HEADER VIRAL PROTEIN/IMMUNE SYSTEM 20-MAR-17 5V7J TITLE CRYSTAL STRUCTURE AT 3.7 A RESOLUTION OF GLYCOSYLATED HIV-1 CLADE A TITLE 2 BG505 SOSIP.664 PREFUSION ENV TRIMER WITH FOUR GLYCANS (N197, N276, TITLE 3 N362, AND N462) REMOVED IN COMPLEX WITH NEUTRALIZING ANTIBODIES TITLE 4 3H+109L AND 35O22. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: G; COMPND 4 FRAGMENT: UNP RESIDUES 31-505; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: UNP RESIDUES 509-661; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: ANTIBODY 3H+109L FAB LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 ENGINEERED: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: ANTIBODY 3H+109L FAB HEAVY CHAIN; COMPND 18 CHAIN: H; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: ANTIBODY 35O22 FAB LIGHT CHAIN; COMPND 22 CHAIN: D; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 6; COMPND 25 MOLECULE: ANTIBODY 35O22 FAB HEAVY CHAIN; COMPND 26 CHAIN: E; 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_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 GENE: ENV; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 MOL_ID: 6; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, ENVELOPE, ANTIBODY, VIRUS, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR G.B.E.STEWART-JONES,T.ZHOU,P.D.KWONG REVDAT 1 21-JUN-17 5V7J 0 JRNL AUTH T.ZHOU,N.A.DORIA-ROSE,C.CHENG,G.B.E.STEWART-JONES, JRNL AUTH 2 G.Y.CHUANG,M.CHAMBERS,A.DRUZ,H.GENG,K.MCKEE,Y.D.KWON, JRNL AUTH 3 S.O'DELL,M.SASTRY,S.D.SCHMIDT,K.XU,L.CHEN,R.E.CHEN, JRNL AUTH 4 M.K.LOUDER,M.PANCERA,T.G.WANNINGER,B.ZHANG,A.ZHENG, JRNL AUTH 5 S.K.FARNEY,K.E.FOULDS,I.S.GEORGIEV,M.G.JOYCE,T.LEMMIN, JRNL AUTH 6 S.NARPALA,R.RAWI,C.SOTO,J.P.TODD,C.H.SHEN,Y.TSYBOVSKY, JRNL AUTH 7 Y.YANG,P.ZHAO,B.F.HAYNES,L.STAMATATOS,M.TIEMEYER,L.WELLS, JRNL AUTH 8 D.G.SCORPIO,L.SHAPIRO,A.B.MCDERMOTT,J.R.MASCOLA,P.D.KWONG JRNL TITL QUANTIFICATION OF THE IMPACT OF THE HIV-1-GLYCAN SHIELD ON JRNL TITL 2 ANTIBODY ELICITATION. JRNL REF CELL REP V. 19 719 2017 JRNL REFN ESSN 2211-1247 JRNL PMID 28445724 JRNL DOI 10.1016/J.CELREP.2017.04.013 REMARK 2 REMARK 2 RESOLUTION. 2.91 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.11.1_2575 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.42 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460 REMARK 3 COMPLETENESS FOR RANGE (%) : 49.9 REMARK 3 NUMBER OF REFLECTIONS : 33547 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.330 REMARK 3 R VALUE (WORKING SET) : 0.316 REMARK 3 FREE R VALUE : 0.339 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.340 REMARK 3 FREE R VALUE TEST SET COUNT : 2128 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.7467 - 7.0599 0.85 4030 261 0.3219 0.3583 REMARK 3 2 7.0599 - 5.6087 0.89 4163 256 0.3431 0.3752 REMARK 3 3 5.6087 - 4.9012 0.90 4214 252 0.3320 0.3358 REMARK 3 4 4.9012 - 4.4537 0.89 4167 257 0.3040 0.3365 REMARK 3 5 4.4537 - 4.1348 0.79 3664 226 0.2984 0.3552 REMARK 3 6 4.1348 - 3.8913 0.62 2882 178 0.3073 0.3191 REMARK 3 7 3.8913 - 3.6965 0.49 2292 149 0.3384 0.3160 REMARK 3 8 3.6965 - 3.5357 0.37 1711 114 0.3706 0.3959 REMARK 3 9 3.5357 - 3.3997 0.30 1386 86 0.3905 0.4311 REMARK 3 10 3.3997 - 3.2824 0.21 976 64 0.3562 0.3962 REMARK 3 11 3.2824 - 3.1799 0.17 793 47 0.3651 0.4324 REMARK 3 12 3.1799 - 3.0890 0.13 626 41 0.3865 0.3904 REMARK 3 13 3.0890 - 3.0077 0.09 440 26 0.4469 0.3595 REMARK 3 14 3.0077 - 2.9343 0.04 207 15 0.6404 0.4449 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.040 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.013 12803 REMARK 3 ANGLE : 1.632 17571 REMARK 3 CHIRALITY : 0.072 2200 REMARK 3 PLANARITY : 0.010 2083 REMARK 3 DIHEDRAL : 7.649 7651 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5V7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-17. REMARK 100 THE DEPOSITION ID IS D_1000226996. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33547 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.907 REMARK 200 RESOLUTION RANGE LOW (A) : 41.423 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 51.3 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.8200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4TVP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 4.95% ISOPROPANOL, 8.25% PEG 3350, REMARK 280 0.2M AMMONIUM CITRATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 157.62000 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 157.62000 REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 157.62000 REMARK 290 REMARK 290 REMARK: NULL 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, B, L, H, D, E 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -131.16000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -65.58000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -113.58789 REMARK 350 BIOMT3 3 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 ASP G 149 REMARK 465 MET G 150 REMARK 465 ARG G 151 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLY L 2 REMARK 465 SER L 3 REMARK 465 VAL L 4 REMARK 465 THR L 5 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 LYS H 127 REMARK 465 LYS H 212 REMARK 465 SER H 213 REMARK 465 CYS H 214 REMARK 465 ASP H 215 REMARK 465 GLN E 1 REMARK 465 CYS E 215 REMARK 465 SER E 216 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASN G 137 CG OD1 ND2 REMARK 470 ILE G 215 CG1 CG2 CD1 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 G 385 SG CYS G 418 1.18 REMARK 500 ND2 ASN B 618 O5 NAG B 702 1.95 REMARK 500 OG SER E 13 O LEU E 110 1.96 REMARK 500 OD1 ASN G 392 C1 NAG G 1671 1.99 REMARK 500 O SER H 113 CE2 PHE H 144 2.01 REMARK 500 NH2 ARG L 54 O PHE L 62 2.05 REMARK 500 CG ASN G 392 C1 NAG G 1671 2.06 REMARK 500 NH1 ARG D 98 OG1 THR D 100C 2.06 REMARK 500 O LYS G 335 ND2 ASN G 339 2.09 REMARK 500 NH1 ARG L 54 O PRO L 59 2.10 REMARK 500 NZ LYS G 252 O ASN G 262 2.10 REMARK 500 OG1 THR G 303 O ASP G 321A 2.10 REMARK 500 O THR G 106 OG SER G 110 2.12 REMARK 500 OD1 ASP E 79 NH2 ARG E 81 2.14 REMARK 500 OD1 ASN B 618 N2 NAG B 702 2.15 REMARK 500 OD1 ASP E 84 OH TYR E 88 2.15 REMARK 500 O4 BMA G 1634 O6 MAN G 1636 2.15 REMARK 500 O VAL G 333 N ILE G 414 2.16 REMARK 500 O MET G 475 N ASN G 478 2.16 REMARK 500 O GLY H 132 N SER H 184 2.17 REMARK 500 O GLU B 647 N ASN B 651 2.17 REMARK 500 N ALA H 134 O VAL H 182 2.17 REMARK 500 O SER D 120 OH TYR D 145 2.17 REMARK 500 O THR B 639 CD1 TYR B 643 2.17 REMARK 500 O GLN G 422 N ALA G 436 2.17 REMARK 500 O ASP D 86 OH TYR D 90 2.18 REMARK 500 O ASP D 99 O6 MAN G 1610 2.18 REMARK 500 O PRO L 142 NE2 HIS L 198 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 CYS B 598 CB CYS B 598 SG -0.113 REMARK 500 CYS B 604 CB CYS B 604 SG -0.137 REMARK 500 CYS D 22 CB CYS D 22 SG -0.188 REMARK 500 GLU E 85 CA GLU E 85 C -0.163 REMARK 500 GLU E 187 CA GLU E 187 C -0.177 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 LEU G 226 CA - CB - CG ANGL. DEV. = -16.3 DEGREES REMARK 500 CYS G 445 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 SER L 20 CB - CA - C ANGL. DEV. = -12.3 DEGREES REMARK 500 CYS H 194 CA - CB - SG ANGL. DEV. = 13.3 DEGREES REMARK 500 CYS D 22 CA - CB - SG ANGL. DEV. = 12.2 DEGREES REMARK 500 LEU D 82C CA - CB - CG ANGL. DEV. = 17.2 DEGREES REMARK 500 LEU D 82C CB - CG - CD1 ANGL. DEV. = -18.9 DEGREES REMARK 500 LEU D 100E CA - CB - CG ANGL. DEV. = 21.5 DEGREES REMARK 500 LEU E 80 CB - CG - CD2 ANGL. DEV. = -11.4 DEGREES REMARK 500 GLU E 85 N - CA - C ANGL. DEV. = 22.4 DEGREES REMARK 500 THR E 86 OG1 - CB - CG2 ANGL. DEV. = -18.5 DEGREES REMARK 500 CYS E 90 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 LEU E 184 CA - CB - CG ANGL. DEV. = 14.6 DEGREES REMARK 500 TRP E 189 C - N - CA ANGL. DEV. = 16.6 DEGREES REMARK 500 CYS E 197 CA - CB - SG ANGL. DEV. = 7.7 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 G 47 104.29 -50.48 REMARK 500 ALA G 60 -71.72 -56.53 REMARK 500 THR G 63 -77.44 -66.30 REMARK 500 HIS G 66 78.83 59.72 REMARK 500 THR G 71 -127.43 48.29 REMARK 500 ASN G 88 39.82 28.01 REMARK 500 LEU G 122 70.59 -106.78 REMARK 500 PRO G 124 5.77 -67.11 REMARK 500 CYS G 126 1.85 -67.44 REMARK 500 VAL G 127 161.29 -49.16 REMARK 500 ASN G 136 149.37 -173.71 REMARK 500 ILE G 138 96.18 -64.53 REMARK 500 THR G 139 -73.21 -122.17 REMARK 500 LEU G 154 -179.52 -177.87 REMARK 500 ARG G 166 -73.62 -73.65 REMARK 500 ILE G 184 -55.92 -142.09 REMARK 500 TYR G 191 -168.36 -117.41 REMARK 500 ALA G 224 139.76 -173.88 REMARK 500 LYS G 229 42.36 -151.19 REMARK 500 THR G 248 152.48 -43.09 REMARK 500 GLN G 258 -0.87 77.41 REMARK 500 GLU G 268 -165.10 -177.21 REMARK 500 VAL G 270 55.27 70.64 REMARK 500 ASN G 276 104.90 -164.47 REMARK 500 PHE G 288 -167.46 -70.68 REMARK 500 ASN G 289 -30.61 -134.31 REMARK 500 PRO G 299 50.81 -97.86 REMARK 500 SER G 306 119.71 -31.43 REMARK 500 PRO G 313 94.69 -67.16 REMARK 500 LYS G 351 10.77 -65.32 REMARK 500 ASN G 356 24.50 -141.68 REMARK 500 PHE G 361 148.11 177.06 REMARK 500 ALA G 362 -165.24 -166.87 REMARK 500 HIS G 374 90.42 -64.14 REMARK 500 TYR G 384 83.63 -155.92 REMARK 500 GLN G 422 -31.43 -136.78 REMARK 500 TRP G 427 30.98 33.39 REMARK 500 PRO G 438 -170.20 -66.45 REMARK 500 VAL G 442 171.39 -57.20 REMARK 500 ARG G 444 116.82 -169.56 REMARK 500 SER G 460 -170.46 -173.81 REMARK 500 SER G 463 -5.58 63.33 REMARK 500 ALA G 464 -74.09 -68.20 REMARK 500 THR G 465 87.79 -151.65 REMARK 500 LYS G 487 119.76 -164.33 REMARK 500 PRO G 493 0.73 -66.65 REMARK 500 LYS G 502 136.18 -173.48 REMARK 500 THR B 536 54.23 -104.43 REMARK 500 SER B 546 95.19 -56.97 REMARK 500 LEU B 565 -80.21 -83.37 REMARK 500 REMARK 500 THIS ENTRY HAS 161 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR G 128 LEU G 129 -147.19 REMARK 500 SER G 158 PHE G 159 -148.25 REMARK 500 GLU G 492 PRO G 493 -145.79 REMARK 500 PHE L 119 PRO L 120 -147.93 REMARK 500 THR L 202 VAL L 203 148.98 REMARK 500 VAL L 203 GLU L 204 -149.44 REMARK 500 GLY H 100H GLU H 100I 140.33 REMARK 500 PHE H 100J PHE H 100K 141.55 REMARK 500 SER D 21 CYS D 22 -147.06 REMARK 500 SER D 100B THR D 100C -149.63 REMARK 500 PHE D 146 PRO D 147 -133.24 REMARK 500 VAL E 28 CYS E 29 148.48 REMARK 500 SER E 34 ILE E 35 -149.43 REMARK 500 TRP E 37 TYR E 38 -147.78 REMARK 500 CYS E 90 CYS E 91 -149.39 REMARK 500 PHE E 101 GLY E 102 -139.39 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 LEU D 96 12.03 REMARK 500 GLU E 187 -12.95 REMARK 500 GLN E 188 15.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG B 701 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 701 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 702 bound REMARK 800 to ASN B 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 703 through BMA B 705 bound to ASN B 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1607 through MAN G 1613 bound to ASN G 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1621 through BMA G 1623 bound to ASN G 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1624 through MAN G 1631 bound to ASN G 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1601 through MAN G 1606 bound to ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1639 through MAN G 1646 bound to ASN G 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1614 through MAN G 1620 bound to ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1647 through MAN G 1652 bound to ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1653 through MAN G 1662 bound to ASN G 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 1663 REMARK 800 bound to ASN G 356 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1673 through NAG G 1674 bound to ASN G 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1632 through MAN G 1638 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1664 through MAN G 1670 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 1671 through NAG G 1672 DBREF 5V7J G 32 508 UNP Q2N0S6 Q2N0S6_9HIV1 31 505 DBREF 5V7J B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 5V7J L 2 213 PDB 5V7J 5V7J 2 213 DBREF 5V7J H 1 215 PDB 5V7J 5V7J 1 215 DBREF 5V7J D 1 222 PDB 5V7J 5V7J 1 222 DBREF 5V7J E 1 216 PDB 5V7J 5V7J 1 216 SEQADV 5V7J ALA G 199 UNP Q2N0S6 SER 198 ENGINEERED MUTATION SEQADV 5V7J ALA G 278 UNP Q2N0S6 THR 277 ENGINEERED MUTATION SEQADV 5V7J ASN G 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 5V7J ALA G 365 UNP Q2N0S6 SER 363 ENGINEERED MUTATION SEQADV 5V7J ALA G 464 UNP Q2N0S6 THR 461 ENGINEERED MUTATION SEQADV 5V7J CYS G 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 5V7J ARG G 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 5V7J ARG G 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 5V7J ARG G 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 5V7J ARG G 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 5V7J ARG G 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 5V7J PRO B 559 UNP Q2N0S6 ILE 556 ENGINEERED MUTATION SEQADV 5V7J CYS B 605 UNP Q2N0S6 THR 602 ENGINEERED MUTATION SEQRES 1 G 480 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 G 480 TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER ASP SEQRES 3 G 480 ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA SEQRES 4 G 480 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 G 480 ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET TRP SEQRES 6 G 480 LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE ILE SEQRES 7 G 480 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 G 480 THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL THR SEQRES 9 G 480 ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS ASN SEQRES 10 G 480 CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS LYS SEQRES 11 G 480 GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL VAL SEQRES 12 G 480 GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SER SEQRES 13 G 480 ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR ALA ALA SEQRES 14 G 480 ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE SEQRES 15 G 480 PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU SEQRES 16 G 480 LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS SEQRES 17 G 480 PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS SEQRES 18 G 480 PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU SEQRES 19 G 480 ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE ALA SEQRES 20 G 480 ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR PRO SEQRES 21 G 480 VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG SEQRES 22 G 480 LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR ALA SEQRES 23 G 480 THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS SEQRES 24 G 480 ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS SEQRES 25 G 480 VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR SEQRES 26 G 480 ILE ILE ARG PHE ALA ASN SER ALA GLY GLY ASP LEU GLU SEQRES 27 G 480 VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 28 G 480 TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SEQRES 29 G 480 SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SER SEQRES 30 G 480 ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE SEQRES 31 G 480 ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA SEQRES 32 G 480 PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE SEQRES 33 G 480 THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SEQRES 34 G 480 SER ALA THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET SEQRES 35 G 480 ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL SEQRES 36 G 480 VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS SEQRES 37 G 480 LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 L 218 GLY SER VAL THR SER TYR VAL ARG PRO LEU SER VAL ALA SEQRES 2 L 218 LEU GLY GLU THR ALA SER ILE SER CYS GLY ARG GLN ALA SEQRES 3 L 218 LEU GLY SER ARG ALA VAL GLN TRP TYR GLN HIS ARG PRO SEQRES 4 L 218 GLY GLN ALA PRO ILE LEU LEU ILE TYR ASN ASN GLN ASP SEQRES 5 L 218 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY THR PRO SEQRES 6 L 218 ASP ILE ASN PHE GLY THR ARG ALA THR LEU THR ILE SER SEQRES 7 L 218 GLY VAL GLU ALA GLY ASP GLU ALA ASP TYR TYR CYS HIS SEQRES 8 L 218 MET TRP ASP SER ARG SER GLY PHE SER TRP SER PHE GLY SEQRES 9 L 218 GLY ALA THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10 L 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11 L 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12 L 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13 L 218 ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR SEQRES 14 L 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15 L 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SEQRES 16 L 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17 L 218 GLU LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 236 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 236 GLY SER ILE SER ASN TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 236 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 H 236 ASP SER GLU SER THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 236 ARG VAL ILE ILE SER VAL ASP THR SER LYS ASN GLN LEU SEQRES 7 H 236 SER LEU LYS LEU ASN SER VAL THR ALA ALA ASP SER ALA SEQRES 8 H 236 ILE TYR TYR CYS ALA ARG ALA GLN GLN GLY LYS ARG ILE SEQRES 9 H 236 TYR GLY MET VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 H 236 TYR MET ASP VAL TRP GLY LYS GLY THR THR VAL THR VAL SEQRES 11 H 236 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 236 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 H 236 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 236 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 H 236 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 236 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 236 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 236 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 H 236 CYS ASP SEQRES 1 D 240 GLU GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 D 240 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 240 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 D 240 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 D 240 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 D 240 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 D 240 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 D 240 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 D 240 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 D 240 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 D 240 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 D 240 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 D 240 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 D 240 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 D 240 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 D 240 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 D 240 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 D 240 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 19 D 240 ASP LYS GLY LEU GLU VAL SEQRES 1 E 216 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 E 216 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 E 216 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 E 216 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 E 216 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 E 216 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 E 216 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 E 216 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 E 216 THR LYS VAL SER VAL LEU GLY GLN SER LYS ALA ASN PRO SEQRES 10 E 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 E 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 E 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 E 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 E 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 E 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 E 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 E 216 THR VAL ALA PRO THR GLU CYS SER HET NAG G1601 14 HET NAG G1602 14 HET BMA G1603 11 HET MAN G1604 11 HET MAN G1605 11 HET MAN G1606 11 HET NAG G1607 14 HET NAG G1608 14 HET BMA G1609 11 HET MAN G1610 11 HET MAN G1611 11 HET MAN G1612 11 HET MAN G1613 11 HET NAG G1614 14 HET NAG G1615 14 HET BMA G1616 11 HET MAN G1617 11 HET MAN G1618 11 HET MAN G1619 11 HET MAN G1620 11 HET NAG G1621 14 HET NAG G1622 14 HET BMA G1623 11 HET NAG G1624 14 HET NAG G1625 14 HET BMA G1626 11 HET MAN G1627 11 HET MAN G1628 11 HET MAN G1629 11 HET MAN G1630 11 HET MAN G1631 11 HET NAG G1632 14 HET NAG G1633 14 HET BMA G1634 11 HET MAN G1635 11 HET MAN G1636 11 HET MAN G1637 11 HET MAN G1638 11 HET NAG G1639 14 HET NAG G1640 14 HET BMA G1641 11 HET MAN G1642 11 HET MAN G1643 11 HET MAN G1644 11 HET MAN G1645 11 HET MAN G1646 11 HET NAG G1647 14 HET NAG G1648 14 HET BMA G1649 11 HET MAN G1650 11 HET MAN G1651 11 HET MAN G1652 11 HET NAG G1653 14 HET NAG G1654 14 HET BMA G1655 11 HET MAN G1656 11 HET MAN G1657 11 HET MAN G1658 11 HET MAN G1659 11 HET MAN G1660 11 HET MAN G1661 11 HET MAN G1662 11 HET NAG G1663 14 HET NAG G1664 14 HET NAG G1665 14 HET BMA G1666 11 HET MAN G1667 11 HET MAN G1668 11 HET MAN G1669 11 HET MAN G1670 11 HET NAG G1671 14 HET NAG G1672 14 HET NAG G1673 14 HET NAG G1674 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET BMA B 705 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 7 NAG 29(C8 H15 N O6) FORMUL 7 BMA 11(C6 H12 O6) FORMUL 7 MAN 39(C6 H12 O6) HELIX 1 AA1 ASN G 99 LEU G 116 1 18 HELIX 2 AA2 TYR G 177 LEU G 179 5 3 HELIX 3 AA3 ASN G 195 THR G 198 5 4 HELIX 4 AA4 LYS G 335 ARG G 350 1 16 HELIX 5 AA5 LYS G 351 PHE G 353 5 3 HELIX 6 AA6 ASN G 425 ARG G 429 5 5 HELIX 7 AA7 ARG G 476 SER G 481 1 6 HELIX 8 AA8 THR B 529 THR B 536 1 8 HELIX 9 AA9 LEU B 537 SER B 546 1 10 HELIX 10 AB1 THR B 569 GLY B 597 1 29 HELIX 11 AB2 ASN B 611 SER B 615 5 5 HELIX 12 AB3 LEU B 619 ASP B 624 1 6 HELIX 13 AB4 TRP B 628 SER B 636 1 9 HELIX 14 AB5 TYR B 638 TYR B 643 1 6 HELIX 15 AB6 GLY B 644 SER B 649 1 6 HELIX 16 AB7 ASN B 656 ALA B 662 1 7 HELIX 17 AB8 GLU L 79 GLU L 83 5 5 HELIX 18 AB9 GLU L 125 ASN L 129 5 5 HELIX 19 AC1 THR L 182 HIS L 189 1 8 HELIX 20 AC2 ASN H 60 LYS H 64 5 5 HELIX 21 AC3 THR H 83 SER H 87 5 5 HELIX 22 AC4 MET H 100D GLY H 100H 5 5 HELIX 23 AC5 SER H 154 ALA H 156 5 3 HELIX 24 AC6 ALA D 60 GLN D 64 5 5 HELIX 25 AC7 LYS D 83 THR D 87 5 5 HELIX 26 AC8 TRP D 154 ALA D 158 5 5 HELIX 27 AC9 ASP D 217 VAL D 222 1 6 HELIX 28 AD1 ARG E 81 GLU E 85 5 5 HELIX 29 AD2 PRO E 186 LYS E 190 5 5 SHEET 1 AA1 3 LEU G 494 THR G 499 0 SHEET 2 AA1 3 TRP G 35 TYR G 40 -1 N THR G 37 O ALA G 497 SHEET 3 AA1 3 ILE B 603 CYS B 604 -1 O CYS B 604 N VAL G 38 SHEET 1 AA2 3 TRP G 45 ASP G 47 0 SHEET 2 AA2 3 VAL G 489 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AA2 3 PHE G 223 ALA G 224 -1 N ALA G 224 O VAL G 489 SHEET 1 AA3 2 PHE G 53 ALA G 55 0 SHEET 2 AA3 2 HIS G 216 CYS G 218 -1 O CYS G 218 N PHE G 53 SHEET 1 AA4 3 ILE G 84 LEU G 86 0 SHEET 2 AA4 3 VAL G 242 THR G 244 -1 O THR G 244 N ILE G 84 SHEET 3 AA4 3 LYS G 227 CYS G 228 -1 N LYS G 227 O SER G 243 SHEET 1 AA5 3 CYS G 131 ASN G 133 0 SHEET 2 AA5 3 LYS G 155 THR G 162 -1 O ASN G 156 N THR G 132 SHEET 3 AA5 3 LYS G 169 SER G 174 -1 O VAL G 172 N PHE G 159 SHEET 1 AA6 2 VAL G 181 GLN G 183 0 SHEET 2 AA6 2 TYR G 191 LEU G 193 -1 O ARG G 192 N VAL G 182 SHEET 1 AA7 3 LEU G 259 LEU G 261 0 SHEET 2 AA7 3 ILE G 449 ARG G 456 -1 O GLY G 451 N LEU G 260 SHEET 3 AA7 3 ILE G 284 GLN G 287 -1 N ILE G 284 O LEU G 454 SHEET 1 AA8 3 LEU G 259 LEU G 261 0 SHEET 2 AA8 3 ILE G 449 ARG G 456 -1 O GLY G 451 N LEU G 260 SHEET 3 AA8 3 PHE G 468 ARG G 469 -1 O ARG G 469 N THR G 455 SHEET 1 AA9 4 SER G 413 THR G 415 0 SHEET 2 AA9 4 HIS G 330 SER G 334 -1 N VAL G 333 O ILE G 414 SHEET 3 AA9 4 ASN G 295 THR G 297 -1 N THR G 297 O HIS G 330 SHEET 4 AA9 4 ARG G 444 CYS G 445 -1 O CYS G 445 N CYS G 296 SHEET 1 AB1 2 THR G 303 ARG G 308 0 SHEET 2 AB1 2 ALA G 316 GLY G 321 -1 O GLY G 321 N THR G 303 SHEET 1 AB2 2 HIS G 374 CYS G 378 0 SHEET 2 AB2 2 GLU G 381 CYS G 385 -1 O PHE G 383 N PHE G 376 SHEET 1 AB3 2 ILE G 423 ILE G 424 0 SHEET 2 AB3 2 MET G 434 TYR G 435 -1 O MET G 434 N ILE G 424 SHEET 1 AB4 2 SER L 12 ALA L 14 0 SHEET 2 AB4 2 THR L 105 LEU L 107 1 O LEU L 107 N VAL L 13 SHEET 1 AB5 3 GLN L 42 ILE L 45 0 SHEET 2 AB5 3 GLN L 37 ARG L 39 -1 N ARG L 39 O GLN L 42 SHEET 3 AB5 3 ASP L 85 TYR L 86 -1 O ASP L 85 N HIS L 38 SHEET 1 AB6 4 SER L 115 LEU L 118 0 SHEET 2 AB6 4 CYS L 135 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AB6 4 TYR L 173 TYR L 178 -1 O ALA L 175 N ILE L 137 SHEET 4 AB6 4 GLU L 161 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AB7 4 SER L 115 LEU L 118 0 SHEET 2 AB7 4 CYS L 135 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AB7 4 TYR L 173 TYR L 178 -1 O ALA L 175 N ILE L 137 SHEET 4 AB7 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AB8 3 SER L 154 PRO L 155 0 SHEET 2 AB8 3 VAL L 147 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AB8 3 TYR L 192 VAL L 196 -1 O GLN L 195 N ALA L 148 SHEET 1 AB9 4 GLN H 5 SER H 7 0 SHEET 2 AB9 4 LEU H 20 THR H 23 -1 O THR H 21 N SER H 7 SHEET 3 AB9 4 GLN H 77 LYS H 81 -1 O LEU H 80 N LEU H 20 SHEET 4 AB9 4 ILE H 68 ILE H 69 -1 N ILE H 68 O LYS H 81 SHEET 1 AC1 4 LYS H 43 TRP H 47 0 SHEET 2 AC1 4 TRP H 34 SER H 40 -1 N ARG H 38 O GLU H 46 SHEET 3 AC1 4 ALA H 88 GLY H 98 -1 O ALA H 93 N SER H 35 SHEET 4 AC1 4 TYR H 100M MET H 100P-1 O TYR H 100O N GLN H 96 SHEET 1 AC2 4 LYS H 43 TRP H 47 0 SHEET 2 AC2 4 TRP H 34 SER H 40 -1 N ARG H 38 O GLU H 46 SHEET 3 AC2 4 ALA H 88 GLY H 98 -1 O ALA H 93 N SER H 35 SHEET 4 AC2 4 THR H 105 VAL H 107 -1 O VAL H 107 N ALA H 88 SHEET 1 AC3 4 VAL H 119 LEU H 122 0 SHEET 2 AC3 4 THR H 133 VAL H 140 -1 O LEU H 139 N PHE H 120 SHEET 3 AC3 4 LEU H 176 PRO H 183 -1 O VAL H 182 N ALA H 134 SHEET 4 AC3 4 VAL H 161 PHE H 164 -1 N HIS H 162 O VAL H 179 SHEET 1 AC4 3 VAL H 150 TRP H 152 0 SHEET 2 AC4 3 ILE H 193 HIS H 198 -1 O ASN H 195 N SER H 151 SHEET 3 AC4 3 THR H 203 LYS H 208 -1 O VAL H 205 N VAL H 196 SHEET 1 AC5 4 GLN D 3 GLN D 6 0 SHEET 2 AC5 4 LYS D 19 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 AC5 4 TYR D 79 GLU D 81 -1 O MET D 80 N ILE D 20 SHEET 4 AC5 4 ILE D 68 THR D 70 -1 N THR D 70 O TYR D 79 SHEET 1 AC6 2 ILE D 37 THR D 40 0 SHEET 2 AC6 2 GLY D 44 TRP D 47 -1 O GLU D 46 N ARG D 38 SHEET 1 AC7 2 GLU D 72B THR D 72F 0 SHEET 2 AC7 2 THR D 73 GLY D 76 -1 O THR D 75 N VAL D 72C SHEET 1 AC8 4 LEU D 124 SER D 130 0 SHEET 2 AC8 4 THR D 135 CYS D 140 -1 O ALA D 137 N SER D 127 SHEET 3 AC8 4 SER D 180 PRO D 185 -1 O VAL D 184 N ALA D 136 SHEET 4 AC8 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AC9 2 THR E 5 GLN E 6 0 SHEET 2 AC9 2 CYS E 22 THR E 23 -1 O THR E 23 N THR E 5 SHEET 1 AD1 2 SER E 34 ILE E 35 0 SHEET 2 AD1 2 SER E 92 TYR E 93 -1 O TYR E 93 N SER E 34 SHEET 1 AD2 2 TYR E 38 GLN E 39 0 SHEET 2 AD2 2 TYR E 88 TYR E 89 -1 O TYR E 89 N TYR E 38 SHEET 1 AD3 2 ILE E 50 GLU E 52 0 SHEET 2 AD3 2 GLU E 55 ARG E 56 -1 O GLU E 55 N GLU E 52 SHEET 1 AD4 4 LEU E 121 PHE E 122 0 SHEET 2 AD4 4 THR E 135 CYS E 138 -1 O VAL E 137 N PHE E 122 SHEET 3 AD4 4 SER E 180 SER E 183 -1 O LEU E 182 N LEU E 136 SHEET 4 AD4 4 VAL E 163 THR E 165 -1 N GLU E 164 O TYR E 181 SHEET 1 AD5 2 ILE E 140 PHE E 143 0 SHEET 2 AD5 2 TYR E 176 ALA E 178 -1 O ALA E 178 N ILE E 140 SHEET 1 AD6 3 THR E 149 VAL E 150 0 SHEET 2 AD6 3 CYS E 197 THR E 200 -1 O THR E 200 N THR E 149 SHEET 3 AD6 3 THR E 205 LYS E 208 -1 O VAL E 206 N VAL E 199 SSBOND 1 CYS G 54 CYS G 74 1555 1555 2.23 SSBOND 2 CYS G 119 CYS G 205 1555 1555 2.01 SSBOND 3 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 4 CYS G 131 CYS G 157 1555 1555 2.06 SSBOND 5 CYS G 218 CYS G 247 1555 1555 2.02 SSBOND 6 CYS G 228 CYS G 239 1555 1555 2.04 SSBOND 7 CYS G 296 CYS G 331 1555 1555 2.07 SSBOND 8 CYS G 378 CYS G 445 1555 1555 2.00 SSBOND 9 CYS G 501 CYS B 605 1555 1555 2.08 SSBOND 10 CYS B 598 CYS B 604 1555 1555 1.99 SSBOND 11 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 12 CYS L 135 CYS L 194 1555 1555 2.07 SSBOND 13 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 14 CYS H 138 CYS H 194 1555 1555 2.09 SSBOND 15 CYS D 22 CYS D 92 1555 1555 2.01 SSBOND 16 CYS D 140 CYS D 196 1555 1555 2.04 SSBOND 17 CYS E 22 CYS E 90 1555 1555 2.01 SSBOND 18 CYS E 91 CYS E 99 1555 1555 2.01 SSBOND 19 CYS E 138 CYS E 197 1555 1555 2.05 LINK ND2 ASN G 88 C1 NAG G1607 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G1621 1555 1555 1.45 LINK ND2 ASN G 156 C1 NAG G1624 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG G1601 1555 1555 1.39 LINK ND2 ASN G 262 C1 NAG G1639 1555 1555 1.43 LINK ND2 ASN G 295 C1 NAG G1614 1555 1555 1.45 LINK ND2 ASN G 301 C1 NAG G1647 1555 1555 1.29 LINK ND2 ASN G 332 C1 NAG G1653 1555 1555 1.44 LINK ND2 ASN G 356 C1 NAG G1663 1555 1555 1.45 LINK ND2 ASN G 448 C1 NAG G1673 1555 1555 1.41 LINK ND2 ASN B 618 C1 NAG B 702 1555 1555 1.32 LINK ND2 ASN B 637 C1 NAG B 703 1555 1555 1.45 LINK O4 NAG G1601 C1 NAG G1602 1555 1555 1.52 LINK O4 NAG G1602 C1 BMA G1603 1555 1555 1.48 LINK O3 BMA G1603 C1 MAN G1604 1555 1555 1.44 LINK O6 BMA G1603 C1 MAN G1605 1555 1555 1.44 LINK O3 MAN G1605 C1 MAN G1606 1555 1555 1.44 LINK O4 NAG G1607 C1 NAG G1608 1555 1555 1.46 LINK O4 NAG G1608 C1 BMA G1609 1555 1555 1.46 LINK O3 BMA G1609 C1 MAN G1610 1555 1555 1.45 LINK O6 BMA G1609 C1 MAN G1611 1555 1555 1.46 LINK O3 MAN G1611 C1 MAN G1612 1555 1555 1.45 LINK O6 MAN G1611 C1 MAN G1613 1555 1555 1.45 LINK O4 NAG G1614 C1 NAG G1615 1555 1555 1.46 LINK O4 NAG G1615 C1 BMA G1616 1555 1555 1.45 LINK O3 BMA G1616 C1 MAN G1617 1555 1555 1.48 LINK O6 BMA G1616 C1 MAN G1618 1555 1555 1.44 LINK O2 MAN G1617 C1 MAN G1619 1555 1555 1.45 LINK O2 MAN G1619 C1 MAN G1620 1555 1555 1.44 LINK O4 NAG G1621 C1 NAG G1622 1555 1555 1.44 LINK O4 NAG G1622 C1 BMA G1623 1555 1555 1.44 LINK O4 NAG G1624 C1 NAG G1625 1555 1555 1.44 LINK O4 NAG G1625 C1 BMA G1626 1555 1555 1.44 LINK O3 BMA G1626 C1 MAN G1627 1555 1555 1.44 LINK O6 BMA G1626 C1 MAN G1628 1555 1555 1.44 LINK O2 MAN G1627 C1 MAN G1629 1555 1555 1.44 LINK O6 MAN G1628 C1 MAN G1630 1555 1555 1.45 LINK O2 MAN G1629 C1 MAN G1631 1555 1555 1.44 LINK O4 NAG G1632 C1 NAG G1633 1555 1555 1.44 LINK O4 NAG G1633 C1 BMA G1634 1555 1555 1.44 LINK O3 BMA G1634 C1 MAN G1635 1555 1555 1.45 LINK O6 BMA G1634 C1 MAN G1636 1555 1555 1.46 LINK O2 MAN G1635 C1 MAN G1637 1555 1555 1.44 LINK O2 MAN G1637 C1 MAN G1638 1555 1555 1.43 LINK O4 NAG G1639 C1 NAG G1640 1555 1555 1.44 LINK O4 NAG G1640 C1 BMA G1641 1555 1555 1.44 LINK O3 BMA G1641 C1 MAN G1642 1555 1555 1.45 LINK O6 BMA G1641 C1 MAN G1643 1555 1555 1.45 LINK O2 MAN G1642 C1 MAN G1644 1555 1555 1.45 LINK O6 MAN G1643 C1 MAN G1645 1555 1555 1.44 LINK O2 MAN G1644 C1 MAN G1646 1555 1555 1.44 LINK O4 NAG G1647 C1 NAG G1648 1555 1555 1.46 LINK O4 NAG G1648 C1 BMA G1649 1555 1555 1.46 LINK O6 BMA G1649 C1 MAN G1650 1555 1555 1.45 LINK O3 MAN G1650 C1 MAN G1651 1555 1555 1.44 LINK O2 MAN G1651 C1 MAN G1652 1555 1555 1.45 LINK O4 NAG G1653 C1 NAG G1654 1555 1555 1.45 LINK O4 NAG G1654 C1 BMA G1655 1555 1555 1.44 LINK O3 BMA G1655 C1 MAN G1656 1555 1555 1.44 LINK O6 BMA G1655 C1 MAN G1657 1555 1555 1.45 LINK O2 MAN G1656 C1 MAN G1658 1555 1555 1.45 LINK O3 MAN G1657 C1 MAN G1659 1555 1555 1.45 LINK O6 MAN G1657 C1 MAN G1660 1555 1555 1.44 LINK O2 MAN G1658 C1 MAN G1662 1555 1555 1.44 LINK O2 MAN G1660 C1 MAN G1661 1555 1555 1.45 LINK O4 NAG G1664 C1 NAG G1665 1555 1555 1.44 LINK O4 NAG G1665 C1 BMA G1666 1555 1555 1.43 LINK O3 BMA G1666 C1 MAN G1667 1555 1555 1.44 LINK O6 BMA G1666 C1 MAN G1668 1555 1555 1.45 LINK O3 MAN G1668 C1 MAN G1669 1555 1555 1.44 LINK O2 MAN G1669 C1 MAN G1670 1555 1555 1.43 LINK O4 NAG G1671 C1 NAG G1672 1555 1555 1.47 LINK O4 NAG G1673 C1 NAG G1674 1555 1555 1.44 LINK O4 NAG B 703 C1 NAG B 704 1555 1555 1.45 LINK O4 NAG B 704 C1 BMA B 705 1555 1555 1.44 LINK C1 NAG G1664 ND2 ASN G 386 1555 1555 1.60 LINK C1 NAG G1671 ND2 ASN G 392 1555 1555 1.65 LINK C1 NAG G1632 ND2 ASN G 234 1555 1555 1.80 CISPEP 1 ASN G 188 LYS G 189 0 -7.95 CISPEP 2 PHE B 519 LEU B 520 0 -13.49 CISPEP 3 TYR L 141 PRO L 142 0 -0.61 CISPEP 4 GLY H 131 GLY H 132 0 12.59 CISPEP 5 LEU H 187 GLY H 188 0 -0.33 CISPEP 6 GLU D 148 PRO D 149 0 -4.13 CISPEP 7 ALA E 131 ASN E 132 0 7.31 CISPEP 8 TYR E 144 PRO E 145 0 -6.49 SITE 1 AC1 1 ASN B 611 SITE 1 AC2 5 ASN B 616 ASN B 618 GLU E 55 ARG E 56 SITE 2 AC2 5 PRO E 58 SITE 1 AC3 2 GLU B 634 ASN B 637 SITE 1 AC4 19 SER B 528 ASN D 30 PHE D 31 HIS D 33 SITE 2 AC4 19 SER D 52 TYR D 53 ASP D 56 LYS D 57 SITE 3 AC4 19 ASN D 58 ARG D 98 ASP D 99 GLY D 100 SITE 4 AC4 19 SER D 100A THR D 100C HIS E 95 ASN E 96 SITE 5 AC4 19 LYS E 133 GLU G 87 ASN G 88 SITE 1 AC5 3 ASN G 133 ILE G 138 LYS G 189 SITE 1 AC6 8 THR G 135 ASN G 156 SER G 158 TYR G 173 SITE 2 AC6 8 GLY L 24 ARG L 25 GLN L 26 ARG L 70 SITE 1 AC7 3 ASN G 160 ASP G 167 LYS G 171 SITE 1 AC8 8 THR G 63 GLU G 64 SER G 209 ASN G 262 SITE 2 AC8 8 GLY G 379 VAL G 446 SER G 447 NAG G1673 SITE 1 AC9 5 GLN G 293 ASN G 295 ASN G 332 SER G 334 SITE 2 AC9 5 ARG G 444 SITE 1 AD1 3 ASN G 301 ILE G 323 VAL G 442 SITE 1 AD2 15 HIS G 330 ASN G 332 ASN G 411 ARG G 444 SITE 2 AD2 15 LYS H 99 ARG H 100 ILE H 100A GLY H 100C SITE 3 AD2 15 MET H 100D SER L 30 ASN L 50 GLN L 52 SITE 4 AD2 15 PRO L 66 ASP L 67 ILE L 67A SITE 1 AD3 4 GLY G 354 ASN G 355 ASN G 356 SER G 463 SITE 1 AD4 4 ASN G 262 PRO G 291 ASN G 448 NAG G1639 SITE 1 AD5 2 ASN G 234 ILE G 277 SITE 1 AD6 3 ASN G 386 SER G 388 NAG G1632 SITE 1 AD7 3 GLY G 389 ASN G 392 NAG G1664 CRYST1 131.160 131.160 315.240 90.00 90.00 120.00 P 63 6 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 0.007624 0.004402 0.000000 0.00000 SCALE2 0.000000 0.008804 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003172 0.00000