HEADER VIRAL PROTEIN/IMMUNE SYSTEM 28-JUL-24 9CV7 TITLE LJF-085 FAB IN COMPLEX WITH HIV ENV ZM233 NFL TD CC3+ TRIMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZM233 NFL TD CC3+ GP140; COMPND 3 CHAIN: B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LJF-085 HEAVY CHAIN FV; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LJF-085 LIGHT CHAIN FV; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 9 ORGANISM_TAXID: 9544; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 15 ORGANISM_TAXID: 9544; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NHP, RHESUS MACAQUE, GP120 INTERFACE, HIV, NFL, NEUTRALIZING KEYWDS 2 ANTIBODY, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR G.OZOROWSKI,A.B.WARD REVDAT 1 21-MAY-25 9CV7 0 JRNL AUTH F.A.SCHLEICH,S.BALE,J.GUENAGA,G.OZOROWSKI,M.ADORI,X.LIN, JRNL AUTH 2 X.CASTRO DOPICO,R.WILSON,M.CHERNYSHEV,A.T.COTGREAVE, JRNL AUTH 3 M.MANDOLESI,J.CLUFF,E.D.DOYLE,L.M.SEWALL,W.H.LEE,S.ZHANG, JRNL AUTH 4 S.O'DELL,B.S.HEALY,D.LIM,V.R.LEWIS,E.BEN-AKIVA,D.J.IRVINE, JRNL AUTH 5 N.A.DORIA-ROSE,M.CORCORAN,D.CARNATHAN,G.SILVESTRI, JRNL AUTH 6 I.A.WILSON,A.B.WARD,G.B.KARLSSON HEDESTAM,R.T.WYATT JRNL TITL VACCINATION OF NONHUMAN PRIMATES ELICITS A BROADLY JRNL TITL 2 NEUTRALIZING ANTIBODY LINEAGE TARGETING A QUATERNARY EPITOPE JRNL TITL 3 ON THE HIV-1 ENV TRIMER. JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 JRNL PMID 40339576 JRNL DOI 10.1016/J.IMMUNI.2025.04.010 REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.800 REMARK 3 NUMBER OF PARTICLES : 34340 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 9CV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000286385. 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 : LJF-085 FAB IN COMPLEX WITH HIV REMARK 245 ENV ZM233 NFL TD CC3+ TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 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 : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 700.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 4500.00 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, L, C, D, A, E, F, G 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 B 7 REMARK 465 PRO B 8 REMARK 465 MET B 9 REMARK 465 GLY B 10 REMARK 465 SER B 11 REMARK 465 LEU B 12 REMARK 465 GLN B 13 REMARK 465 PRO B 14 REMARK 465 LEU B 15 REMARK 465 ALA B 16 REMARK 465 THR B 17 REMARK 465 LEU B 18 REMARK 465 TYR B 19 REMARK 465 LEU B 20 REMARK 465 LEU B 21 REMARK 465 GLY B 22 REMARK 465 MET B 23 REMARK 465 LEU B 24 REMARK 465 VAL B 25 REMARK 465 ALA B 26 REMARK 465 SER B 27 REMARK 465 VAL B 28 REMARK 465 LEU B 29 REMARK 465 ALA B 30 REMARK 465 THR B 184A REMARK 465 ASN B 184B REMARK 465 SER B 184C REMARK 465 SER B 184D REMARK 465 ASN B 184E REMARK 465 THR B 184F REMARK 465 GLY B 457A REMARK 465 GLY B 457B REMARK 465 GLU B 457C REMARK 465 ASN B 457D REMARK 465 SER B 457E REMARK 465 SER B 457F REMARK 465 SER B 457G REMARK 465 THR B 457H REMARK 465 THR B 457I REMARK 465 GLU B 457J REMARK 465 VAL B 504A REMARK 465 VAL B 504B REMARK 465 GLU B 504C REMARK 465 GLY B 504D REMARK 465 GLY B 504E REMARK 465 GLY B 504F REMARK 465 GLY B 504G REMARK 465 SER B 504H REMARK 465 GLY B 504I REMARK 465 GLY B 504J REMARK 465 GLY B 504K REMARK 465 GLY B 504L REMARK 465 SER B 504M REMARK 465 ALA B 504N REMARK 465 VAL B 504O REMARK 465 GLY B 504P REMARK 465 ILE B 504Q REMARK 465 GLY B 504R REMARK 465 ALA B 504S REMARK 465 VAL B 504T REMARK 465 ARG B 504U REMARK 465 ARG B 504V REMARK 465 GLY B 504W REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 PRO 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 LYS 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 MET B 565 REMARK 465 LEU B 566 REMARK 465 GLN B 567 REMARK 465 LEU B 568 REMARK 465 GLY B 569 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 GLY B 666 REMARK 465 GLY B 667 REMARK 465 GLY B 668 REMARK 465 SER B 669 REMARK 465 HIS B 670 REMARK 465 HIS B 671 REMARK 465 HIS B 672 REMARK 465 HIS B 673 REMARK 465 HIS B 674 REMARK 465 HIS B 675 REMARK 465 HIS B 676 REMARK 465 HIS B 677 REMARK 465 GLY B 678 REMARK 465 SER B 679 REMARK 465 GLY B 680 REMARK 465 CYS B 681 REMARK 465 GLN H 1 REMARK 465 SER H 112 REMARK 465 SER H 113 REMARK 465 LYS L 107 REMARK 465 MET C 7 REMARK 465 PRO C 8 REMARK 465 MET C 9 REMARK 465 GLY C 10 REMARK 465 SER C 11 REMARK 465 LEU C 12 REMARK 465 GLN C 13 REMARK 465 PRO C 14 REMARK 465 LEU C 15 REMARK 465 ALA C 16 REMARK 465 THR C 17 REMARK 465 LEU C 18 REMARK 465 TYR C 19 REMARK 465 LEU C 20 REMARK 465 LEU C 21 REMARK 465 GLY C 22 REMARK 465 MET C 23 REMARK 465 LEU C 24 REMARK 465 VAL C 25 REMARK 465 ALA C 26 REMARK 465 SER C 27 REMARK 465 VAL C 28 REMARK 465 LEU C 29 REMARK 465 ALA C 30 REMARK 465 MET C 31 REMARK 465 GLU C 64 REMARK 465 LYS C 65 REMARK 465 HIS C 66 REMARK 465 SER C 67 REMARK 465 VAL C 68 REMARK 465 TRP C 69 REMARK 465 THR C 184A REMARK 465 ASN C 184B REMARK 465 SER C 184C REMARK 465 SER C 184D REMARK 465 ASN C 184E REMARK 465 THR C 184F REMARK 465 GLY C 457A REMARK 465 GLY C 457B REMARK 465 GLU C 457C REMARK 465 ASN C 457D REMARK 465 SER C 457E REMARK 465 SER C 457F REMARK 465 SER C 457G REMARK 465 THR C 457H REMARK 465 THR C 457I REMARK 465 GLU C 457J REMARK 465 CYS C 500A REMARK 465 LYS C 500B REMARK 465 ARG C 500C REMARK 465 ARG C 500D REMARK 465 VAL C 500E REMARK 465 VAL C 500F REMARK 465 GLU C 500G REMARK 465 GLY C 500H REMARK 465 GLY C 500I REMARK 465 GLY C 500J REMARK 465 GLY C 500K REMARK 465 SER C 500L REMARK 465 GLY C 500M REMARK 465 GLY C 500N REMARK 465 GLY C 500O REMARK 465 GLY C 500P REMARK 465 SER C 500Q REMARK 465 ALA C 500R REMARK 465 VAL C 500S REMARK 465 GLY C 500T REMARK 465 ILE C 500U REMARK 465 GLY C 500V REMARK 465 ALA C 500W REMARK 465 VAL C 500X REMARK 465 ARG C 500Y REMARK 465 ARG C 500Z REMARK 465 GLY C 501A REMARK 465 GLY C 547 REMARK 465 ILE C 548 REMARK 465 VAL C 549 REMARK 465 GLN C 550 REMARK 465 PRO C 551 REMARK 465 GLN C 552 REMARK 465 SER C 553 REMARK 465 ASN C 554 REMARK 465 LEU C 555 REMARK 465 LEU C 556 REMARK 465 LYS C 557 REMARK 465 ALA C 558 REMARK 465 PRO C 559 REMARK 465 GLU C 560 REMARK 465 ALA C 561 REMARK 465 GLN C 562 REMARK 465 GLN C 563 REMARK 465 HIS C 564 REMARK 465 MET C 565 REMARK 465 LEU C 566 REMARK 465 GLN C 567 REMARK 465 LEU C 568 REMARK 465 GLY C 569 REMARK 465 ASP C 664 REMARK 465 GLY C 665 REMARK 465 GLY C 666 REMARK 465 GLY C 667 REMARK 465 GLY C 668 REMARK 465 SER C 669 REMARK 465 HIS C 670 REMARK 465 HIS C 671 REMARK 465 HIS C 672 REMARK 465 HIS C 673 REMARK 465 HIS C 674 REMARK 465 HIS C 675 REMARK 465 HIS C 676 REMARK 465 HIS C 677 REMARK 465 GLY C 678 REMARK 465 SER C 679 REMARK 465 GLY C 680 REMARK 465 CYS C 681 REMARK 465 MET D 7 REMARK 465 PRO D 8 REMARK 465 MET D 9 REMARK 465 GLY D 10 REMARK 465 SER D 11 REMARK 465 LEU D 12 REMARK 465 GLN D 13 REMARK 465 PRO D 14 REMARK 465 LEU D 15 REMARK 465 ALA D 16 REMARK 465 THR D 17 REMARK 465 LEU D 18 REMARK 465 TYR D 19 REMARK 465 LEU D 20 REMARK 465 LEU D 21 REMARK 465 GLY D 22 REMARK 465 MET D 23 REMARK 465 LEU D 24 REMARK 465 VAL D 25 REMARK 465 ALA D 26 REMARK 465 SER D 27 REMARK 465 VAL D 28 REMARK 465 LEU D 29 REMARK 465 ALA D 30 REMARK 465 MET D 31 REMARK 465 GLY D 32 REMARK 465 ASP D 57 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 GLU D 64 REMARK 465 LYS D 65 REMARK 465 HIS D 66 REMARK 465 SER D 67 REMARK 465 THR D 184A REMARK 465 ASN D 184B REMARK 465 SER D 184C REMARK 465 SER D 184D REMARK 465 ASN D 184E REMARK 465 THR D 184F REMARK 465 GLY D 457A REMARK 465 GLY D 457B REMARK 465 GLU D 457C REMARK 465 ASN D 457D REMARK 465 SER D 457E REMARK 465 SER D 457F REMARK 465 SER D 457G REMARK 465 THR D 457H REMARK 465 THR D 457I REMARK 465 GLU D 457J REMARK 465 ARG D 503A REMARK 465 VAL D 503B REMARK 465 VAL D 503C REMARK 465 GLU D 503D REMARK 465 GLY D 503E REMARK 465 GLY D 503F REMARK 465 GLY D 503G REMARK 465 GLY D 503H REMARK 465 SER D 503I REMARK 465 GLY D 503J REMARK 465 GLY D 503K REMARK 465 GLY D 503L REMARK 465 GLY D 503M REMARK 465 SER D 503N REMARK 465 ALA D 503O REMARK 465 VAL D 503P REMARK 465 GLY D 503Q REMARK 465 ILE D 503R REMARK 465 GLY D 503S REMARK 465 ALA D 503T REMARK 465 VAL D 503U REMARK 465 ARG D 503V REMARK 465 ARG D 503W REMARK 465 GLY D 503X REMARK 465 PHE D 503Y REMARK 465 LEU D 503Z REMARK 465 GLY D 504A REMARK 465 SER D 546 REMARK 465 GLY D 547 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 PRO 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 LYS 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 MET D 565 REMARK 465 LEU D 566 REMARK 465 GLN D 567 REMARK 465 LEU D 568 REMARK 465 GLY D 569 REMARK 465 VAL D 570 REMARK 465 LEU D 660 REMARK 465 LEU D 661 REMARK 465 CYS D 662 REMARK 465 LEU D 663 REMARK 465 ASP D 664 REMARK 465 GLY D 665 REMARK 465 GLY D 666 REMARK 465 GLY D 667 REMARK 465 GLY D 668 REMARK 465 SER D 669 REMARK 465 HIS D 670 REMARK 465 HIS D 671 REMARK 465 HIS D 672 REMARK 465 HIS D 673 REMARK 465 HIS D 674 REMARK 465 HIS D 675 REMARK 465 HIS D 676 REMARK 465 HIS D 677 REMARK 465 GLY D 678 REMARK 465 SER D 679 REMARK 465 GLY D 680 REMARK 465 CYS D 681 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 378 CB CYS D 445 1.81 REMARK 500 OG SER B 364 O PRO B 470 2.14 REMARK 500 NE1 TRP D 45 OE2 GLU D 91 2.16 REMARK 500 O SER D 256 ND2 ASN D 478 2.16 REMARK 500 O THR B 50 NE2 GLN B 103 2.17 REMARK 500 ND2 ASN H 35 CD2 TYR H 50 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 C 228 CA - CB - SG ANGL. DEV. = -10.8 DEGREES REMARK 500 CYS D 296 CA - CB - SG ANGL. DEV. = 7.2 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 ASP B 47 97.29 -69.40 REMARK 500 THR B 163 -169.33 -101.47 REMARK 500 GLN B 258 -8.83 73.63 REMARK 500 PHE B 353 88.68 -154.81 REMARK 500 GLN B 428 14.93 58.71 REMARK 500 CYS B 598 45.52 -141.27 REMARK 500 ILE H 48 -85.94 -116.92 REMARK 500 LEU H 63 78.67 -103.15 REMARK 500 ASN H 65 17.94 56.01 REMARK 500 SER H 82B 61.14 60.55 REMARK 500 ALA H 88 -178.93 -174.15 REMARK 500 ASN H 100E 61.99 33.80 REMARK 500 PHE H 100G 94.75 -68.22 REMARK 500 SER L 14 -65.44 -94.25 REMARK 500 GLN L 24 -137.65 53.63 REMARK 500 ALA L 25 -128.97 54.29 REMARK 500 ASN L 32 57.38 -94.46 REMARK 500 GLU L 70 52.43 -95.18 REMARK 500 ALA L 84 -175.42 -172.52 REMARK 500 LEU C 122 50.28 -90.59 REMARK 500 ASP C 167 -55.18 -150.87 REMARK 500 PRO C 253 72.63 -69.62 REMARK 500 GLN C 258 -8.41 73.22 REMARK 500 GLU C 290 -157.66 66.55 REMARK 500 ASN C 355 -10.38 74.34 REMARK 500 THR C 387 32.17 -97.84 REMARK 500 LEU C 410 -2.56 74.18 REMARK 500 MET C 426 -162.90 -115.01 REMARK 500 TRP C 427 10.12 57.56 REMARK 500 THR C 450 -4.83 -59.45 REMARK 500 CYS C 604 -146.68 -108.48 REMARK 500 THR C 605 -98.72 -102.47 REMARK 500 ASN C 607 26.59 82.21 REMARK 500 ASP D 47 90.66 -67.60 REMARK 500 GLN D 258 -40.99 64.23 REMARK 500 GLU D 290 161.13 64.55 REMARK 500 PRO D 363 -179.13 -66.84 REMARK 500 ASN D 396 -0.81 66.28 REMARK 500 THR D 450 26.99 -140.28 REMARK 500 LEU D 452 143.14 -171.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-45957 RELATED DB: EMDB REMARK 900 LJF-085 FAB IN COMPLEX WITH HIV ENV ZM233 NFL TD CC3+ TRIMER DBREF 9CV7 B 7 681 PDB 9CV7 9CV7 7 681 DBREF 9CV7 H 1 113 PDB 9CV7 9CV7 1 113 DBREF 9CV7 L 1 107 PDB 9CV7 9CV7 1 107 DBREF 9CV7 C 7 681 PDB 9CV7 9CV7 7 681 DBREF 9CV7 D 7 681 PDB 9CV7 9CV7 7 681 SEQRES 1 B 661 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 B 661 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA MET GLY SEQRES 3 B 661 SER LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 B 661 ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 B 661 LYS ALA TYR GLU THR GLU LYS HIS SER VAL TRP ALA THR SEQRES 6 B 661 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU MET SEQRES 7 B 661 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 8 B 661 ASN ASP MET VAL ASP GLN MET HIS THR ASP VAL ILE SER SEQRES 9 B 661 ILE TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 B 661 PRO LEU CYS VAL THR LEU ASP CYS SER THR TYR ASN ASN SEQRES 11 B 661 THR HIS ASN ILE SER LYS GLU MET LYS ILE CYS SER PHE SEQRES 12 B 661 ASN MET THR THR GLU LEU ARG ASP LYS LYS ARG LYS VAL SEQRES 13 B 661 ASN VAL LEU PHE TYR LYS LEU ASP LEU VAL PRO LEU THR SEQRES 14 B 661 ASN SER SER ASN THR THR ASN TYR ARG LEU ILE SER CYS SEQRES 15 B 661 ASN THR SER THR ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 16 B 661 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 17 B 661 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE ASN GLY SEQRES 18 B 661 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 19 B 661 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 20 B 661 ASN GLY SER LEU ALA GLU GLU GLU ILE ILE ILE ARG PHE SEQRES 21 B 661 GLU ASN LEU THR ASP ASN VAL LYS ILE ILE ILE VAL GLN SEQRES 22 B 661 LEU ASN GLU THR ILE ASN ILE THR CYS THR ARG PRO ASN SEQRES 23 B 661 ASN TYR THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN SEQRES 24 B 661 SER PHE TYR ALA MET GLY GLU ILE VAL GLY ASN ILE ARG SEQRES 25 B 661 GLU ALA HIS CYS ASN ILE SER ALA SER LYS TRP ASN LYS SEQRES 26 B 661 THR LEU GLU ARG VAL ARG THR LYS LEU LYS GLU HIS PHE SEQRES 27 B 661 PRO ASN LYS THR ILE GLU PHE GLU PRO SER SER GLY GLY SEQRES 28 B 661 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 29 B 661 GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER SEQRES 30 B 661 ALA ILE ASN GLY THR LEU THR SER ASN VAL THR LEU PRO SEQRES 31 B 661 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG VAL SEQRES 32 B 661 GLY GLN ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE SEQRES 33 B 661 THR CYS LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 34 B 661 ASP GLY GLY GLU ASN SER SER SER THR THR GLU THR PHE SEQRES 35 B 661 ARG PRO THR GLY GLY ASP MET LYS ASN ASN TRP ARG SER SEQRES 36 B 661 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE LYS PRO LEU SEQRES 37 B 661 GLY ILE ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 38 B 661 GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL GLY SEQRES 39 B 661 ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA GLY SEQRES 40 B 661 SER THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN SEQRES 41 B 661 ALA ARG GLN LEU LEU SER GLY ILE VAL GLN PRO GLN SER SEQRES 42 B 661 ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN HIS MET LEU SEQRES 43 B 661 GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG SEQRES 44 B 661 VAL LEU ALA ILE GLU ARG TYR LEU LYS ASP GLN GLN LEU SEQRES 45 B 661 LEU GLY LEU TRP GLY CYS SER GLY LYS LEU ILE CYS THR SEQRES 46 B 661 THR ASN VAL PRO TRP ASN ALA SER TRP SER ASN LYS SER SEQRES 47 B 661 LYS ASN ASP ILE TRP ASP ASN MET THR TRP MET GLN TRP SEQRES 48 B 661 ASP ARG GLU ILE GLY ASN HIS THR ASP THR ILE TYR ARG SEQRES 49 B 661 LEU LEU GLU ASP SER GLN ASN GLN GLN GLU LYS ASN GLU SEQRES 50 B 661 LYS ASP LEU LEU CYS LEU ASP GLY GLY GLY GLY SER HIS SEQRES 51 B 661 HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS SEQRES 1 H 123 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 123 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 123 GLY SER ILE ASP ASP TYR PHE TRP ASN TRP VAL ARG GLN SEQRES 4 H 123 PRO PRO GLY LYS PRO LEU GLU CYS ILE GLY TYR ILE PHE SEQRES 5 H 123 GLY ARG GLY GLY GLY THR LYS TYR ASN PRO SER LEU ASP SEQRES 6 H 123 ASN ARG VAL THR ILE SER THR ASP THR PRO ASN GLN PHE SEQRES 7 H 123 SER LEU LYS LEU ARG SER VAL THR VAL ALA ASP THR ALA SEQRES 8 H 123 ILE TYR TYR CYS ALA ARG TRP ASN LEU TYR ASP ASP ASP SEQRES 9 H 123 PHE GLY TYR ASN SER PHE ALA VAL TRP GLY ARG GLY VAL SEQRES 10 H 123 LEU VAL THR VAL SER SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 107 SER VAL GLY ASP THR VAL THR ILE THR CYS GLN ALA ARG SEQRES 3 L 107 HIS ALA VAL GLY LYS ASN LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY ARG GLY PRO GLN LEU LEU ILE TYR MET ALA SER SEQRES 5 L 107 SER ARG HIS SER GLY VAL PRO SER ARG PHE ARG GLY SER SEQRES 6 L 107 GLY SER GLY ARG GLU PHE THR LEU THR ILE ASN ASN LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR SER CYS GLN GLN GLY SEQRES 8 L 107 TYR THR TYR PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 107 GLU MET LYS SEQRES 1 C 661 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 C 661 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA MET GLY SEQRES 3 C 661 SER LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 C 661 ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 C 661 LYS ALA TYR GLU THR GLU LYS HIS SER VAL TRP ALA THR SEQRES 6 C 661 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU MET SEQRES 7 C 661 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 8 C 661 ASN ASP MET VAL ASP GLN MET HIS THR ASP VAL ILE SER SEQRES 9 C 661 ILE TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 C 661 PRO LEU CYS VAL THR LEU ASP CYS SER THR TYR ASN ASN SEQRES 11 C 661 THR HIS ASN ILE SER LYS GLU MET LYS ILE CYS SER PHE SEQRES 12 C 661 ASN MET THR THR GLU LEU ARG ASP LYS LYS ARG LYS VAL SEQRES 13 C 661 ASN VAL LEU PHE TYR LYS LEU ASP LEU VAL PRO LEU THR SEQRES 14 C 661 ASN SER SER ASN THR THR ASN TYR ARG LEU ILE SER CYS SEQRES 15 C 661 ASN THR SER THR ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 16 C 661 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 17 C 661 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE ASN GLY SEQRES 18 C 661 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 19 C 661 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 20 C 661 ASN GLY SER LEU ALA GLU GLU GLU ILE ILE ILE ARG PHE SEQRES 21 C 661 GLU ASN LEU THR ASP ASN VAL LYS ILE ILE ILE VAL GLN SEQRES 22 C 661 LEU ASN GLU THR ILE ASN ILE THR CYS THR ARG PRO ASN SEQRES 23 C 661 ASN TYR THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN SEQRES 24 C 661 SER PHE TYR ALA MET GLY GLU ILE VAL GLY ASN ILE ARG SEQRES 25 C 661 GLU ALA HIS CYS ASN ILE SER ALA SER LYS TRP ASN LYS SEQRES 26 C 661 THR LEU GLU ARG VAL ARG THR LYS LEU LYS GLU HIS PHE SEQRES 27 C 661 PRO ASN LYS THR ILE GLU PHE GLU PRO SER SER GLY GLY SEQRES 28 C 661 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 29 C 661 GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER SEQRES 30 C 661 ALA ILE ASN GLY THR LEU THR SER ASN VAL THR LEU PRO SEQRES 31 C 661 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG VAL SEQRES 32 C 661 GLY GLN ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE SEQRES 33 C 661 THR CYS LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 34 C 661 ASP GLY GLY GLU ASN SER SER SER THR THR GLU THR PHE SEQRES 35 C 661 ARG PRO THR GLY GLY ASP MET LYS ASN ASN TRP ARG SER SEQRES 36 C 661 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE LYS PRO LEU SEQRES 37 C 661 GLY ILE ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 38 C 661 GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL GLY SEQRES 39 C 661 ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA GLY SEQRES 40 C 661 SER THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN SEQRES 41 C 661 ALA ARG GLN LEU LEU SER GLY ILE VAL GLN PRO GLN SER SEQRES 42 C 661 ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN HIS MET LEU SEQRES 43 C 661 GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG SEQRES 44 C 661 VAL LEU ALA ILE GLU ARG TYR LEU LYS ASP GLN GLN LEU SEQRES 45 C 661 LEU GLY LEU TRP GLY CYS SER GLY LYS LEU ILE CYS THR SEQRES 46 C 661 THR ASN VAL PRO TRP ASN ALA SER TRP SER ASN LYS SER SEQRES 47 C 661 LYS ASN ASP ILE TRP ASP ASN MET THR TRP MET GLN TRP SEQRES 48 C 661 ASP ARG GLU ILE GLY ASN HIS THR ASP THR ILE TYR ARG SEQRES 49 C 661 LEU LEU GLU ASP SER GLN ASN GLN GLN GLU LYS ASN GLU SEQRES 50 C 661 LYS ASP LEU LEU CYS LEU ASP GLY GLY GLY GLY SER HIS SEQRES 51 C 661 HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS SEQRES 1 D 661 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR SEQRES 2 D 661 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA MET GLY SEQRES 3 D 661 SER LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 4 D 661 ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 5 D 661 LYS ALA TYR GLU THR GLU LYS HIS SER VAL TRP ALA THR SEQRES 6 D 661 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU MET SEQRES 7 D 661 VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP LYS SEQRES 8 D 661 ASN ASP MET VAL ASP GLN MET HIS THR ASP VAL ILE SER SEQRES 9 D 661 ILE TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 10 D 661 PRO LEU CYS VAL THR LEU ASP CYS SER THR TYR ASN ASN SEQRES 11 D 661 THR HIS ASN ILE SER LYS GLU MET LYS ILE CYS SER PHE SEQRES 12 D 661 ASN MET THR THR GLU LEU ARG ASP LYS LYS ARG LYS VAL SEQRES 13 D 661 ASN VAL LEU PHE TYR LYS LEU ASP LEU VAL PRO LEU THR SEQRES 14 D 661 ASN SER SER ASN THR THR ASN TYR ARG LEU ILE SER CYS SEQRES 15 D 661 ASN THR SER THR ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 16 D 661 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 17 D 661 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE ASN GLY SEQRES 18 D 661 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 19 D 661 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 20 D 661 ASN GLY SER LEU ALA GLU GLU GLU ILE ILE ILE ARG PHE SEQRES 21 D 661 GLU ASN LEU THR ASP ASN VAL LYS ILE ILE ILE VAL GLN SEQRES 22 D 661 LEU ASN GLU THR ILE ASN ILE THR CYS THR ARG PRO ASN SEQRES 23 D 661 ASN TYR THR ARG LYS SER ILE ARG ILE GLY PRO GLY GLN SEQRES 24 D 661 SER PHE TYR ALA MET GLY GLU ILE VAL GLY ASN ILE ARG SEQRES 25 D 661 GLU ALA HIS CYS ASN ILE SER ALA SER LYS TRP ASN LYS SEQRES 26 D 661 THR LEU GLU ARG VAL ARG THR LYS LEU LYS GLU HIS PHE SEQRES 27 D 661 PRO ASN LYS THR ILE GLU PHE GLU PRO SER SER GLY GLY SEQRES 28 D 661 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 29 D 661 GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER SEQRES 30 D 661 ALA ILE ASN GLY THR LEU THR SER ASN VAL THR LEU PRO SEQRES 31 D 661 CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG VAL SEQRES 32 D 661 GLY GLN ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE SEQRES 33 D 661 THR CYS LYS SER ASN ILE THR GLY LEU LEU LEU THR ARG SEQRES 34 D 661 ASP GLY GLY GLU ASN SER SER SER THR THR GLU THR PHE SEQRES 35 D 661 ARG PRO THR GLY GLY ASP MET LYS ASN ASN TRP ARG SER SEQRES 36 D 661 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE LYS PRO LEU SEQRES 37 D 661 GLY ILE ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 38 D 661 GLY GLY GLY GLY SER GLY GLY GLY GLY SER ALA VAL GLY SEQRES 39 D 661 ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY ALA ALA GLY SEQRES 40 D 661 SER THR MET GLY ALA ALA SER MET THR LEU THR VAL GLN SEQRES 41 D 661 ALA ARG GLN LEU LEU SER GLY ILE VAL GLN PRO GLN SER SEQRES 42 D 661 ASN LEU LEU LYS ALA PRO GLU ALA GLN GLN HIS MET LEU SEQRES 43 D 661 GLN LEU GLY VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG SEQRES 44 D 661 VAL LEU ALA ILE GLU ARG TYR LEU LYS ASP GLN GLN LEU SEQRES 45 D 661 LEU GLY LEU TRP GLY CYS SER GLY LYS LEU ILE CYS THR SEQRES 46 D 661 THR ASN VAL PRO TRP ASN ALA SER TRP SER ASN LYS SER SEQRES 47 D 661 LYS ASN ASP ILE TRP ASP ASN MET THR TRP MET GLN TRP SEQRES 48 D 661 ASP ARG GLU ILE GLY ASN HIS THR ASP THR ILE TYR ARG SEQRES 49 D 661 LEU LEU GLU ASP SER GLN ASN GLN GLN GLU LYS ASN GLU SEQRES 50 D 661 LYS ASP LEU LEU CYS LEU ASP GLY GLY GLY GLY SER HIS SEQRES 51 D 661 HIS HIS HIS HIS HIS HIS HIS GLY SER GLY CYS HET NAG A 1 14 HET NAG A 2 14 HET BMA A 3 11 HET MAN A 4 11 HET MAN A 5 11 HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET NAG B 705 14 HET NAG B 706 14 HET NAG B 707 14 HET NAG B 708 14 HET NAG B 709 14 HET NAG B 710 14 HET NAG B 711 14 HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 14 HET NAG C 704 14 HET NAG C 705 14 HET NAG C 706 14 HET NAG C 707 14 HET NAG C 708 14 HET NAG C 709 14 HET NAG C 710 14 HET NAG C 711 14 HET NAG D 701 14 HET NAG D 702 14 HET NAG D 703 14 HET NAG D 704 14 HET NAG D 705 14 HET NAG D 706 14 HET NAG D 707 14 HET NAG D 708 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 6 NAG 38(C8 H15 N O6) FORMUL 6 BMA 2(C6 H12 O6) FORMUL 6 MAN 2(C6 H12 O6) HELIX 1 AA1 LYS B 59 LYS B 65 1 7 HELIX 2 AA2 ASN B 98 LYS B 117 1 20 HELIX 3 AA3 THR B 123 CYS B 126 5 4 HELIX 4 AA4 SER B 195 ASN B 197 5 3 HELIX 5 AA5 SER B 334 LYS B 350 1 17 HELIX 6 AA6 ASP B 368 THR B 373 1 6 HELIX 7 AA7 THR B 387 ASN B 392 1 6 HELIX 8 AA8 ASN B 425 ARG B 429 5 5 HELIX 9 AA9 ASP B 474 LEU B 483 1 10 HELIX 10 AB1 THR B 529 THR B 536 1 8 HELIX 11 AB2 THR B 536 SER B 546 1 11 HELIX 12 AB3 TRP B 571 GLY B 597 1 27 HELIX 13 AB4 SER B 618 ASN B 625 1 8 HELIX 14 AB5 THR B 627 GLY B 636 1 10 HELIX 15 AB6 HIS B 638 CYS B 662 1 25 HELIX 16 AB7 PRO H 61 ASP H 64 5 4 HELIX 17 AB8 THR H 83 THR H 87 5 5 HELIX 18 AB9 GLN L 79 PHE L 83 5 5 HELIX 19 AC1 ASN C 98 LYS C 117 1 20 HELIX 20 AC2 LEU C 122 CYS C 126 5 5 HELIX 21 AC3 SER C 334 PHE C 353 1 20 HELIX 22 AC4 ASP C 368 THR C 373 1 6 HELIX 23 AC5 ASP C 474 LEU C 483 1 10 HELIX 24 AC6 THR C 529 SER C 534 1 6 HELIX 25 AC7 THR C 536 LEU C 544 1 9 HELIX 26 AC8 TRP C 571 GLY C 597 1 27 HELIX 27 AC9 ASN C 611 SER C 615 5 5 HELIX 28 AD1 ASN C 620 MET C 626 1 7 HELIX 29 AD2 THR C 627 GLY C 636 1 10 HELIX 30 AD3 HIS C 638 CYS C 662 1 25 HELIX 31 AD4 ASN D 98 LYS D 117 1 20 HELIX 32 AD5 LEU D 122 CYS D 126 5 5 HELIX 33 AD6 SER D 334 PHE D 353 1 20 HELIX 34 AD7 THR D 387 ASN D 392 1 6 HELIX 35 AD8 ASN D 425 ARG D 429 5 5 HELIX 36 AD9 ASP D 474 TYR D 484 1 11 HELIX 37 AE1 THR D 529 SER D 534 1 6 HELIX 38 AE2 THR D 536 LEU D 545 1 10 HELIX 39 AE3 GLY D 572 TRP D 596 1 25 HELIX 40 AE4 THR D 627 ASP D 659 1 33 SHEET 1 AA1 3 LEU B 494 PRO B 498 0 SHEET 2 AA1 3 TRP B 35 TYR B 40 -1 N TYR B 39 O GLY B 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL B 36 SHEET 1 AA2 5 TRP B 45 ARG B 46 0 SHEET 2 AA2 5 LYS B 487 ILE B 491 -1 O GLU B 490 N ARG B 46 SHEET 3 AA2 5 TYR B 223 CYS B 228 -1 N LEU B 226 O LYS B 487 SHEET 4 AA2 5 VAL B 242 VAL B 245 -1 O VAL B 245 N ILE B 225 SHEET 5 AA2 5 GLU B 83 VAL B 85 -1 N MET B 84 O THR B 244 SHEET 1 AA3 2 ALA B 55 SER B 56 0 SHEET 2 AA3 2 VAL B 75 PRO B 76 1 O VAL B 75 N SER B 56 SHEET 1 AA4 2 GLU B 91 ASN B 94 0 SHEET 2 AA4 2 THR B 236 CYS B 239 -1 O GLY B 237 N PHE B 93 SHEET 1 AA5 4 LYS B 121 LEU B 122 0 SHEET 2 AA5 4 ILE B 201 GLN B 203 -1 O ILE B 201 N LEU B 122 SHEET 3 AA5 4 MET B 434 TYR B 435 1 O TYR B 435 N THR B 202 SHEET 4 AA5 4 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AA6 5 LYS B 169 TYR B 177 0 SHEET 2 AA6 5 ILE B 150 THR B 162 -1 N CYS B 157 O VAL B 174 SHEET 3 AA6 5 LEU B 129 ASN B 135 -1 N ASP B 130 O SER B 158 SHEET 4 AA6 5 ASN B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AA6 5 LEU B 181 PRO B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AA7 7 LEU B 259 LEU B 261 0 SHEET 2 AA7 7 ILE B 443 THR B 455 -1 O GLY B 451 N LEU B 260 SHEET 3 AA7 7 ILE B 284 ARG B 298 -1 N ILE B 284 O LEU B 454 SHEET 4 AA7 7 ALA B 329 ILE B 333 -1 O ASN B 332 N THR B 295 SHEET 5 AA7 7 PRO B 417 ILE B 420 -1 O CYS B 418 N ALA B 329 SHEET 6 AA7 7 GLU B 381 CYS B 385 -1 N TYR B 384 O ARG B 419 SHEET 7 AA7 7 HIS B 374 CYS B 378 -1 N PHE B 376 O PHE B 383 SHEET 1 AA8 4 ILE B 271 PHE B 274 0 SHEET 2 AA8 4 ILE B 284 ARG B 298 -1 O ILE B 285 N ARG B 273 SHEET 3 AA8 4 ILE B 443 THR B 455 -1 O LEU B 454 N ILE B 284 SHEET 4 AA8 4 ARG B 469 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 1 AA9 2 ARG B 304 GLY B 312 0 SHEET 2 AA9 2 GLN B 315 MET B 320 -1 O PHE B 317 N ILE B 307 SHEET 1 AB1 4 LEU H 4 SER H 7 0 SHEET 2 AB1 4 LEU H 18 VAL H 24 -1 O THR H 23 N GLN H 5 SHEET 3 AB1 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AB1 4 VAL H 67 THR H 73 -1 N SER H 70 O SER H 79 SHEET 1 AB2 3 GLU H 46 CYS H 47 0 SHEET 2 AB2 3 PHE H 33 ARG H 38 -1 N ARG H 38 O GLU H 46 SHEET 3 AB2 3 CYS H 92 TRP H 95 -1 O ALA H 93 N ASN H 35 SHEET 1 AB3 2 GLY H 49 ILE H 51 0 SHEET 2 AB3 2 THR H 57 TYR H 59 -1 O LYS H 58 N TYR H 50 SHEET 1 AB4 2 ALA H 88 TYR H 90 0 SHEET 2 AB4 2 VAL H 107 VAL H 109 -1 O VAL H 109 N ALA H 88 SHEET 1 AB5 3 THR L 18 THR L 20 0 SHEET 2 AB5 3 THR L 72 ILE L 75 -1 O LEU L 73 N VAL L 19 SHEET 3 AB5 3 PHE L 62 SER L 65 -1 N SER L 65 O THR L 72 SHEET 1 AB6 2 TYR L 36 GLN L 38 0 SHEET 2 AB6 2 PRO L 44 LEU L 46 -1 O GLN L 45 N GLN L 37 SHEET 1 AB7 2 THR L 85 TYR L 86 0 SHEET 2 AB7 2 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 86 SHEET 1 AB8 2 TRP C 35 TYR C 39 0 SHEET 2 AB8 2 GLY C 495 THR C 499 -1 O ALA C 497 N THR C 37 SHEET 1 AB9 5 TRP C 45 ARG C 46 0 SHEET 2 AB9 5 LYS C 487 ILE C 491 -1 O GLU C 490 N ARG C 46 SHEET 3 AB9 5 TYR C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AB9 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB9 5 GLU C 83 VAL C 85 -1 N MET C 84 O THR C 244 SHEET 1 AC1 2 GLU C 91 PHE C 93 0 SHEET 2 AC1 2 GLY C 237 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AC2 5 VAL C 172 TYR C 177 0 SHEET 2 AC2 5 ILE C 150 PHE C 159 -1 N CYS C 157 O VAL C 174 SHEET 3 AC2 5 LEU C 129 ASN C 135 -1 N TYR C 134 O SER C 151 SHEET 4 AC2 5 ASN C 190 ARG C 192 -1 O TYR C 191 N LEU C 129 SHEET 5 AC2 5 VAL C 182 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AC3 3 THR C 200 ILE C 201 0 SHEET 2 AC3 3 GLN C 432 TYR C 435 1 O ALA C 433 N THR C 200 SHEET 3 AC3 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC4 4 LEU C 259 LEU C 260 0 SHEET 2 AC4 4 GLY C 451 THR C 455 -1 O GLY C 451 N LEU C 260 SHEET 3 AC4 4 ILE C 283 GLN C 287 -1 N ILE C 284 O LEU C 454 SHEET 4 AC4 4 ILE C 271 PHE C 274 -1 N ILE C 271 O GLN C 287 SHEET 1 AC5 3 LEU C 259 LEU C 260 0 SHEET 2 AC5 3 GLY C 451 THR C 455 -1 O GLY C 451 N LEU C 260 SHEET 3 AC5 3 ARG C 469 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AC6 6 HIS C 374 CYS C 378 0 SHEET 2 AC6 6 GLU C 381 CYS C 385 -1 O PHE C 383 N PHE C 376 SHEET 3 AC6 6 VAL C 414 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 4 AC6 6 HIS C 330 ILE C 333 -1 N CYS C 331 O LEU C 416 SHEET 5 AC6 6 ILE C 294 ARG C 298 -1 N THR C 295 O ASN C 332 SHEET 6 AC6 6 ILE C 443 SER C 447 -1 O SER C 447 N ILE C 294 SHEET 1 AC7 2 ASN C 301 TYR C 302 0 SHEET 2 AC7 2 ILE C 323 VAL C 323A-1 O VAL C 323A N ASN C 301 SHEET 1 AC8 2 LYS C 305 GLY C 312 0 SHEET 2 AC8 2 GLN C 315 ALA C 319 -1 O ALA C 319 N LYS C 305 SHEET 1 AC9 3 GLY D 495 ILE D 496 0 SHEET 2 AC9 3 TRP D 35 TYR D 39 -1 N TYR D 39 O GLY D 495 SHEET 3 AC9 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL D 38 SHEET 1 AD1 4 MET D 84 VAL D 85 0 SHEET 2 AD1 4 VAL D 242 VAL D 245 -1 O THR D 244 N MET D 84 SHEET 3 AD1 4 TYR D 223 CYS D 228 -1 N ILE D 225 O VAL D 245 SHEET 4 AD1 4 TYR D 486 GLU D 490 -1 O LYS D 487 N LEU D 226 SHEET 1 AD2 5 LYS D 169 TYR D 177 0 SHEET 2 AD2 5 ILE D 150 THR D 162 -1 N MET D 161 O ARG D 170 SHEET 3 AD2 5 LEU D 129 ASN D 135 -1 N SER D 132 O ILE D 156 SHEET 4 AD2 5 ASN D 190 LEU D 193 -1 O TYR D 191 N LEU D 129 SHEET 5 AD2 5 LEU D 181 PRO D 183 -1 N VAL D 182 O ARG D 192 SHEET 1 AD3 3 ILE D 201 GLN D 203 0 SHEET 2 AD3 3 ALA D 433 TYR D 435 1 O TYR D 435 N THR D 202 SHEET 3 AD3 3 ILE D 423 ILE D 424 -1 N ILE D 424 O MET D 434 SHEET 1 AD4 3 ILE D 271 PHE D 274 0 SHEET 2 AD4 3 ILE D 284 THR D 297 -1 O ILE D 285 N ARG D 273 SHEET 3 AD4 3 THR D 444 LEU D 454 -1 O LEU D 452 N VAL D 286 SHEET 1 AD5 2 ASN D 301 GLY D 312 0 SHEET 2 AD5 2 GLN D 315 VAL D 323A-1 O GLY D 321 N THR D 303 SHEET 1 AD6 4 ALA D 329 ASN D 332 0 SHEET 2 AD6 4 THR D 415 ILE D 420 -1 O CYS D 418 N ALA D 329 SHEET 3 AD6 4 GLU D 381 CYS D 385 -1 N TYR D 384 O ARG D 419 SHEET 4 AD6 4 HIS D 374 CYS D 378 -1 N PHE D 376 O PHE D 383 SSBOND 1 CYS B 54 CYS B 74 1555 1555 2.03 SSBOND 2 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 3 CYS B 126 CYS B 196 1555 1555 2.03 SSBOND 4 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 5 CYS B 218 CYS B 247 1555 1555 2.02 SSBOND 6 CYS B 228 CYS B 239 1555 1555 2.03 SSBOND 7 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 8 CYS B 378 CYS B 445 1555 1555 2.04 SSBOND 9 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 10 CYS B 501 CYS C 662 1555 1555 2.03 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS B 662 CYS D 501 1555 1555 2.03 SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 14 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 15 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 16 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 17 CYS C 126 CYS C 196 1555 1555 2.02 SSBOND 18 CYS C 131 CYS C 157 1555 1555 2.04 SSBOND 19 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 20 CYS C 228 CYS C 239 1555 1555 2.01 SSBOND 21 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 22 CYS C 378 CYS C 445 1555 1555 2.02 SSBOND 23 CYS C 385 CYS C 418 1555 1555 2.02 SSBOND 24 CYS C 598 CYS C 604 1555 1555 2.03 SSBOND 25 CYS D 54 CYS D 74 1555 1555 2.03 SSBOND 26 CYS D 119 CYS D 205 1555 1555 2.03 SSBOND 27 CYS D 126 CYS D 196 1555 1555 2.03 SSBOND 28 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 29 CYS D 218 CYS D 247 1555 1555 2.03 SSBOND 30 CYS D 228 CYS D 239 1555 1555 2.03 SSBOND 31 CYS D 296 CYS D 331 1555 1555 2.03 SSBOND 32 CYS D 378 CYS D 445 1555 1555 1.85 SSBOND 33 CYS D 385 CYS D 418 1555 1555 2.03 SSBOND 34 CYS D 598 CYS D 604 1555 1555 2.03 LINK ND2 ASN B 160 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 197 C1 NAG B 702 1555 1555 1.45 LINK ND2 ASN B 229 C1 NAG B 705 1555 1555 1.45 LINK ND2 ASN B 230 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 234 C1 NAG B 704 1555 1555 1.44 LINK ND2 ASN B 262 C1 NAG A 1 1555 1555 1.44 LINK ND2 ASN B 289 C1 NAG B 706 1555 1555 1.43 LINK ND2 ASN B 301 C1 NAG B 707 1555 1555 1.46 LINK ND2 ASN B 332 C1 NAG B 708 1555 1555 1.44 LINK ND2 ASN B 386 C1 NAG B 709 1555 1555 1.44 LINK ND2 ASN B 448 C1 NAG B 710 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 711 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 707 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN C 230 C1 NAG C 701 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 241 C1 NAG C 703 1555 1555 1.45 LINK ND2 ASN C 262 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG C 708 1555 1555 1.44 LINK ND2 ASN C 289 C1 NAG C 704 1555 1555 1.45 LINK ND2 ASN C 293 C1 NAG C 709 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 705 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 710 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 706 1555 1555 1.45 LINK ND2 ASN C 413 C1 NAG C 711 1555 1555 1.44 LINK ND2 ASN D 160 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 197 C1 NAG D 702 1555 1555 1.44 LINK ND2 ASN D 230 C1 NAG D 703 1555 1555 1.45 LINK ND2 ASN D 234 C1 NAG D 704 1555 1555 1.44 LINK ND2 ASN D 241 C1 NAG D 705 1555 1555 1.45 LINK ND2 ASN D 262 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN D 289 C1 NAG D 706 1555 1555 1.44 LINK ND2 ASN D 332 C1 NAG D 707 1555 1555 1.44 LINK ND2 ASN D 386 C1 NAG D 708 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.47 LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.46 LINK O3 BMA A 3 C1 MAN A 4 1555 1555 1.44 LINK O6 BMA A 3 C1 MAN A 5 1555 1555 1.48 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.47 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.46 CISPEP 1 SER L 7 PRO L 8 0 -5.05 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