HEADER VIRAL PROTEIN 05-SEP-18 6MDT TITLE CRYSTAL STRUCTURE OF THE B41 SOSIP.664 ENV TRIMER WITH PGT124 AND TITLE 2 35O22 FABS, IN P63 SPACE GROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSMEMBRANE PROTEIN GP41; COMPND 3 CHAIN: B; COMPND 4 FRAGMENT: RESIDUES 516-668; COMPND 5 SYNONYM: TM; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: SURFACE PROTEIN GP120; COMPND 9 CHAIN: G; COMPND 10 FRAGMENT: RESIDUES 30-511; COMPND 11 SYNONYM: SU, GLYCOPROTEIN 120, GP120; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: 35O22 FAB HEAVY CHAIN; COMPND 15 CHAIN: D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: 35O22 FAB LIGHT CHAIN; COMPND 19 CHAIN: E; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: PGT124 FAB HEAVY CHAIN; COMPND 23 CHAIN: H; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: PGT124 FAB LIGHT CHAIN; COMPND 27 CHAIN: L; COMPND 28 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 VIRAL PROTEIN, HIV, ENVELOPE, GLYCOPROTEIN, PREFUSION TRIMER, GLYCAN, KEYWDS 2 HIV-1 GP120, HIV-1 GP41, N332 SUPERSITE, IMMUNE SYSTEM, NEUTRALIZING KEYWDS 3 ANTIBODIES, COMPLEX, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.KUMAR,A.SARKAR,I.A.WILSON REVDAT 1 27-FEB-19 6MDT 0 JRNL AUTH S.KUMAR,A.SARKAR,P.PUGACH,R.W.SANDERS,J.P.MOORE,A.B.WARD, JRNL AUTH 2 I.A.WILSON JRNL TITL CAPTURING THE INHERENT STRUCTURAL DYNAMICS OF THE HIV-1 JRNL TITL 2 ENVELOPE GLYCOPROTEIN FUSION PEPTIDE. JRNL REF NAT COMMUN V. 10 763 2019 JRNL REFN ESSN 2041-1723 JRNL PMID 30770829 JRNL DOI 10.1038/S41467-019-08738-5 REMARK 2 REMARK 2 RESOLUTION. 3.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12_2829) 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.96 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 28721 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.295 REMARK 3 R VALUE (WORKING SET) : 0.294 REMARK 3 FREE R VALUE : 0.311 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.730 REMARK 3 FREE R VALUE TEST SET COUNT : 1359 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 41.9580 - 8.2021 1.00 2762 155 0.2527 0.2646 REMARK 3 2 8.2021 - 6.5182 1.00 2715 157 0.2945 0.2981 REMARK 3 3 6.5182 - 5.6965 1.00 2771 117 0.2802 0.3499 REMARK 3 4 5.6965 - 5.1767 1.00 2733 138 0.2664 0.2766 REMARK 3 5 5.1767 - 4.8062 1.00 2736 135 0.2625 0.3021 REMARK 3 6 4.8062 - 4.5232 1.00 2735 128 0.2875 0.3273 REMARK 3 7 4.5232 - 4.2969 1.00 2728 127 0.3045 0.3366 REMARK 3 8 4.2969 - 4.1100 1.00 2758 132 0.3313 0.3248 REMARK 3 9 4.1100 - 3.9519 1.00 2744 137 0.3605 0.3609 REMARK 3 10 3.9519 - 3.8157 1.00 2680 133 0.4298 0.4395 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.800 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.870 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 : 0.004 12668 REMARK 3 ANGLE : 0.911 17372 REMARK 3 CHIRALITY : 0.067 2150 REMARK 3 PLANARITY : 0.004 2085 REMARK 3 DIHEDRAL : 12.152 7450 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 6MDT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-18. REMARK 100 THE DEPOSITION ID IS D_1000236729. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-FEB-17 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28747 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 10.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 9.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: 4R26, 5CEZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 73.28 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CALCIUM ACETATE, 0.1M MES (PH 6), REMARK 280 15%(V/V) PEG400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 277.15K 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 156.53550 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 156.53550 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 156.53550 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: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, D, E, H, L 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 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 ASN B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 ILE 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 ASN G 140A REMARK 465 SER G 140B REMARK 465 THR G 140C REMARK 465 ASN G 140D REMARK 465 ALA G 140E REMARK 465 THR G 140F REMARK 465 ILE G 140G REMARK 465 SER G 140H REMARK 465 ASP G 140I REMARK 465 TRP G 140J REMARK 465 GLU G 140K REMARK 465 LYS G 140L REMARK 465 MET G 140M REMARK 465 GLU G 140N REMARK 465 ASN G 185A REMARK 465 LYS G 185B REMARK 465 ASN G 185C REMARK 465 ASN G 185D REMARK 465 ILE G 185E REMARK 465 ASN G 185F REMARK 465 ASN G 185G REMARK 465 THR G 185H REMARK 465 ASN G 185I REMARK 465 ARG G 402 REMARK 465 THR G 403 REMARK 465 ASP G 404 REMARK 465 ASP G 405 REMARK 465 LEU D 223 REMARK 465 PHE D 224 REMARK 465 GLN D 225 REMARK 465 GLN E 1 REMARK 465 CYS E 215 REMARK 465 SER E 216 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 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 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 NE2 GLN L 52 C4 MAN L 308 1.62 REMARK 500 CD GLU B 621 O7 NAG B 702 1.88 REMARK 500 N GLU D 1 C8 NAG B 703 1.89 REMARK 500 OG SER G 264 OE1 GLU G 482 1.97 REMARK 500 N GLU D 1 O7 NAG B 703 1.98 REMARK 500 N GLU D 1 N2 NAG B 703 1.99 REMARK 500 OG1 THR H 129 OG1 THR H 133 2.00 REMARK 500 O4 NAG L 302 O5 BMA L 303 2.07 REMARK 500 CB GLU B 621 O7 NAG B 702 2.08 REMARK 500 ND2 ASN G 413 C1 NAG G 647 2.09 REMARK 500 O4 NAG L 302 C2 BMA L 303 2.12 REMARK 500 C2 MAN L 304 C1 MAN L 308 2.16 REMARK 500 CD GLN L 52 O4 MAN L 308 2.17 REMARK 500 O6 NAG L 302 O2 BMA L 303 2.17 REMARK 500 O4 NAG L 302 O2 BMA L 303 2.19 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 ALA H 85 N - CA - CB ANGL. DEV. = 11.4 DEGREES REMARK 500 GLN L 109 N - CA - C ANGL. DEV. = -16.4 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 ILE B 519 38.51 36.11 REMARK 500 LEU B 545 55.73 -142.74 REMARK 500 THR B 606 -168.18 -121.62 REMARK 500 ILE B 651 -44.00 60.38 REMARK 500 PRO G 43 78.07 -68.94 REMARK 500 LYS G 155 -167.50 57.41 REMARK 500 THR G 163 -168.47 -68.66 REMARK 500 THR G 198 -70.01 -87.70 REMARK 500 PHE G 210 38.58 -98.41 REMARK 500 GLN G 258 -110.76 54.20 REMARK 500 GLU G 268 -132.83 63.77 REMARK 500 ILE G 359 -155.42 -128.01 REMARK 500 ILE G 360 -166.67 -125.18 REMARK 500 SER G 364 80.24 63.59 REMARK 500 GLN G 422 -12.97 -140.53 REMARK 500 ASP G 461 -8.14 -152.26 REMARK 500 THR G 465 -118.04 43.95 REMARK 500 SER D 25 149.62 -172.93 REMARK 500 THR D 72F -162.78 -120.81 REMARK 500 ASP D 144 71.06 58.63 REMARK 500 GLN E 16 -162.47 -105.40 REMARK 500 CYS E 22 104.32 -162.62 REMARK 500 ASP E 53 -124.18 68.64 REMARK 500 ASP E 79 71.21 52.40 REMARK 500 THR E 86 -158.77 -158.65 REMARK 500 THR E 94 -167.51 -114.26 REMARK 500 ALA E 147 87.66 61.04 REMARK 500 GLU H 55 78.03 56.14 REMARK 500 THR H 58 118.66 -164.58 REMARK 500 PHE H 100G 42.80 -98.56 REMARK 500 LYS H 141 -176.89 -67.73 REMARK 500 HIS H 162 89.57 -155.13 REMARK 500 TYR L 7 -166.71 -108.11 REMARK 500 ARG L 25 68.01 34.65 REMARK 500 ASP L 67 64.33 -107.53 REMARK 500 GLU L 79 -167.60 -123.99 REMARK 500 ALA L 84 -169.71 -166.70 REMARK 500 PRO L 142 98.25 -62.41 REMARK 500 ALA L 144 67.57 -155.02 REMARK 500 ASP L 152 -123.20 58.21 REMARK 500 LYS L 157 -10.36 72.32 REMARK 500 GLN L 168 -168.84 -114.41 REMARK 500 GLU L 199 -125.62 60.80 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 702 REMARK 610 NAG G 620 REMARK 610 NAG G 647 REMARK 610 NAG L 301 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 707 bound REMARK 800 to ASN B 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 701 bound REMARK 800 to ASN B 616 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 708 bound REMARK 800 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 800 601 through MAN G 607 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 800 608 through NAG G 609 bound to ASN G 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 610 bound REMARK 800 to ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 611 bound REMARK 800 to ASN G 197 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 800 612 through MAN G 616 bound to ASN G 234 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 800 617 through BMA G 619 bound to ASN G 241 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 625 bound REMARK 800 to ASN G 276 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 800 626 through BMA G 628 bound to ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 629 through MAN G 632 bound to ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 633 bound REMARK 800 to ASN G 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 654 bound REMARK 800 to ASN G 355 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 800 634 through BMA G 636 bound to ASN G 362 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 800 637 through MAN G 640 bound to ASN G 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLU G REMARK 800 411 through MAN G 645 bound to ASN G 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 646 bound REMARK 800 to ASN G 396 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 651 through BMA G 653 bound to ASN G 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLU D REMARK 800 1 through MAN B 706 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-Saccharide NAG B 702 and NAG REMARK 800 B 703 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-Saccharide NAG B 703 and GLU REMARK 800 D 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-Saccharide NAG B 703 and BMA REMARK 800 B 704 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-Saccharide BMA B 704 and MAN REMARK 800 B 706 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 620 through MAN G 624 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 647 through MAN G 650 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLN L REMARK 800 52 through MAN L 309 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6MCO RELATED DB: PDB REMARK 900 6MCO CONTAINS SAME PROTEIN COMPLEX IN P23 SPACE GROUP DBREF 6MDT B 512 664 UNP B3UES2 B3UES2_9HIV1 516 668 DBREF 6MDT G 32 507 UNP B3UF58 B3UF58_9HIV1 30 511 DBREF 6MDT D 1 225 PDB 6MDT 6MDT 1 225 DBREF 6MDT E 1 216 PDB 6MDT 6MDT 1 216 DBREF 6MDT H 1 215 PDB 6MDT 6MDT 1 215 DBREF 6MDT L 6 213 PDB 6MDT 6MDT 6 213 SEQADV 6MDT CYS B 605 UNP B3UES2 THR 609 CONFLICT SEQADV 6MDT CYS G 501 UNP B3UF58 ALA 505 CONFLICT SEQRES 1 B 153 ALA VAL GLY LEU GLY ALA PHE ILE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET ALA LEU SEQRES 3 B 153 THR VAL GLN ALA ARG LEU LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN ASN ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 B 153 HIS MET LEU GLN 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 ILE SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN ASP SER TRP SER SEQRES 9 B 153 ASN LYS THR ILE ASN GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 MET GLN TRP GLU LYS GLU ILE ASP ASN TYR THR GLN HIS SEQRES 11 B 153 ILE TYR THR LEU LEU GLU VAL SER GLN ILE GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 G 482 ALA LYS LYS TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 G 482 TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER ASP SEQRES 3 G 482 ALA LYS ALA TYR ASP THR GLU VAL HIS ASN VAL TRP ALA SEQRES 4 G 482 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 G 482 ILE VAL LEU GLY ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 G 482 LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SEQRES 7 G 482 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 G 482 THR PRO LEU CYS VAL THR LEU ASN CYS ASN ASN VAL ASN SEQRES 9 G 482 THR ASN ASN THR ASN ASN SER THR ASN ALA THR ILE SER SEQRES 10 G 482 ASP TRP GLU LYS MET GLU THR GLY GLU MET LYS ASN CYS SEQRES 11 G 482 SER PHE ASN VAL THR THR SER ILE ARG ASP LYS ILE LYS SEQRES 12 G 482 LYS GLU TYR ALA LEU PHE TYR LYS LEU ASP VAL VAL PRO SEQRES 13 G 482 LEU GLU ASN LYS ASN ASN ILE ASN ASN THR ASN ILE THR SEQRES 14 G 482 ASN TYR ARG LEU ILE ASN CYS ASN THR SER VAL ILE THR SEQRES 15 G 482 GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 16 G 482 HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 17 G 482 ASN SER LYS THR PHE ASN GLY SER GLY PRO CYS THR ASN SEQRES 18 G 482 VAL SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL SEQRES 19 G 482 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 20 G 482 GLU GLU ILE VAL ILE ARG SER GLU ASN ILE THR ASP ASN SEQRES 21 G 482 ALA LYS THR ILE ILE VAL GLN LEU ASN GLU ALA VAL GLU SEQRES 22 G 482 ILE ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER SEQRES 23 G 482 ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR ALA THR GLY SEQRES 24 G 482 ASP ILE ILE GLY ASN ILE ARG GLN ALA HIS CYS ASN ILE SEQRES 25 G 482 SER LYS ALA ARG TRP ASN GLU THR LEU GLY GLN ILE VAL SEQRES 26 G 482 ALA LYS LEU GLU GLU GLN PHE PRO ASN LYS THR ILE ILE SEQRES 27 G 482 PHE ASN HIS SER SER GLY GLY ASP PRO GLU ILE VAL THR SEQRES 28 G 482 HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN SEQRES 29 G 482 THR THR PRO LEU PHE ASN SER THR TRP ASN ASN THR ARG SEQRES 30 G 482 THR ASP ASP TYR PRO THR GLY GLY GLU GLN ASN ILE THR SEQRES 31 G 482 LEU GLN CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN SEQRES 32 G 482 GLY VAL GLY LYS ALA MET TYR ALA PRO PRO ILE ARG GLY SEQRES 33 G 482 GLN ILE ARG CYS SER SER ASN ILE THR GLY LEU LEU LEU SEQRES 34 G 482 THR ARG ASP GLY GLY ARG ASP GLN ASN GLY THR GLU THR SEQRES 35 G 482 PHE ARG PRO GLY GLY GLY ASN MET ARG ASP ASN TRP ARG SEQRES 36 G 482 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 37 G 482 LEU GLY ILE ALA PRO THR ALA CYS LYS ARG ARG VAL VAL SEQRES 38 G 482 GLN SEQRES 1 D 243 GLU GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 D 243 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 243 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 D 243 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 D 243 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 D 243 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 D 243 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 D 243 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 D 243 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 D 243 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 D 243 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 D 243 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 D 243 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 D 243 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 D 243 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 D 243 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 D 243 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 D 243 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 19 D 243 ASP LYS GLY LEU GLU VAL LEU PHE GLN 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 SEQRES 1 H 236 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 H 236 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 H 236 GLY SER ILE SER ASN TYR TYR TRP THR 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 ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 H 236 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 H 236 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 H 236 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 H 236 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 H 236 TYR MET ASP VAL TRP GLY LYS GLY THR ALA 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 L 214 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 L 214 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 L 214 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 L 214 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 L 214 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 L 214 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 L 214 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 L 214 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 L 214 LEU THR VAL LEU SER GLN PRO LYS ALA ALA PRO SER VAL SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL SEQRES 17 L 214 ALA PRO THR GLU CYS SER HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET BMA B 704 11 HET MAN B 705 11 HET MAN B 706 11 HET NAG B 707 14 HET NAG B 708 14 HET NAG G 601 14 HET NAG G 602 14 HET BMA G 603 11 HET MAN G 604 11 HET MAN G 605 11 HET MAN G 606 11 HET MAN G 607 11 HET NAG G 608 14 HET NAG G 609 14 HET NAG G 610 14 HET NAG G 611 14 HET NAG G 612 14 HET NAG G 613 14 HET BMA G 614 11 HET MAN G 615 11 HET MAN G 616 11 HET NAG G 617 14 HET NAG G 618 14 HET BMA G 619 11 HET NAG G 620 14 HET NAG G 621 14 HET BMA G 622 11 HET MAN G 623 11 HET MAN G 624 11 HET NAG G 625 14 HET NAG G 626 14 HET NAG G 627 14 HET BMA G 628 11 HET NAG G 629 14 HET NAG G 630 14 HET BMA G 631 11 HET MAN G 632 11 HET NAG G 633 14 HET NAG G 634 14 HET NAG G 635 14 HET BMA G 636 11 HET NAG G 637 14 HET NAG G 638 14 HET BMA G 639 11 HET MAN G 640 11 HET NAG G 641 14 HET NAG G 642 14 HET BMA G 643 11 HET MAN G 644 11 HET MAN G 645 11 HET NAG G 646 14 HET NAG G 647 14 HET NAG G 648 14 HET BMA G 649 11 HET MAN G 650 11 HET NAG G 651 14 HET NAG G 652 14 HET BMA G 653 11 HET NAG G 654 14 HET NAG L 301 14 HET NAG L 302 14 HET BMA L 303 11 HET MAN L 304 11 HET MAN L 305 11 HET MAN L 306 11 HET MAN L 307 11 HET MAN L 308 11 HET MAN L 309 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 7 NAG 37(C8 H15 N O6) FORMUL 8 BMA 13(C6 H12 O6) FORMUL 8 MAN 21(C6 H12 O6) HELIX 1 AA1 THR B 529 SER B 534 1 6 HELIX 2 AA2 THR B 538 LEU B 543 1 6 HELIX 3 AA3 LEU B 544 VAL B 549 5 6 HELIX 4 AA4 THR B 569 ILE B 595 1 27 HELIX 5 AA5 THR B 618 MET B 626 1 9 HELIX 6 AA6 THR B 627 ASP B 636 1 10 HELIX 7 AA7 TYR B 638 GLN B 650 1 13 HELIX 8 AA8 ILE B 651 GLU B 662 1 12 HELIX 9 AA9 ASN G 98 LYS G 117 1 20 HELIX 10 AB1 THR G 123 VAL G 127 5 5 HELIX 11 AB2 TYR G 177 LEU G 179 5 3 HELIX 12 AB3 LYS G 335 GLN G 352 1 18 HELIX 13 AB4 ASP G 368 THR G 373 1 6 HELIX 14 AB5 ASN G 425 GLY G 429 5 5 HELIX 15 AB6 ARG G 476 SER G 481 1 6 HELIX 16 AB7 LYS D 83 THR D 87 5 5 HELIX 17 AB8 SER D 156 ALA D 158 5 3 HELIX 18 AB9 LYS D 201 ASN D 204 5 4 HELIX 19 AC1 ASP D 217 VAL D 222 1 6 HELIX 20 AC2 PRO E 25 CYS E 29 5 5 HELIX 21 AC3 ARG E 81 GLU E 85 5 5 HELIX 22 AC4 SER E 125 ALA E 131 1 7 HELIX 23 AC5 THR E 185 SER E 191 1 7 HELIX 24 AC6 THR H 129 GLY H 131 5 3 HELIX 25 AC7 GLU L 79 GLU L 83 5 5 HELIX 26 AC8 SER L 122 ALA L 128 1 7 HELIX 27 AC9 THR L 182 HIS L 189 1 8 SHEET 1 AA1 3 ILE B 603 PRO B 609 0 SHEET 2 AA1 3 TRP G 35 TYR G 40 -1 O VAL G 36 N VAL B 608 SHEET 3 AA1 3 LEU G 494 THR G 499 -1 O THR G 499 N TRP G 35 SHEET 1 AA2 5 TRP G 45 LYS G 46 0 SHEET 2 AA2 5 TYR G 486 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AA2 5 PHE G 223 LYS G 227 -1 N LEU G 226 O LYS G 487 SHEET 4 AA2 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AA2 5 GLU G 83 LEU G 86 -1 N ILE G 84 O THR G 244 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 2 GLU G 91 ASN G 94 0 SHEET 2 AA4 2 SER G 236 CYS G 239 -1 O GLY G 237 N PHE G 93 SHEET 1 AA5 5 ILE G 169 ALA G 174 0 SHEET 2 AA5 5 ASN G 156 THR G 162 -1 N CYS G 157 O ALA G 174 SHEET 3 AA5 5 LEU G 129 ASN G 132 -1 N ASN G 130 O SER G 158 SHEET 4 AA5 5 ASN G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 AA5 5 VAL G 181 GLU G 185 -1 N VAL G 182 O ARG G 192 SHEET 1 AA6 3 ILE G 201 GLN G 203 0 SHEET 2 AA6 3 ALA G 433 TYR G 435 1 O ALA G 433 N THR G 202 SHEET 3 AA6 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AA7 4 LEU G 260 LEU G 261 0 SHEET 2 AA7 4 GLY G 441 LEU G 454 -1 O GLY G 451 N LEU G 260 SHEET 3 AA7 4 ILE G 284 ASN G 302 -1 N ILE G 294 O SER G 447 SHEET 4 AA7 4 VAL G 271 SER G 274 -1 N ARG G 273 O ILE G 285 SHEET 1 AA8 7 LEU G 260 LEU G 261 0 SHEET 2 AA8 7 GLY G 441 LEU G 454 -1 O GLY G 451 N LEU G 260 SHEET 3 AA8 7 ILE G 284 ASN G 302 -1 N ILE G 294 O SER G 447 SHEET 4 AA8 7 HIS G 330 SER G 334 -1 O ASN G 332 N ASN G 295 SHEET 5 AA8 7 ASN G 413 LYS G 421 -1 O ILE G 414 N ILE G 333 SHEET 6 AA8 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AA8 7 HIS G 374 CYS G 378 -1 N HIS G 374 O CYS G 385 SHEET 1 AA9 2 ARG G 304 GLY G 312 0 SHEET 2 AA9 2 ARG G 315 THR G 320 -1 O ALA G 319 N LYS G 305 SHEET 1 AB1 4 GLN D 3 GLN D 6 0 SHEET 2 AB1 4 SER D 17 TYR D 27 -1 O LYS D 23 N VAL D 5 SHEET 3 AB1 4 SER D 74 ARG D 82A-1 O MET D 80 N ILE D 20 SHEET 4 AB1 4 VAL D 67 THR D 71 -1 N THR D 70 O TYR D 79 SHEET 1 AB2 4 GLN D 3 GLN D 6 0 SHEET 2 AB2 4 SER D 17 TYR D 27 -1 O LYS D 23 N VAL D 5 SHEET 3 AB2 4 SER D 74 ARG D 82A-1 O MET D 80 N ILE D 20 SHEET 4 AB2 4 VAL D 72C PRO D 72D-1 N VAL D 72C O THR D 75 SHEET 1 AB3 6 GLU D 10 LYS D 12 0 SHEET 2 AB3 6 THR D 107 VAL D 111 1 O THR D 110 N LYS D 12 SHEET 3 AB3 6 GLY D 88 LYS D 94 -1 N TYR D 90 O THR D 107 SHEET 4 AB3 6 ILE D 34 THR D 40 -1 N ILE D 37 O PHE D 91 SHEET 5 AB3 6 GLY D 44 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB3 6 LYS D 57 LEU D 59 -1 O ASN D 58 N TRP D 50 SHEET 1 AB4 4 GLU D 10 LYS D 12 0 SHEET 2 AB4 4 THR D 107 VAL D 111 1 O THR D 110 N LYS D 12 SHEET 3 AB4 4 GLY D 88 LYS D 94 -1 N TYR D 90 O THR D 107 SHEET 4 AB4 4 LEU D 102 TRP D 103 -1 O LEU D 102 N LYS D 94 SHEET 1 AB5 4 PHE D 122 SER D 130 0 SHEET 2 AB5 4 THR D 135 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AB5 4 TYR D 176 PRO D 185 -1 O VAL D 182 N LEU D 138 SHEET 4 AB5 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AB6 4 PHE D 122 SER D 130 0 SHEET 2 AB6 4 THR D 135 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AB6 4 TYR D 176 PRO D 185 -1 O VAL D 182 N LEU D 138 SHEET 4 AB6 4 VAL D 169 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AB7 3 THR D 151 TRP D 154 0 SHEET 2 AB7 3 ILE D 195 HIS D 200 -1 O ASN D 197 N SER D 153 SHEET 3 AB7 3 THR D 205 ARG D 210 -1 O VAL D 207 N VAL D 198 SHEET 1 AB8 4 THR E 5 GLN E 6 0 SHEET 2 AB8 4 SER E 17 THR E 23 -1 O THR E 23 N THR E 5 SHEET 3 AB8 4 SER E 72 SER E 78 -1 O ILE E 77 N VAL E 18 SHEET 4 AB8 4 PHE E 64 LYS E 68 -1 N TYR E 67 O TYR E 74 SHEET 1 AB9 5 SER E 9 SER E 13 0 SHEET 2 AB9 5 THR E 105 LEU E 110 1 O LEU E 110 N GLY E 12 SHEET 3 AB9 5 THR E 87 TYR E 93 -1 N TYR E 88 O THR E 105 SHEET 4 AB9 5 SER E 34 GLN E 39 -1 N TYR E 38 O TYR E 89 SHEET 5 AB9 5 THR E 47 ILE E 50 -1 O THR E 47 N GLN E 39 SHEET 1 AC1 4 SER E 9 SER E 13 0 SHEET 2 AC1 4 THR E 105 LEU E 110 1 O LEU E 110 N GLY E 12 SHEET 3 AC1 4 THR E 87 TYR E 93 -1 N TYR E 88 O THR E 105 SHEET 4 AC1 4 VAL E 100 PHE E 101 -1 O VAL E 100 N SER E 92 SHEET 1 AC2 4 SER E 118 PHE E 122 0 SHEET 2 AC2 4 ALA E 134 SER E 141 -1 O LEU E 139 N THR E 120 SHEET 3 AC2 4 TYR E 176 LEU E 184 -1 O LEU E 184 N ALA E 134 SHEET 4 AC2 4 VAL E 163 THR E 165 -1 N GLU E 164 O TYR E 181 SHEET 1 AC3 4 SER E 118 PHE E 122 0 SHEET 2 AC3 4 ALA E 134 SER E 141 -1 O LEU E 139 N THR E 120 SHEET 3 AC3 4 TYR E 176 LEU E 184 -1 O LEU E 184 N ALA E 134 SHEET 4 AC3 4 SER E 169 LYS E 170 -1 N SER E 169 O ALA E 177 SHEET 1 AC4 3 THR E 149 ALA E 154 0 SHEET 2 AC4 3 TYR E 195 THR E 200 -1 O GLN E 198 N ALA E 151 SHEET 3 AC4 3 THR E 205 VAL E 210 -1 O VAL E 210 N TYR E 195 SHEET 1 AC5 4 LEU H 4 SER H 7 0 SHEET 2 AC5 4 LEU H 18 VAL H 24 -1 O ILE H 23 N GLN H 5 SHEET 3 AC5 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AC5 4 ALA H 67 ARG H 71 -1 N SER H 70 O SER H 79 SHEET 1 AC6 6 LEU H 11 VAL H 12 0 SHEET 2 AC6 6 THR H 105 VAL H 109 1 O THR H 108 N VAL H 12 SHEET 3 AC6 6 ALA H 88 ILE H 100A-1 N TYR H 90 O THR H 105 SHEET 4 AC6 6 TYR H 33 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 AC6 6 LEU H 45 ILE H 51 -1 O ILE H 51 N TRP H 34 SHEET 6 AC6 6 THR H 57 TYR H 59 -1 O THR H 58 N TYR H 50 SHEET 1 AC7 4 LEU H 11 VAL H 12 0 SHEET 2 AC7 4 THR H 105 VAL H 109 1 O THR H 108 N VAL H 12 SHEET 3 AC7 4 ALA H 88 ILE H 100A-1 N TYR H 90 O THR H 105 SHEET 4 AC7 4 PHE H 100J TRP H 101 -1 O TYR H 100M N GLY H 98 SHEET 1 AC8 4 VAL H 119 LEU H 122 0 SHEET 2 AC8 4 THR H 133 TYR H 143 -1 O LEU H 139 N PHE H 120 SHEET 3 AC8 4 TYR H 174 PRO H 183 -1 O TYR H 174 N TYR H 143 SHEET 4 AC8 4 VAL H 161 THR H 163 -1 N HIS H 162 O VAL H 179 SHEET 1 AC9 4 VAL H 119 LEU H 122 0 SHEET 2 AC9 4 THR H 133 TYR H 143 -1 O LEU H 139 N PHE H 120 SHEET 3 AC9 4 TYR H 174 PRO H 183 -1 O TYR H 174 N TYR H 143 SHEET 4 AC9 4 VAL H 167 LEU H 168 -1 N VAL H 167 O SER H 175 SHEET 1 AD1 3 THR H 149 TRP H 152 0 SHEET 2 AD1 3 ILE H 193 HIS H 198 -1 O ASN H 195 N SER H 151 SHEET 3 AD1 3 THR H 203 LYS H 208 -1 O VAL H 205 N VAL H 196 SHEET 1 AD2 5 SER L 9 ALA L 14 0 SHEET 2 AD2 5 THR L 102 LEU L 107 1 O LEU L 107 N VAL L 13 SHEET 3 AD2 5 ASP L 85 HIS L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AD2 5 GLN L 34 HIS L 38 -1 N HIS L 38 O ASP L 85 SHEET 5 AD2 5 ILE L 45 ILE L 48 -1 O ILE L 45 N GLN L 37 SHEET 1 AD3 3 ALA L 19 ILE L 21 0 SHEET 2 AD3 3 LEU L 73 ILE L 75 -1 O ILE L 75 N ALA L 19 SHEET 3 AD3 3 PHE L 62 GLY L 64 -1 N SER L 63 O THR L 74 SHEET 1 AD4 4 SER L 115 PHE L 119 0 SHEET 2 AD4 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AD4 4 TYR L 173 LEU L 181 -1 O LEU L 181 N ALA L 131 SHEET 4 AD4 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AD5 4 SER L 115 PHE L 119 0 SHEET 2 AD5 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AD5 4 TYR L 173 LEU L 181 -1 O LEU L 181 N ALA L 131 SHEET 4 AD5 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AD6 4 SER L 154 PRO L 155 0 SHEET 2 AD6 4 VAL L 145 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AD6 4 TYR L 192 HIS L 198 -1 O SER L 193 N LYS L 150 SHEET 4 AD6 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196 SSBOND 1 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 2 CYS B 605 CYS G 501 1555 1555 2.04 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.04 SSBOND 4 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 5 CYS G 126 CYS G 196 1555 1555 2.04 SSBOND 6 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 7 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 8 CYS G 228 CYS G 239 1555 1555 2.04 SSBOND 9 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 10 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 11 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 12 CYS D 140 CYS D 196 1555 1555 2.04 SSBOND 13 CYS E 22 CYS E 90 1555 1555 2.04 SSBOND 14 CYS E 91 CYS E 99 1555 1555 2.03 SSBOND 15 CYS E 138 CYS E 197 1555 1555 2.03 SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 17 CYS H 138 CYS H 194 1555 1555 2.03 SSBOND 18 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 19 CYS L 135 CYS L 194 1555 1555 2.04 SSBOND 20 CYS G 296 CYS G 331 1555 1555 1.50 LINK ND2 ASN B 611 C1 NAG B 707 1555 1555 1.44 LINK ND2 ASN B 616 C1 NAG B 701 1555 1555 1.44 LINK CG GLU B 621 O7 NAG B 702 1555 1555 1.37 LINK ND2 ASN B 637 C1 NAG B 708 1555 1555 1.45 LINK ND2 ASN G 88 C1 NAG G 601 1555 1555 1.43 LINK ND2 ASN G 156 C1 NAG G 608 1555 1555 1.45 LINK ND2 ASN G 160 C1 NAG G 610 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG G 611 1555 1555 1.45 LINK ND2 ASN G 234 C1 NAG G 612 1555 1555 1.44 LINK ND2 ASN G 241 C1 NAG G 617 1555 1555 1.42 LINK ND2 ASN G 276 C1 NAG G 625 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG G 626 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 629 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G 633 1555 1555 1.44 LINK ND2 ASN G 355 C1 NAG G 654 1555 1555 1.47 LINK ND2 ASN G 362 C1 NAG G 634 1555 1555 1.46 LINK ND2 ASN G 386 C1 NAG G 637 1555 1555 1.45 LINK ND2 ASN G 392 C1 NAG G 641 1555 1555 1.44 LINK ND2 ASN G 396 C1 NAG G 646 1555 1555 1.44 LINK N GLU G 411 O7 NAG G 642 1555 1555 1.30 LINK ND2 ASN G 448 C1 NAG G 651 1555 1555 1.44 LINK N GLU D 1 C7 NAG B 703 1555 1555 1.44 LINK NE2 GLN L 52 O4 MAN L 308 1555 1555 1.30 LINK O4 NAG B 702 C1 NAG B 703 1555 1555 1.46 LINK O4 NAG B 703 C1 BMA B 704 1555 1555 1.47 LINK O3 BMA B 704 C1 MAN B 706 1555 1555 1.46 LINK O6 BMA B 704 C1 MAN B 705 1555 1555 1.44 LINK O4 NAG G 601 C1 NAG G 602 1555 1555 1.44 LINK O4 NAG G 602 C1 BMA G 603 1555 1555 1.44 LINK O3 BMA G 603 C1 MAN G 604 1555 1555 1.44 LINK O6 BMA G 603 C1 MAN G 605 1555 1555 1.45 LINK O2 MAN G 605 C1 MAN G 607 1555 1555 1.47 LINK O6 MAN G 605 C1 MAN G 606 1555 1555 1.45 LINK O4 NAG G 608 C1 NAG G 609 1555 1555 1.45 LINK O4 NAG G 612 C1 NAG G 613 1555 1555 1.45 LINK O4 NAG G 613 C1 BMA G 614 1555 1555 1.45 LINK O3 BMA G 614 C1 MAN G 616 1555 1555 1.44 LINK O6 BMA G 614 C1 MAN G 615 1555 1555 1.44 LINK O4 NAG G 617 C1 NAG G 618 1555 1555 1.43 LINK O4 NAG G 618 C1 BMA G 619 1555 1555 1.44 LINK O4 NAG G 620 C1 NAG G 621 1555 1555 1.44 LINK O4 NAG G 621 C1 BMA G 622 1555 1555 1.43 LINK O3 BMA G 622 C1 MAN G 624 1555 1555 1.45 LINK O6 BMA G 622 C1 MAN G 623 1555 1555 1.46 LINK O4 NAG G 626 C1 NAG G 627 1555 1555 1.44 LINK O4 NAG G 627 C1 BMA G 628 1555 1555 1.45 LINK O4 NAG G 629 C1 NAG G 630 1555 1555 1.43 LINK O4 NAG G 630 C1 BMA G 631 1555 1555 1.45 LINK O3 BMA G 631 C1 MAN G 632 1555 1555 1.46 LINK O4 NAG G 634 C1 NAG G 635 1555 1555 1.45 LINK O4 NAG G 635 C1 BMA G 636 1555 1555 1.46 LINK O4 NAG G 637 C1 NAG G 638 1555 1555 1.48 LINK O4 NAG G 638 C1 BMA G 639 1555 1555 1.44 LINK O3 BMA G 639 C1 MAN G 640 1555 1555 1.44 LINK O4 NAG G 641 C1 NAG G 642 1555 1555 1.44 LINK O4 NAG G 642 C1 BMA G 643 1555 1555 1.44 LINK O3 BMA G 643 C1 MAN G 645 1555 1555 1.45 LINK O6 BMA G 643 C1 MAN G 644 1555 1555 1.45 LINK O4 NAG G 647 C1 NAG G 648 1555 1555 1.43 LINK O4 NAG G 648 C1 BMA G 649 1555 1555 1.44 LINK O6 BMA G 649 C1 MAN G 650 1555 1555 1.45 LINK O4 NAG G 651 C1 NAG G 652 1555 1555 1.43 LINK O4 NAG G 652 C1 BMA G 653 1555 1555 1.45 LINK O4 NAG L 301 C1 NAG L 302 1555 1555 1.43 LINK O4 NAG L 302 C1 BMA L 303 1555 1555 1.40 LINK O3 BMA L 303 C1 MAN L 304 1555 1555 1.44 LINK O6 BMA L 303 C1 MAN L 305 1555 1555 1.44 LINK O2 MAN L 304 C1 MAN L 308 1555 1555 1.44 LINK O3 MAN L 305 C1 MAN L 306 1555 1555 1.45 LINK O6 MAN L 305 C1 MAN L 307 1555 1555 1.45 LINK O2 MAN L 308 C1 MAN L 309 1555 1555 1.44 SITE 1 AC1 2 ASN B 611 SER B 613 SITE 1 AC2 1 ASN B 616 SITE 1 AC3 1 ASN B 637 SITE 1 AC4 18 SER B 528 ASN D 30 PHE D 31 TYR D 32 SITE 2 AC4 18 HIS D 33 TRP D 50 SER D 52 TYR D 53 SITE 3 AC4 18 SER D 54 ASP D 56 LYS D 57 ASN D 58 SITE 4 AC4 18 ARG D 98 ASP D 99 GLY D 100 THR D 100C SITE 5 AC4 18 ASN E 96 ASN G 88 SITE 1 AC5 3 ASN G 135 ASN G 156 SER G 158 SITE 1 AC6 1 ASN G 160 SITE 1 AC7 2 ARG G 192 ASN G 197 SITE 1 AC8 2 ASN G 234 SER G 236 SITE 1 AC9 4 GLU G 83 ASN G 229 LYS G 231 ASN G 241 SITE 1 AD1 3 ASN G 276 THR G 278 ASP G 279 SITE 1 AD2 8 GLU G 293 ASN G 295 ASN G 332 ILE G 333 SITE 2 AD2 8 SER G 334 ASN G 413 NAG G 647 MAN G 650 SITE 1 AD3 4 ASN G 301 THR G 303 ILE G 323 ARG G 440 SITE 1 AD4 4 LYS G 335 ASN G 339 TRP G 395 PRO G 407 SITE 1 AD5 2 ASN G 355 LYS G 357 SITE 1 AD6 2 ASN G 362 SER G 365 SITE 1 AD7 2 ASN G 386 THR G 388 SITE 1 AD8 5 PRO G 389 ASN G 392 GLY G 410 GLN G 412 SITE 2 AD8 5 ASN G 413 SITE 1 AD9 2 ASN G 396 ASN G 397 SITE 1 AE1 2 GLU G 293 ASN G 448 SITE 1 AE2 15 LYS B 617 THR B 618 ILE B 619 ASN B 620 SITE 2 AE2 15 ILE B 622 TRP B 623 ASN B 625 GLY D 2 SITE 3 AE2 15 GLN D 3 GLY D 26 LYS D 94 LEU D 97 SITE 4 AE2 15 TYR D 101 LEU D 102 PRO E 58 SITE 1 AE3 11 GLU B 621 ASN B 625 BMA B 704 GLU D 1 SITE 2 AE3 11 GLY D 2 GLY D 26 LYS D 94 LEU D 97 SITE 3 AE3 11 TYR D 101 LEU D 102 PRO E 58 SITE 1 AE4 8 NAG B 702 BMA B 704 GLY D 2 GLY D 26 SITE 2 AE4 8 LYS D 94 TYR D 101 LEU D 102 PRO E 58 SITE 1 AE5 10 NAG B 702 MAN B 705 MAN B 706 GLU D 1 SITE 2 AE5 10 GLY D 2 GLY D 26 LYS D 94 TYR D 101 SITE 3 AE5 10 LEU D 102 PRO E 58 SITE 1 AE6 4 NAG B 703 MAN B 705 GLN D 3 TYR D 101 SITE 1 AE7 25 GLY B 531 LYS B 617 THR B 618 ILE B 619 SITE 2 AE7 25 ASN B 625 MET B 626 TRP B 631 NAG B 702 SITE 3 AE7 25 NAG B 703 MAN B 706 ARG D 98 ASP D 99 SITE 4 AE7 25 GLY D 100 TYR D 101 TYR E 51 GLU E 55 SITE 5 AE7 25 PRO E 58 TYR G 39 ASN G 262 ASN G 377 SITE 6 AE7 25 SER G 446 SER G 447 ALA G 497 PRO G 498 SITE 7 AE7 25 THR G 499 SITE 1 AE8 9 ASN G 295 ASN G 413 ARG G 444 SER G 446 SITE 2 AE8 9 NAG G 620 NAG G 626 NAG G 627 NAG L 301 SITE 3 AE8 9 MAN L 306 SITE 1 AE9 47 LYS B 574 THR G 50 THR G 51 PHE G 53 SITE 2 AE9 47 GLN G 103 VAL G 161 THR G 162 THR G 163 SITE 3 AE9 47 GLU G 172 TYR G 173 TYR G 177 TYR G 217 SITE 4 AE9 47 CYS G 218 ARG G 298 PRO G 299 ASN G 300 SITE 5 AE9 47 ILE G 311 GLY G 312 ALA G 316 PHE G 317 SITE 6 AE9 47 TYR G 318 ALA G 319 THR G 320 GLY G 321 SITE 7 AE9 47 ASP G 321A ILE G 323 HIS G 330 ASN G 332 SITE 8 AE9 47 PRO G 438 ARG G 440 GLY G 441 ARG G 444 SITE 9 AE9 47 NAG G 627 NAG G 629 NAG G 647 ARG H 100 SITE 10 AE9 47 ILE H 100A GLY H 100C VAL H 100D VAL H 100E SITE 11 AE9 47 SER L 30 ASN L 50 ASN L 51 ASP L 53 SITE 12 AE9 47 PRO L 66 ASP L 67 ILE L 67A CRYST1 129.343 129.343 313.071 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 0.007731 0.004464 0.000000 0.00000 SCALE2 0.000000 0.008927 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003194 0.00000