HEADER VIRAL PROTEIN/IMMUNE SYSTEM 03-JUN-22 8D53 TITLE CRYSTAL STRUCTURE OF MOSAIC HIV-1 ENVELOPE (MOSM3.3) IN COMPLEX WITH TITLE 2 ANTIBODIES PGT124 AND 35O22 AT 3.25 ANGSTROM CAVEAT 8D53 RESIDUES THR G 137 AND THR G 151 THAT ARE NEXT TO EACH OTHER CAVEAT 2 8D53 IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 3 8D53 BETWEEN C AND N IS 8.62. RESIDUES LYS G 185 AND ARG G 192 CAVEAT 4 8D53 THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT CAVEAT 5 8D53 PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 9.20. RESIDUES CAVEAT 6 8D53 THR G 400 AND ASN G 410 THAT ARE NEXT TO EACH OTHER IN THE CAVEAT 7 8D53 SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE BETWEEN C CAVEAT 8 8D53 AND N IS 11.90. RESIDUES GLN B 550 AND GLN B 562 THAT ARE CAVEAT 9 8D53 NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT PROPERLY CAVEAT 10 8D53 LINKED: DISTANCE BETWEEN C AND N IS 10.54. RESIDUES LYS L CAVEAT 11 8D53 110 AND ALA L 112 THAT ARE NEXT TO EACH OTHER IN THE SAMPLE CAVEAT 12 8D53 SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE BETWEEN C AND N CAVEAT 13 8D53 IS 5.25. RESIDUES SER H 128 AND GLY H 133 THAT ARE NEXT TO CAVEAT 14 8D53 EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: CAVEAT 15 8D53 DISTANCE BETWEEN C AND N IS 6.81. RESIDUES ILE D 37 AND TRP CAVEAT 16 8D53 D 47 THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE CAVEAT 17 8D53 NOT PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 5.04. CAVEAT 18 8D53 RESIDUES GLU D 81 AND ASN D 82B THAT ARE NEXT TO EACH OTHER CAVEAT 19 8D53 IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE CAVEAT 20 8D53 BETWEEN C AND N IS 9.00. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: G; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: MOSM3.3 GP120; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: MOSM3.3 GP41; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: PGT124 FAB LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: PGT124 FAB HEAVY CHAIN; COMPND 17 CHAIN: H; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: 35O22SCFV HEAVY CHAIN VARIABLE; COMPND 21 CHAIN: D; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: 35O22SCFV LIGHT CHAIN VARIABLE; COMPND 25 CHAIN: E; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 8 ORGANISM_TAXID: 11676; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 5; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 26 MOL_ID: 6; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENVELOP PROTEIN, B CELL TARGETING, MOSAIC DESIGN, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Y.XIAN,I.A.WILSON JRNL AUTH Y.XIAN,I.A.WILSON JRNL TITL STRUCTURAL AND ANTIGENIC CHARACTERIZATION OF B CELL MOSAIC JRNL TITL 2 ENV TRIMERS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.1_4122 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.79 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.4 REMARK 3 NUMBER OF REFLECTIONS : 47563 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.318 REMARK 3 R VALUE (WORKING SET) : 0.317 REMARK 3 FREE R VALUE : 0.331 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820 REMARK 3 FREE R VALUE TEST SET COUNT : 2293 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 42.7900 - 8.1400 0.98 3487 173 0.2761 0.2866 REMARK 3 2 8.1400 - 6.4700 0.99 3428 181 0.3097 0.3521 REMARK 3 3 6.4700 - 5.6500 0.99 3383 183 0.3204 0.3097 REMARK 3 4 5.6500 - 5.1400 0.99 3394 137 0.3074 0.2828 REMARK 3 5 5.1400 - 4.7700 0.99 3371 179 0.2897 0.3249 REMARK 3 6 4.7700 - 4.4900 1.00 3355 159 0.2972 0.3188 REMARK 3 7 4.4900 - 4.2600 0.99 3360 193 0.3226 0.2799 REMARK 3 8 4.2600 - 4.0800 0.99 3336 158 0.3303 0.3626 REMARK 3 9 4.0800 - 3.9200 0.95 3241 158 0.3475 0.4022 REMARK 3 10 3.9200 - 3.7900 0.88 2976 146 0.3743 0.3851 REMARK 3 11 3.7900 - 3.6700 0.81 2718 120 0.3784 0.3641 REMARK 3 12 3.6700 - 3.5600 0.70 2368 126 0.3923 0.3959 REMARK 3 13 3.5600 - 3.4700 0.63 2130 106 0.3868 0.4233 REMARK 3 14 3.4700 - 3.3800 0.55 1839 115 0.3877 0.4555 REMARK 3 15 3.3800 - 3.3100 0.47 1580 83 0.4058 0.4112 REMARK 3 16 3.3100 - 3.2400 0.39 1304 76 0.4273 0.5084 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) : 0.610 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.890 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 98.22 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 123.6 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 8D53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000266059. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-JUL-21 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 : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03316 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47686 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.240 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 (%) : 83.6 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.15700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 39.8 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 1.28500 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: 5CEZ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 81.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.825M AMMONIUM SULFATE, 2% PGE 400, REMARK 280 0.1M HEPES, PH 7.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 1 2 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 -Y,-X,-Z REMARK 290 5555 -X+Y,Y,-Z REMARK 290 6555 X,X-Y,-Z 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 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 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 0.00000 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, A, C, F, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S 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 APPLY THE FOLLOWING TO CHAINS: G, B, L, H, D, E, A, C, F, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -69.63300 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -120.60789 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, B, L, H, D, E, A, C, F, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 69.63300 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -120.60789 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 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 NH1 ARG G 66 C6 MAN J 4 1.43 REMARK 500 NZ LYS B 617 C6 NAG R 1 1.43 REMARK 500 C3 NAG O 2 C6 MAN O 3 1.99 REMARK 500 O4 MAN N 4 C6 MAN N 5 2.06 REMARK 500 CZ ARG G 66 C6 MAN J 4 2.08 REMARK 500 O3 NAG O 2 C5 MAN O 3 2.12 REMARK 500 ND2 ASN G 197 O5 NAG Q 1 2.13 REMARK 500 NH1 ARG G 66 C5 MAN J 4 2.17 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 THR G 63 -132.67 49.87 REMARK 500 CYS G 73 95.01 -173.07 REMARK 500 ASN G 94 105.35 -160.07 REMARK 500 THR G 163 -155.26 -110.88 REMARK 500 PRO G 253 78.63 -68.66 REMARK 500 GLN G 258 -2.81 66.47 REMARK 500 ASN G 262 -116.03 58.68 REMARK 500 CYS G 378 118.43 -161.74 REMARK 500 ARG G 379 -2.90 62.34 REMARK 500 ASN G 392 50.99 -156.07 REMARK 500 THR G 450 -57.71 -126.56 REMARK 500 ASP G 462 -138.86 56.18 REMARK 500 LEU G 483 35.37 -97.60 REMARK 500 GLN B 567 62.53 61.38 REMARK 500 HIS B 570 11.87 59.68 REMARK 500 ASN L 51 -33.54 -39.96 REMARK 500 ASP L 66A 53.23 -94.85 REMARK 500 PRO L 141 -158.99 -82.02 REMARK 500 ASP L 151 -123.02 57.57 REMARK 500 SER H 180 116.00 -161.79 REMARK 500 ASN H 204 67.02 -104.92 REMARK 500 THR D 12 -153.39 -115.15 REMARK 500 THR D 72F -158.86 -131.75 REMARK 500 THR D 100C -70.11 -59.33 REMARK 500 LEU D 100E 125.31 -170.89 REMARK 500 PRO D 100F 108.14 -58.13 REMARK 500 LEU D 109 -159.70 -117.88 REMARK 500 GLN E 17 -159.69 -96.45 REMARK 500 SER E 29 -125.49 58.83 REMARK 500 TRP E 69 -1.76 -142.36 REMARK 500 THR E 92 -169.12 -116.92 REMARK 500 SER E 105 -71.29 -66.78 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 MAN N 5 REMARK 610 NAG S 1 REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 NAG G 601 REMARK 615 NAG B 701 REMARK 615 NAG A 1 REMARK 615 NAG C 1 REMARK 615 NAG F 1 REMARK 615 NAG F 2 REMARK 615 BMA F 3 REMARK 615 MAN F 4 REMARK 615 MAN F 5 REMARK 615 MAN F 6 REMARK 615 MAN F 7 REMARK 615 MAN F 8 REMARK 615 MAN F 9 REMARK 615 NAG I 1 REMARK 615 NAG J 1 REMARK 615 NAG J 2 REMARK 615 NAG K 1 REMARK 615 NAG M 1 REMARK 615 NAG M 2 REMARK 615 NAG N 1 REMARK 615 NAG N 2 REMARK 615 BMA N 3 REMARK 615 NAG R 1 REMARK 615 NAG R 2 DBREF 8D53 G 30 506 PDB 8D53 8D53 30 506 DBREF 8D53 B 522 664 PDB 8D53 8D53 522 664 DBREF 8D53 L 6 211 PDB 8D53 8D53 6 211 DBREF 8D53 H 1 214 PDB 8D53 8D53 1 214 DBREF 8D53 D 1 110 PDB 8D53 8D53 1 110 DBREF 8D53 E 3 106 PDB 8D53 8D53 3 106 SEQRES 1 G 446 ARG SER ASP ASN LEU TRP VAL THR VAL TYR TYR GLY VAL SEQRES 2 G 446 PRO VAL TRP ARG ASP ALA GLU THR THR LEU PHE CYS ALA SEQRES 3 G 446 SER ASP ALA LYS TYR ALA ASP THR GLU LYS ARG ASN VAL SEQRES 4 G 446 TRP ALA THR HIS CYS CYS VAL PRO THR ASP PRO ASN PRO SEQRES 5 G 446 GLN GLU ILE HIS LEU GLU ASN VAL THR GLU ASN PHE ASN SEQRES 6 G 446 MET TRP LYS ASN ASN MET VAL GLU GLN MET GLN GLU ASP SEQRES 7 G 446 VAL ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL SEQRES 8 G 446 LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR LYS SEQRES 9 G 446 ALA ASN LEU THR THR ASP GLU VAL ARG ASN CYS SER PHE SEQRES 10 G 446 ASN MET THR THR LEU LEU ARG ASP LYS LYS ARG LEU VAL SEQRES 11 G 446 HIS ALA LEU PHE TYR LYS LEU ASP ILE VAL PRO ILE LYS SEQRES 12 G 446 ARG LEU ILE ASN CYS ASN THR SER VAL ILE LYS GLN ALA SEQRES 13 G 446 CYS PRO LYS VAL THR PHE ASP PRO ILE PRO ILE HIS TYR SEQRES 14 G 446 CYS THR PRO ALA GLY TYR ALA ILE LEU LYS CYS ASN ASP SEQRES 15 G 446 LYS ASN PHE ASN GLY THR GLY PRO CYS LYS ASN VAL SER SEQRES 16 G 446 SER VAL GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER SEQRES 17 G 446 THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU SEQRES 18 G 446 ILE ILE ILE ARG SER GLU ASN LEU THR ASN ASN ALA LYS SEQRES 19 G 446 THR ILE ILE VAL HIS LEU ASN LYS SER VAL GLU ILE ASN SEQRES 20 G 446 CYS THR ARG PRO SER ASN ASN THR VAL THR SER VAL ARG SEQRES 21 G 446 ILE GLY PRO GLY GLN TRP PHE TYR TYR THR GLY ASP ILE SEQRES 22 G 446 ILE GLY ASP ILE ARG GLN ALA TYR CYS ASN ILE SER GLY SEQRES 23 G 446 THR LYS TRP ASN GLU THR LEU ARG GLN VAL ALA LYS LYS SEQRES 24 G 446 LEU LYS GLU HIS PHE ASN LYS THR ILE ILE PHE GLN GLN SEQRES 25 G 446 PRO SER GLY GLY ASP LEU GLU ILE THR MET HIS HIS PHE SEQRES 26 G 446 ASN CYS ARG GLY GLU PHE PHE TYR CYS ASN THR THR LYS SEQRES 27 G 446 LEU PHE ASN SER THR TRP ILE GLY ASN GLU THR ASN ASN SEQRES 28 G 446 ASP THR ILE ILE LEU PRO CYS ARG ILE LYS GLN ILE ILE SEQRES 29 G 446 ASN MET TRP GLN ARG VAL GLY GLN ALA MET TYR ALA PRO SEQRES 30 G 446 PRO ILE SER GLY ILE ILE ASN CYS VAL SER ASN ILE THR SEQRES 31 G 446 GLY ILE LEU LEU THR ARG ASP GLY GLY SER GLY ASP ASN SEQRES 32 G 446 ALA THR GLU THR PHE ARG PRO GLY GLY GLY ASN ILE LYS SEQRES 33 G 446 ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL SEQRES 34 G 446 GLU ILE GLU PRO LEU GLY ILE ALA PRO THR ARG CYS LYS SEQRES 35 G 446 ARG ARG VAL VAL SEQRES 1 B 132 PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA ALA SER SEQRES 2 B 132 MET THR LEU THR VAL GLN ALA ARG ASN LEU LEU SER GLY SEQRES 3 B 132 ILE VAL GLN GLN GLN HIS LEU LEU GLN ASP THR HIS TRP SEQRES 4 B 132 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 5 B 132 HIS TYR LEU LYS ASP GLN LYS PHE LEU GLY LEU TRP GLY SEQRES 6 B 132 CYS SER GLY LYS ILE ILE CYS CYS THR ALA VAL PRO TRP SEQRES 7 B 132 ASN SER THR TRP SER ASN LYS SER TYR GLU GLU ILE TRP SEQRES 8 B 132 ASN ASN MET THR TRP ILE GLU TRP GLU ARG GLU ILE SER SEQRES 9 B 132 ASN TYR THR SER GLN ILE TYR GLU ILE LEU THR GLU SER SEQRES 10 B 132 GLN ASN GLN GLN ASP ARG ASN GLU LYS ASP LEU LEU GLU SEQRES 11 B 132 LEU ASP SEQRES 1 L 212 SER TYR VAL SER PRO LEU SER VAL ALA LEU GLY GLU THR SEQRES 2 L 212 ALA ARG ILE SER CYS GLY ARG GLN ALA LEU GLY SER ARG SEQRES 3 L 212 ALA VAL GLN TRP TYR GLN HIS LYS PRO GLY GLN ALA PRO SEQRES 4 L 212 ILE LEU LEU ILE TYR ASN ASN GLN ASP ARG PRO SER GLY SEQRES 5 L 212 ILE PRO GLU ARG PHE SER GLY THR PRO ASP ILE ASN PHE SEQRES 6 L 212 GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU VAL SEQRES 7 L 212 GLY ASP GLU ALA ASP TYR TYR CYS HIS MET TRP ASP SER SEQRES 8 L 212 ARG SER GLY PHE SER TRP SER PHE GLY GLY ALA THR ARG SEQRES 9 L 212 LEU THR VAL LEU SER GLN PRO LYS ALA PRO SER VAL THR SEQRES 10 L 212 LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS SEQRES 11 L 212 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 212 ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL SEQRES 13 L 212 LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER SEQRES 14 L 212 ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 212 PRO GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN SEQRES 16 L 212 VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA SEQRES 17 L 212 PRO THR GLU CYS SEQRES 1 H 229 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL ARG SEQRES 2 H 229 PRO SER GLU THR LEU SER VAL THR CYS ILE VAL SER GLY SEQRES 3 H 229 GLY SER ILE SER ASN TYR TYR TRP THR TRP ILE ARG GLN SEQRES 4 H 229 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE SER SEQRES 5 H 229 ASP ARG GLU THR THR THR TYR ASN PRO SER LEU ASN SER SEQRES 6 H 229 ARG ALA VAL ILE SER ARG ASP THR SER LYS ASN GLN LEU SEQRES 7 H 229 SER LEU GLN LEU ARG SER VAL THR THR ALA ASP THR ALA SEQRES 8 H 229 ILE TYR PHE CYS ALA THR ALA ARG ARG GLY GLN ARG ILE SEQRES 9 H 229 TYR GLY VAL VAL SER PHE GLY GLU PHE PHE TYR TYR TYR SEQRES 10 H 229 TYR MET ASP VAL TRP GLY LYS GLY THR ALA VAL THR VAL SEQRES 11 H 229 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 229 ALA PRO SER SER GLY GLY THR ALA ALA LEU GLY CYS LEU SEQRES 13 H 229 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP SEQRES 14 H 229 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO SEQRES 15 H 229 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER SEQRES 16 H 229 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR SEQRES 17 H 229 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS SEQRES 18 H 229 VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 D 117 GLN GLY GLN LEU VAL GLN SER GLY ALA THR THR THR LYS SEQRES 2 D 117 PRO GLY SER SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 117 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE TRP MET SEQRES 4 D 117 GLY TRP ILE SER PRO TYR SER GLY ASP LYS ASN LEU ALA SEQRES 5 D 117 PRO ALA PHE GLN ASP ARG VAL ASN MET THR THR ASP THR SEQRES 6 D 117 GLU VAL PRO VAL THR SER PHE THR SER THR GLY ALA ALA SEQRES 7 D 117 TYR MET GLU ASN LEU THR SER ASP ASP THR GLY THR TYR SEQRES 8 D 117 PHE CYS ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR SEQRES 9 D 117 TRP LEU PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR SEQRES 1 E 107 VAL LEU THR GLN SER ALA SER VAL SER GLY SER LEU GLY SEQRES 2 E 107 GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SER VAL SEQRES 3 E 107 CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN TRP PRO SEQRES 4 E 107 PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU ASP ASN SEQRES 5 E 107 GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER GLY TYR SEQRES 6 E 107 LYS SER TYR TRP SER ALA TYR LEU THR ILE SER ASP LEU SEQRES 7 E 107 ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SER TYR SEQRES 8 E 107 THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY THR LYS SEQRES 9 E 107 VAL SER VAL HET NAG G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG B 701 14 HET NAG A 1 14 HET NAG A 2 14 HET NAG C 1 14 HET NAG C 2 14 HET NAG F 1 14 HET NAG F 2 14 HET BMA F 3 11 HET MAN F 4 11 HET MAN F 5 11 HET MAN F 6 11 HET MAN F 7 11 HET MAN F 8 11 HET MAN F 9 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET MAN J 4 11 HET NAG K 1 14 HET NAG K 2 14 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET MAN N 5 11 HET MAN N 6 11 HET NAG O 1 14 HET NAG O 2 14 HET MAN O 3 11 HET BMA O 4 11 HET MAN O 5 11 HET NAG P 1 14 HET NAG P 2 14 HET BMA P 3 11 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 7 NAG 31(C8 H15 N O6) FORMUL 14 BMA 7(C6 H12 O6) FORMUL 14 MAN 12(C6 H12 O6) HELIX 1 AA1 ASP G 57 ASP G 62 1 6 HELIX 2 AA2 ASN G 99 LYS G 117 1 19 HELIX 3 AA3 LEU G 122 VAL G 127 5 6 HELIX 4 AA4 SER G 334 PHE G 353 1 20 HELIX 5 AA5 ASN G 425 ARG G 429 5 5 HELIX 6 AA6 ILE G 475 SER G 481 1 7 HELIX 7 AA7 THR B 529 SER B 546 1 18 HELIX 8 AA8 GLY B 572 TRP B 596 1 25 HELIX 9 AA9 SER B 618 MET B 626 1 9 HELIX 10 AB1 THR B 627 SER B 636 1 10 HELIX 11 AB2 TYR B 638 ASP B 664 1 27 HELIX 12 AB3 GLU L 79 GLU L 83 5 5 HELIX 13 AB4 SER L 121 GLN L 126 1 6 HELIX 14 AB5 THR L 181 HIS L 188 1 8 HELIX 15 AB6 PRO H 61 ASN H 64 5 4 HELIX 16 AB7 THR H 83 THR H 87 5 5 HELIX 17 AB8 VAL H 100D GLY H 100H 5 5 HELIX 18 AB9 SER H 156 ALA H 158 5 3 HELIX 19 AC1 PRO H 185 LEU H 189 5 5 HELIX 20 AC2 PRO D 61 GLN D 64 5 4 HELIX 21 AC3 ARG E 79 GLU E 83 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 TRP G 35 O THR G 499 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL G 36 SHEET 1 AA2 5 TRP G 45 ASP G 47 0 SHEET 2 AA2 5 TYR G 486 ILE G 491 -1 O GLU G 490 N ARG G 46 SHEET 3 AA2 5 TYR G 223 CYS G 228 -1 N ALA G 224 O VAL G 489 SHEET 4 AA2 5 VAL G 242 VAL G 245 -1 O VAL G 245 N ILE G 225 SHEET 5 AA2 5 ILE G 84 HIS G 85 -1 N ILE G 84 O SER G 244 SHEET 1 AA3 2 PHE G 53 SER G 56 0 SHEET 2 AA3 2 ILE G 215 CYS G 218 -1 O HIS G 216 N ALA G 55 SHEET 1 AA4 2 GLU G 91 PHE G 93 0 SHEET 2 AA4 2 GLY G 237 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AA5 3 ASN G 130 THR G 132 0 SHEET 2 AA5 3 VAL G 154 THR G 162 -1 O SER G 158 N ASN G 130 SHEET 3 AA5 3 LYS G 169 TYR G 177 -1 O VAL G 172 N PHE G 159 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 LYS G 202 SHEET 3 AA6 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AA712 LEU G 260 LEU G 261 0 SHEET 2 AA712 ILE G 271 ARG G 273 0 SHEET 3 AA712 ILE G 284 VAL G 307 -1 O ILE G 285 N ARG G 273 SHEET 4 AA712 PHE G 317 ILE G 323 -1 O GLY G 321 N THR G 303 SHEET 5 AA712 TYR G 330 ILE G 333 -1 O ASN G 332 N ASN G 295 SHEET 6 AA712 ILE G 360 PHE G 361 0 SHEET 7 AA712 HIS G 375 CYS G 378 0 SHEET 8 AA712 GLU G 381 CYS G 385 -1 O PHE G 383 N PHE G 376 SHEET 9 AA712 SER G 393 THR G 394 -1 O SER G 393 N PHE G 361 SHEET 10 AA712 ILE G 414 LYS G 421 -1 O ARG G 419 N TYR G 384 SHEET 11 AA712 GLY G 441 ARG G 456 -1 O CYS G 445 N CYS G 296 SHEET 12 AA712 THR G 467 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 1 AA8 5 VAL L 8 VAL L 13 0 SHEET 2 AA8 5 ALA L 101 VAL L 106 1 O ARG L 103 N SER L 9 SHEET 3 AA8 5 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 5 ARG L 31 HIS L 38 -1 N GLN L 34 O HIS L 89 SHEET 5 AA8 5 ILE L 45 ILE L 48 -1 O ILE L 45 N GLN L 37 SHEET 1 AA9 3 ALA L 19 SER L 22 0 SHEET 2 AA9 3 THR L 72 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AA9 3 PHE L 62 GLY L 64 -1 N SER L 63 O THR L 74 SHEET 1 AB1 5 SER L 114 PHE L 118 0 SHEET 2 AB1 5 ALA L 130 PHE L 139 -1 O SER L 137 N SER L 114 SHEET 3 AB1 5 VAL L 159 THR L 161 0 SHEET 4 AB1 5 SER L 165 LYS L 166 0 SHEET 5 AB1 5 TYR L 172 LEU L 180 -1 O ALA L 173 N SER L 165 SHEET 1 AB2 4 SER L 153 VAL L 155 0 SHEET 2 AB2 4 THR L 145 ALA L 150 -1 N TRP L 148 O VAL L 155 SHEET 3 AB2 4 TYR L 191 HIS L 197 -1 O THR L 196 N THR L 145 SHEET 4 AB2 4 SER L 200 VAL L 206 -1 O SER L 200 N HIS L 197 SHEET 1 AB3 4 GLN H 3 SER H 7 0 SHEET 2 AB3 4 LEU H 18 SER H 25 -1 O ILE H 23 N GLN H 5 SHEET 3 AB3 4 GLN H 77 LEU H 82 -1 O LEU H 78 N CYS H 22 SHEET 4 AB3 4 ALA H 67 ASP H 72 -1 N SER H 70 O SER H 79 SHEET 1 AB4 7 LEU H 11 VAL H 12 0 SHEET 2 AB4 7 TYR H 33 GLN H 39 0 SHEET 3 AB4 7 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 4 AB4 7 THR H 57 TYR H 59 -1 O THR H 58 N TYR H 50 SHEET 5 AB4 7 ALA H 88 ILE H 100A-1 O PHE H 91 N ILE H 37 SHEET 6 AB4 7 PHE H 100J TRP H 103 -1 O TYR H 100M N GLY H 98 SHEET 7 AB4 7 THR H 107 VAL H 111 -1 O VAL H 109 N ALA H 88 SHEET 1 AB5 4 VAL H 121 LEU H 124 0 SHEET 2 AB5 4 ALA H 136 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB5 4 TYR H 176 VAL H 184 -1 O LEU H 178 N VAL H 142 SHEET 4 AB5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB6 3 THR H 151 TRP H 154 0 SHEET 2 AB6 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151 SHEET 3 AB6 3 THR H 205 VAL H 211 -1 O LYS H 209 N CYS H 196 SHEET 1 AB7 4 GLN D 3 GLN D 6 0 SHEET 2 AB7 4 ILE D 20 SER D 25 -1 O LYS D 23 N VAL D 5 SHEET 3 AB7 4 SER D 74 GLU D 81 -1 O GLY D 76 N THR D 24 SHEET 4 AB7 4 ASN D 68 PRO D 72D-1 N THR D 70 O TYR D 79 SHEET 1 AB8 5 LYS D 57 LEU D 59 0 SHEET 2 AB8 5 GLY D 49 ILE D 51 -1 N TRP D 50 O ASN D 58 SHEET 3 AB8 5 ILE D 34 ILE D 37 -1 N TRP D 36 O GLY D 49 SHEET 4 AB8 5 PHE D 91 LYS D 94 -1 O ALA D 93 N ASN D 35 SHEET 5 AB8 5 TYR D 101 TRP D 103 -1 O TYR D 101 N LYS D 94 SHEET 1 AB9 4 THR E 5 GLN E 6 0 SHEET 2 AB9 4 SER E 18 THR E 24 -1 O THR E 24 N THR E 5 SHEET 3 AB9 4 ALA E 71 SER E 76 -1 O ALA E 71 N CYS E 23 SHEET 4 AB9 4 PHE E 62 LYS E 66 -1 N SER E 63 O THR E 74 SHEET 1 AC1 7 SER E 9 VAL E 11 0 SHEET 2 AC1 7 SER E 32 GLN E 37 0 SHEET 3 AC1 7 THR E 45 GLU E 50 -1 O ILE E 48 N TRP E 35 SHEET 4 AC1 7 GLU E 53 ARG E 54 -1 O GLU E 53 N GLU E 50 SHEET 5 AC1 7 THR E 85 TYR E 91 -1 O TYR E 87 N TYR E 36 SHEET 6 AC1 7 VAL E 97 PHE E 98 -1 O VAL E 97 N SER E 90 SHEET 7 AC1 7 THR E 102 VAL E 104 -1 O THR E 102 N TYR E 86 SSBOND 1 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 2 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 3 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 4 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 5 CYS G 218 CYS G 247 1555 1555 2.03 SSBOND 6 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 7 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 8 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 9 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 10 CYS G 501 CYS B 605 1555 1555 2.04 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 13 CYS L 134 CYS L 193 1555 1555 2.04 SSBOND 14 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 15 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 16 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 17 CYS E 23 CYS E 88 1555 1555 2.03 SSBOND 18 CYS E 89 CYS E 96 1555 1555 2.03 LINK ND2 ASN G 88 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN G 130 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG A 1 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN G 241 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN G 289 C1 NAG K 1 1555 1555 1.46 LINK ND2 ASN G 295 C1 NAG G 602 1555 1555 1.45 LINK ND2 ASN G 301 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG R 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44 LINK O6 BMA F 3 C1 MAN F 4 1555 1555 1.44 LINK O3 BMA F 3 C1 MAN F 8 1555 1555 1.44 LINK O6 MAN F 4 C1 MAN F 5 1555 1555 1.46 LINK O3 MAN F 4 C1 MAN F 7 1555 1555 1.44 LINK O2 MAN F 5 C1 MAN F 6 1555 1555 1.44 LINK O2 MAN F 8 C1 MAN F 9 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.43 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.44 LINK O6 BMA N 3 C1 MAN N 4 1555 1555 1.44 LINK O3 BMA N 3 C1 MAN N 6 1555 1555 1.44 LINK O4 MAN N 4 C5 MAN N 5 1555 1555 1.38 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45 LINK O3 NAG O 2 C6 MAN O 3 1555 1555 1.38 LINK O4 NAG O 2 C1 BMA O 4 1555 1555 1.45 LINK C1 MAN O 3 O6 BMA O 4 1555 1555 1.45 LINK O3 BMA O 4 C1 MAN O 5 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.47 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45 CISPEP 1 TYR L 140 PRO L 141 0 3.18 CISPEP 2 PHE H 146 PRO H 147 0 -4.80 CISPEP 3 GLU H 148 PRO H 149 0 5.61 CRYST1 139.266 139.266 320.332 90.00 90.00 120.00 P 3 1 2 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 0.007181 0.004146 0.000000 0.00000 SCALE2 0.000000 0.008291 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003122 0.00000