARG A 308 0 SHEET 2 AB1 2 ALA A 316 THR A 320 -1 O ALA A 319 N LYS A 305 SHEET 1 AB2 2 TRP B 35 TYR B 40 0 SHEET 2 AB2 2 LEU B 494 THR B 499 -1 O THR B 499 N TRP B 35 SHEET 1 AB3 5 TRP B 45 ASP B 47 0 SHEET 2 AB3 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AB3 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AB3 5 VAL B 242 VAL B 245 -1 O SER B 243 N LYS B 227 SHEET 5 AB3 5 ILE B 84 HIS B 85 -1 N ILE B 84 O THR B 244 SHEET 1 AB4 3 VAL B 75 PRO B 76 0 SHEET 2 AB4 3 PHE B 53 SER B 56 1 N SER B 56 O VAL B 75 SHEET 3 AB4 3 TYR B 217 CYS B 218 -1 O CYS B 218 N PHE B 53 SHEET 1 AB5 2 GLU B 91 ASN B 94 0 SHEET 2 AB5 2 THR B 236 CYS B 239 -1 O CYS B 239 N GLU B 91 SHEET 1 AB6 5 LYS B 169 PHE B 176 0 SHEET 2 AB6 5 LYS B 155 THR B 162 -1 N LYS B 155 O PHE B 176 SHEET 3 AB6 5 LEU B 129 ASN B 133 -1 N THR B 132 O ASN B 156 SHEET 4 AB6 5 GLU B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AB6 5 VAL B 181 GLN B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AB7 3 ALA B 200 GLN B 203 0 SHEET 2 AB7 3 GLN B 432 TYR B 435 1 O TYR B 435 N THR B 202 SHEET 3 AB7 3 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AB8 4 LEU B 259 LEU B 260 0 SHEET 2 AB8 4 GLY B 451 ARG B 456 -1 O GLY B 451 N LEU B 260 SHEET 3 AB8 4 ASN B 283 GLN B 287 -1 N VAL B 286 O LEU B 452 SHEET 4 AB8 4 MET B 271 ARG B 273 -1 N ARG B 273 O LEU B 285 SHEET 1 AB9 5 LEU B 259 LEU B 260 0 SHEET 2 AB9 5 GLY B 451 ARG B 456 -1 O GLY B 451 N LEU B 260 SHEET 3 AB9 5 THR B 465 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 4 AB9 5 ILE B 358 PHE B 361 1 N ILE B 358 O GLU B 466 SHEET 5 AB9 5 THR B 394 TRP B 395 -1 O TRP B 395 N ILE B 359 SHEET 1 AC1 6 HIS B 374 ASN B 377 0 SHEET 2 AC1 6 PHE B 382 CYS B 385 -1 O CYS B 385 N HIS B 374 SHEET 3 AC1 6 SER B 413 ILE B 420 -1 O ARG B 419 N TYR B 384 SHEET 4 AC1 6 HIS B 330 SER B 334 -1 N VAL B 333 O ILE B 414 SHEET 5 AC1 6 VAL B 292 ARG B 298 -1 N THR B 297 O HIS B 330 SHEET 6 AC1 6 ILE B 443 ILE B 449 -1 O ILE B 443 N ARG B 298 SHEET 1 AC2 2 ARG B 304 GLY B 312 0 SHEET 2 AC2 2 GLN B 315 THR B 320 -1 O PHE B 317 N ILE B 307 SHEET 1 AC3 2 THR C 37 TYR C 40 0 SHEET 2 AC3 2 LEU C 494 ALA C 497 -1 O GLY C 495 N TYR C 39 SHEET 1 AC4 5 TRP C 45 ASP C 47 0 SHEET 2 AC4 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AC4 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AC4 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AC4 5 GLU C 83 ILE C 84 -1 N ILE C 84 O THR C 244 SHEET 1 AC5 2 PHE C 53 ALA C 55 0 SHEET 2 AC5 2 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AC6 2 GLU C 92 ASN C 94 0 SHEET 2 AC6 2 THR C 236 PRO C 238 -1 O GLY C 237 N PHE C 93 SHEET 1 AC7 5 LYS C 169 PHE C 176 0 SHEET 2 AC7 5 LYS C 155 THR C 162 -1 N LYS C 155 O PHE C 176 SHEET 3 AC7 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AC7 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AC7 5 VAL C 181 ILE C 184 -1 N ILE C 184 O GLU C 190 SHEET 1 AC8 9 HIS C 374 ASN C 377 0 SHEET 2 AC8 9 PHE C 382 CYS C 385 -1 O PHE C 383 N PHE C 376 SHEET 3 AC8 9 SER C 413 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 4 AC8 9 ALA C 329 SER C 334 -1 N VAL C 333 O ILE C 414 SHEET 5 AC8 9 ILE C 284 ASN C 302 -1 N ASN C 295 O ASN C 332 SHEET 6 AC8 9 GLY C 441 ARG C 456 -1 O THR C 450 N PHE C 288 SHEET 7 AC8 9 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 8 AC8 9 ILE C 358 PHE C 361 1 N ILE C 358 O GLU C 466 SHEET 9 AC8 9 THR C 394 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AC9 2 ARG C 304 ARG C 308 0 SHEET 2 AC9 2 ALA C 316 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AD1 2 ILE C 423 ILE C 424 0 SHEET 2 AD1 2 MET C 434 TYR C 435 -1 O MET C 434 N ILE C 424 SHEET 1 AD2 6 GLN H 10 LYS H 12 0 SHEET 2 AD2 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AD2 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AD2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AD2 6 LEU H 45 ASN H 52 -1 O MET H 48 N TRP H 36 SHEET 6 AD2 6 ALA H 56 TYR H 59 -1 O ALA H 56 N ASN H 52 SHEET 1 AD3 4 GLN H 10 LYS H 12 0 SHEET 2 AD3 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AD3 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AD3 4 ALA H 102 TRP H 103 -1 O ALA H 102 N ARG H 94 SHEET 1 AD4 3 VAL H 18 THR H 23 0 SHEET 2 AD4 3 ILE H 77 LEU H 82 -1 O LEU H 82 N VAL H 18 SHEET 3 AD4 3 VAL H 67 ASP H 72 -1 N SER H 68 O GLU H 81 SHEET 1 AD5 4 VAL I 5 GLN I 6 0 SHEET 2 AD5 4 SER I 17 THR I 23 -1 O THR I 23 N VAL I 5 SHEET 3 AD5 4 ILE I 77 SER I 82A-1 O LEU I 82 N VAL I 18 SHEET 4 AD5 4 VAL I 67 ASP I 72 -1 N SER I 68 O GLU I 81 SHEET 1 AD6 6 GLN I 10 LYS I 12 0 SHEET 2 AD6 6 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AD6 6 ALA I 88 ARG I 94 -1 N ALA I 88 O VAL I 109 SHEET 4 AD6 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 AD6 6 LEU I 45 ASN I 52 -1 O MET I 48 N TRP I 36 SHEET 6 AD6 6 ALA I 56 TYR I 59 -1 O ALA I 56 N ASN I 52 SHEET 1 AD7 4 GLN I 10 LYS I 12 0 SHEET 2 AD7 4 THR I 107 VAL I 111 1 O THR I 110 N LYS I 12 SHEET 3 AD7 4 ALA I 88 ARG I 94 -1 N ALA I 88 O VAL I 109 SHEET 4 AD7 4 ALA I 102 TRP I 103 -1 O ALA I 102 N ARG I 94 SHEET 1 AD8 3 ILE K 19 THR K 24 0 SHEET 2 AD8 3 THR K 70 ILE K 75 -1 O LEU K 73 N ILE K 21 SHEET 3 AD8 3 PHE K 62 SER K 67 -1 N SER K 65 O SER K 72 SHEET 1 AD9 4 LYS K 45 ILE K 48 0 SHEET 2 AD9 4 SER K 34 GLN K 38 -1 N TRP K 35 O MET K 47 SHEET 3 AD9 4 ASP K 85 TYR K 91 -1 O TYR K 89 N SER K 34 SHEET 4 AD9 4 VAL K 96 PHE K 98 -1 O ALA K 97 N SER K 90 SHEET 1 AE1 5 SER L 9 VAL L 11 0 SHEET 2 AE1 5 THR L 102 LEU L 104 1 O LYS L 103 N VAL L 11 SHEET 3 AE1 5 ASP L 85 TYR L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AE1 5 SER L 34 GLN L 38 -1 N SER L 34 O TYR L 89 SHEET 5 AE1 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AE2 3 ILE L 19 THR L 24 0 SHEET 2 AE2 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AE2 3 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AE3 2 LEU M 11 VAL M 12 0 SHEET 2 AE3 2 THR M 110 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 1 AE4 3 LEU M 18 VAL M 20 0 SHEET 2 AE4 3 GLN M 77 LEU M 82 -1 O LEU M 82 N LEU M 18 SHEET 3 AE4 3 VAL M 67 ASP M 72 -1 N VAL M 68 O LYS M 81 SHEET 1 AE5 4 LEU M 45 ILE M 51 0 SHEET 2 AE5 4 TYR M 33 GLN M 39 -1 N ARG M 38 O GLU M 46 SHEET 3 AE5 4 VAL M 89 ARG M 100 -1 O VAL M 89 N GLN M 39 SHEET 4 AE5 4 PHE M 100K SER M 100O-1 O SER M 100O N ARG M 96 SHEET 1 AE6 2 LEU N 11 VAL N 12 0 SHEET 2 AE6 2 THR N 110 VAL N 111 1 O THR N 110 N VAL N 12 SHEET 1 AE7 3 LEU N 18 SER N 23 0 SHEET 2 AE7 3 GLN N 77 LEU N 82 -1 O LEU N 82 N LEU N 18 SHEET 3 AE7 3 VAL N 68 ASP N 72 -1 N VAL N 68 O LYS N 81 SHEET 1 AE8 4 LEU N 45 ILE N 51 0 SHEET 2 AE8 4 TYR N 33 GLN N 39 -1 N ARG N 38 O GLU N 46 SHEET 3 AE8 4 VAL N 89 ILE N 100A-1 O ALA N 93 N THR N 35 SHEET 4 AE8 4 PHE N 100J SER N 100O-1 O SER N 100O N ARG N 96 SHEET 1 AE9 4 LEU N 45 ILE N 51 0 SHEET 2 AE9 4 TYR N 33 GLN N 39 -1 N ARG N 38 O GLU N 46 SHEET 3 AE9 4 VAL N 89 ILE N 100A-1 O ALA N 93 N THR N 35 SHEET 4 AE9 4 THR N 107 THR N 108 -1 O THR N 107 N TYR N 90 SHEET 1 AF1 6 LEU O 11 VAL O 12 0 SHEET 2 AF1 6 THR O 107 VAL O 111 1 O THR O 110 N VAL O 12 SHEET 3 AF1 6 ALA O 88 ILE O 100A-1 N ALA O 88 O VAL O 109 SHEET 4 AF1 6 TYR O 33 GLN O 39 -1 N ILE O 37 O TYR O 91 SHEET 5 AF1 6 GLY O 49 ILE O 51 -1 O GLY O 49 N TRP O 36 SHEET 6 AF1 6 ALA O 57 THR O 58 -1 O THR O 58 N TYR O 50 SHEET 1 AF2 4 LEU O 11 VAL O 12 0 SHEET 2 AF2 4 THR O 107 VAL O 111 1 O THR O 110 N VAL O 12 SHEET 3 AF2 4 ALA O 88 ILE O 100A-1 N ALA O 88 O VAL O 109 SHEET 4 AF2 4 PHE O 100J SER O 100O-1 O SER O 100O N ARG O 96 SHEET 1 AF3 2 VAL O 68 ASP O 72 0 SHEET 2 AF3 2 GLN O 77 LYS O 81 -1 O LYS O 81 N VAL O 68 SHEET 1 AF4 5 ARG P 9 LEU P 11 0 SHEET 2 AF4 5 THR P 102 LEU P 104 1 O ARG P 103 N ARG P 9 SHEET 3 AF4 5 ASP P 85 TRP P 91 -1 N TYR P 86 O THR P 102 SHEET 4 AF4 5 ALA P 32 HIS P 38 -1 N HIS P 38 O ASP P 85 SHEET 5 AF4 5 PRO P 44 TYR P 49 -1 O LEU P 47 N TRP P 35 SHEET 1 AF5 3 THR P 18 SER P 22 0 SHEET 2 AF5 3 THR P 72 SER P 76 -1 O ILE P 75 N ALA P 19 SHEET 3 AF5 3 PHE P 62 SER P 63 -1 N SER P 63 O THR P 74 SHEET 1 AF6 5 ARG Q 9 ALA Q 14 0 SHEET 2 AF6 5 THR Q 102 LEU Q 107 1 O THR Q 105 N LEU Q 11 SHEET 3 AF6 5 ASP Q 85 MET Q 90 -1 N TYR Q 86 O THR Q 102 SHEET 4 AF6 5 VAL Q 33 HIS Q 38 -1 N GLN Q 34 O HIS Q 89 SHEET 5 AF6 5 ILE Q 45 ILE Q 48 -1 O LEU Q 47 N TRP Q 35 SHEET 1 AF7 3 THR Q 18 SER Q 22 0 SHEET 2 AF7 3 THR Q 72 SER Q 76 -1 O LEU Q 73 N ILE Q 21 SHEET 3 AF7 3 PHE Q 62 SER Q 63 -1 N SER Q 63 O THR Q 74 SHEET 1 AF8 3 ALA R 19 SER R 22 0 SHEET 2 AF8 3 THR R 72 ILE R 75 -1 O ILE R 75 N ALA R 19 SHEET 3 AF8 3 PHE R 62 SER R 63 -1 N SER R 63 O THR R 74 SHEET 1 AF9 3 ALA R 32 HIS R 38 0 SHEET 2 AF9 3 ASP R 85 TRP R 91 -1 O HIS R 89 N GLN R 34 SHEET 3 AF9 3 ALA R 101 ARG R 103 -1 O THR R 102 N TYR R 86 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.04 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS A 501 CYS D 605 1555 1555 2.03 SSBOND 11 CYS B 54 CYS B 74 1555 1555 2.03 SSBOND 12 CYS B 119 CYS B 205 1555 1555 2.04 SSBOND 13 CYS B 126 CYS B 196 1555 1555 2.03 SSBOND 14 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 15 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 16 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 17 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 18 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 19 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 20 CYS B 501 CYS E 605 1555 1555 2.03 SSBOND 21 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 22 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 23 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 24 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 25 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 26 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 27 CYS C 331 CYS C 385 1555 1555 2.05 SSBOND 28 CYS C 331 CYS C 418 1555 1555 2.03 SSBOND 29 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 30 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 31 CYS C 501 CYS F 605 1555 1555 2.03 SSBOND 32 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 33 CYS E 598 CYS E 604 1555 1555 2.03 SSBOND 34 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 35 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 36 CYS I 22 CYS I 92 1555 1555 2.03 SSBOND 37 CYS K 23 CYS K 88 1555 1555 2.03 SSBOND 38 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 39 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 40 CYS N 22 CYS N 92 1555 1555 2.03 SSBOND 41 CYS O 22 CYS O 92 1555 1555 2.03 SSBOND 42 CYS P 23 CYS P 88 1555 1555 2.03 SSBOND 43 CYS Q 23 CYS Q 88 1555 1555 2.03 SSBOND 44 CYS R 23 CYS R 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 602 1555 1555 1.43 LINK ND2 ASN A 133 C1 NAG A 603 1555 1555 1.43 LINK ND2 ASN A 156 C1 NAG G 1 1555 1555 1.43 LINK ND2 ASN A 160 C1 NAG J 1 1555 1555 1.43 LINK ND2 ASN A 197 C1 NAG S 1 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG A 604 1555 1555 1.43 LINK ND2 ASN A 262 C1 NAG T 1 1555 1555 1.43 LINK ND2 ASN A 276 C1 NAG A 605 1555 1555 1.43 LINK ND2 ASN A 295 C1 NAG A 606 1555 1555 1.43 LINK ND2 ASN A 301 C1 NAG U 1 1555 1555 1.43 LINK ND2 ASN A 332 C1 NAG W 1 1555 1555 1.43 LINK ND2 ASN A 339 C1 NAG A 601 1555 1555 1.43 LINK ND2 ASN A 363 C1 NAG A 609 1555 1555 1.43 LINK ND2 ASN A 386 C1 NAG V 1 1555 1555 1.43 LINK ND2 ASN A 392 C1 NAG A 607 1555 1555 1.43 LINK ND2 ASN A 448 C1 NAG A 608 1555 1555 1.43 LINK ND2 ASN B 88 C1 NAG B 602 1555 1555 1.43 LINK ND2 ASN B 133 C1 NAG B 607 1555 1555 1.43 LINK ND2 ASN B 156 C1 NAG X 1 1555 1555 1.43 LINK ND2 ASN B 160 C1 NAG Y 1 1555 1555 1.43 LINK ND2 ASN B 197 C1 NAG Z 1 1555 1555 1.43 LINK ND2 ASN B 234 C1 NAG B 603 1555 1555 1.43 LINK ND2 ASN B 262 C1 NAG a 1 1555 1555 1.43 LINK ND2 ASN B 276 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN B 295 C1 NAG B 604 1555 1555 1.44 LINK ND2 ASN B 301 C1 NAG c 1 1555 1555 1.43 LINK ND2 ASN B 332 C1 NAG d 1 1555 1555 1.43 LINK ND2 ASN B 339 C1 NAG B 601 1555 1555 1.43 LINK ND2 ASN B 363 C1 NAG f 1 1555 1555 1.43 LINK ND2 ASN B 386 C1 NAG e 1 1555 1555 1.43 LINK ND2 ASN B 392 C1 NAG B 605 1555 1555 1.43 LINK ND2 ASN B 448 C1 NAG B 606 1555 1555 1.43 LINK ND2 ASN C 88 C1 NAG C 602 1555 1555 1.43 LINK ND2 ASN C 133 C1 NAG C 603 1555 1555 1.43 LINK ND2 ASN C 156 C1 NAG g 1 1555 1555 1.43 LINK ND2 ASN C 160 C1 NAG h 1 1555 1555 1.43 LINK ND2 ASN C 197 C1 NAG i 1 1555 1555 1.43 LINK ND2 ASN C 234 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG j 1 1555 1555 1.43 LINK ND2 ASN C 276 C1 NAG k 1 1555 1555 1.43 LINK ND2 ASN C 295 C1 NAG C 605 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG l 1 1555 1555 1.43 LINK ND2 ASN C 332 C1 NAG o 1 1555 1555 1.43 LINK ND2 ASN C 339 C1 NAG C 601 1555 1555 1.43 LINK ND2 ASN C 363 C1 NAG m 1 1555 1555 1.43 LINK ND2 ASN C 386 C1 NAG n 1 1555 1555 1.43 LINK OG SER C 388 C1 NAG n 1 1555 1555 1.43 LINK ND2 ASN C 392 C1 NAG C 606 1555 1555 1.43 LINK ND2 ASN C 448 C1 NAG C 607 1555 1555 1.43 LINK ND2 ASN D 611 C1 NAG D 701 1555 1555 1.43 LINK ND2 ASN D 637 C1 NAG D 702 1555 1555 1.43 LINK ND2 ASN E 611 C1 NAG E 701 1555 1555 1.43 LINK ND2 ASN E 637 C1 NAG E 702 1555 1555 1.43 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.43 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.39 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.39 LINK O4 NAG T 2 C1 MAN T 3 1555 1555 1.39 LINK O3 MAN T 3 C1 BMA T 4 1555 1555 1.39 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.40 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.39 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.39 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.39 LINK O3 BMA W 3 C1 BMA W 4 1555 1555 1.39 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.39 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.39 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.39 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.39 LINK O3 BMA Z 3 C1 MAN Z 4 1555 1555 1.39 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.39 LINK O4 NAG a 2 C1 MAN a 3 1555 1555 1.39 LINK O3 MAN a 3 C1 BMA a 4 1555 1555 1.39 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.39 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.39 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.39 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.39 LINK O3 BMA d 3 C1 MAN d 4 1555 1555 1.39 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.39 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.39 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.39 LINK O4 NAG g 2 C1 MAN g 3 1555 1555 1.39 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.39 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.39 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.39 LINK O3 BMA i 3 C1 MAN i 4 1555 1555 1.40 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.39 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.39 LINK O3 BMA j 3 C1 BMA j 4 1555 1555 1.40 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.39 LINK O4 NAG k 2 C1 MAN k 3 1555 1555 1.39 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.39 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.39 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.40 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.40 LINK O4 NAG o 2 C1 BMA o 3 1555 1555 1.39 LINK O3 BMA o 3 C1 MAN o 4 1555 1555 1.40 LINK O6 BMA o 3 C1 BMA o 6 1555 1555 1.40 LINK O2 MAN o 4 C1 BMA o 5 1555 1555 1.39 CISPEP 1 GLY C 312 PRO C 313 0 7.45 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