REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890 REMARK 3 COMPLETENESS FOR RANGE (%) : 47.1 REMARK 3 NUMBER OF REFLECTIONS : 35358 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 1778 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 43.2083 - 7.5123 0.54 2963 178 0.2193 0.2331 REMARK 3 2 7.5123 - 5.9678 0.53 2931 145 0.2038 0.2498 REMARK 3 3 5.9678 - 5.2148 0.53 2873 153 0.1633 0.2326 REMARK 3 4 5.2148 - 4.7387 0.52 2875 153 0.1449 0.2066 REMARK 3 5 4.7387 - 4.3994 0.52 2841 153 0.1468 0.2054 REMARK 3 6 4.3994 - 4.1402 0.52 2886 134 0.1627 0.1814 REMARK 3 7 4.1402 - 3.9330 0.52 2795 158 0.1719 0.2130 REMARK 3 8 3.9330 - 3.7619 0.51 2822 155 0.1926 0.2264 REMARK 3 9 3.7619 - 3.6172 0.50 2732 139 0.2085 0.2749 REMARK 3 10 3.6172 - 3.4924 0.47 2565 135 0.2250 0.2812 REMARK 3 11 3.4924 - 3.3833 0.41 2233 124 0.2465 0.2930 REMARK 3 12 3.3833 - 3.2866 0.33 1815 92 0.2726 0.3040 REMARK 3 13 3.2866 - 3.2000 0.23 1249 59 0.2856 0.3897 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 : 0.29 REMARK 3 B_SOL : 97.97 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : -0.000 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL 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 12184 REMARK 3 ANGLE : 0.796 16518 REMARK 3 CHIRALITY : 0.051 1895 REMARK 3 PLANARITY : 0.004 2084 REMARK 3 DIHEDRAL : 15.911 4424 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN C AND RESID 110:214 REMARK 3 ORIGIN FOR THE GROUP (A): 75.6898 49.5791 21.0140 REMARK 3 T TENSOR REMARK 3 T11: 0.9186 T22: 1.0294 REMARK 3 T33: 1.0746 T12: 0.0863 REMARK 3 T13: 0.2481 T23: 0.0794 REMARK 3 L TENSOR REMARK 3 L11: 0.9692 L22: -0.7162 REMARK 3 L33: 2.9942 L12: 0.1442 REMARK 3 L13: -0.2274 L23: -0.2981 REMARK 3 S TENSOR REMARK 3 S11: -0.1795 S12: 0.2881 S13: -0.3859 REMARK 3 S21: -0.0066 S22: -0.1439 S23: 0.0043 REMARK 3 S31: 0.0873 S32: 0.2210 S33: 0.2681 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain G and (resseq 83:119 or resseq 205: REMARK 3 299 or resseq 329:397 or resseq 410:418 or REMARK 3 resid 420:458 or resid 465:492 ) and (not REMARK 3 element H) REMARK 3 SELECTION : chain A and (resseq 83:119 or resseq 205: REMARK 3 299 or resseq 329:397 or resseq 410:418 or REMARK 3 resid 420:458 or resid 465:492 ) and (not REMARK 3 element H) REMARK 3 ATOM PAIRS NUMBER : 2166 REMARK 3 RMSD : 0.021 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain H and (resseq 1:101 or resid 110: REMARK 3 231 ) and (not element H) REMARK 3 SELECTION : chain B and (resseq 1:101 or resid 110: REMARK 3 231 ) and (not element H) REMARK 3 ATOM PAIRS NUMBER : 1662 REMARK 3 RMSD : 0.013 REMARK 3 NCS GROUP : 3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain L and (resseq 1:29 or resseq 31:212 REMARK 3 ) and (not element H) REMARK 3 SELECTION : chain C and (resseq 1:29 or resseq 31:212 REMARK 3 ) and (not element H) REMARK 3 ATOM PAIRS NUMBER : 1630 REMARK 3 RMSD : 0.015 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3IDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-09. REMARK 100 THE RCSB ID CODE IS RCSB054291. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 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) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35856 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 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 (%) : 86.5 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09900 REMARK 200 FOR THE DATA SET : 21.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 34.0 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.45000 REMARK 200 FOR SHELL : 1.700 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: PDB ENTRY 3IDX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 8 % PEG 8000, 6.5 % ISOPROPANOL, 200 REMARK 280 MM AMMONIUM SULFATE, 100 MM HEPES, PH 7.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 108.44300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 108.44300 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 53.08400 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 102.15800 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.08400 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 102.15800 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 108.44300 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.08400 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 102.15800 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.44300 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.08400 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 102.15800 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN ANTIGEN-ANTIBODY COMPLEX THAT REMARK 300 CONTAINS CHAIN G IN COMPLEX WITH CHAIN H AND L OR CHAIN A IN REMARK 300 COMPLEX WITH CHAIN B AND C. 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: G, A, H, B, L, C 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, B, H, C, 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 THR G 399 REMARK 465 TRP G 400 REMARK 465 SER G 401 REMARK 465 THR G 402 REMARK 465 GLU G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 ASN G 407 REMARK 465 THR G 408 REMARK 465 GLU G 409 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 CYS L 214 REMARK 465 GLY A 192 REMARK 465 ALA A 193 REMARK 465 GLY A 194 REMARK 465 THR A 399 REMARK 465 TRP A 400 REMARK 465 SER A 401 REMARK 465 THR A 402 REMARK 465 GLU A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 ASN A 407 REMARK 465 THR A 408 REMARK 465 GLU A 409 REMARK 465 LYS B 129 REMARK 465 SER B 130 REMARK 465 CYS C 214 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 ND2 ASN A 241 C2 NAG A 741 1.71 REMARK 500 ND2 ASN G 241 C2 NAG G 741 1.72 REMARK 500 ND2 ASN G 295 C2 NAG G 795 1.99 REMARK 500 ND2 ASN A 230 C2 NAG A 730 1.99 REMARK 500 CG ASN G 463 C1 NAG G 963 2.03 REMARK 500 ND2 ASN G 392 C2 NAG G 892 2.15 REMARK 500 ND2 ASN G 276 C2 NAG G 776 2.16 REMARK 500 ND2 ASN A 234 C2 NAG A 734 2.19 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 ASN G 88 -12.47 69.61 REMARK 500 ASP G 107 -164.55 -77.76 REMARK 500 ILE G 108 113.71 75.66 REMARK 500 LEU G 111 119.79 66.45 REMARK 500 CYS G 205 53.04 81.59 REMARK 500 LYS G 207 116.23 -26.91 REMARK 500 PRO G 220 -179.43 -56.94 REMARK 500 ASN G 230 106.76 -56.01 REMARK 500 GLN G 258 -57.82 74.40 REMARK 500 GLU G 268 -96.52 -90.07 REMARK 500 ASN G 276 100.49 -178.76 REMARK 500 SER G 387 31.90 -85.73 REMARK 500 ASN G 392 67.15 -155.22 REMARK 500 SER G 440 -95.12 -175.34 REMARK 500 SER G 446 128.73 89.70 REMARK 500 SER G 447 -153.84 -146.78 REMARK 500 ASN G 460 -34.81 -35.60 REMARK 500 SER G 461 38.37 -75.99 REMARK 500 ASN G 463 -98.41 -121.68 REMARK 500 PHE H 27 136.87 -174.43 REMARK 500 THR H 28 98.55 -52.25 REMARK 500 ARG H 55 -86.51 -64.19 REMARK 500 VAL H 63 -11.80 -146.07 REMARK 500 LYS H 64 105.71 -48.75 REMARK 500 ASN H 73 1.65 -62.51 REMARK 500 TYR H 100C 1.00 -150.71 REMARK 500 ASP H 101 -53.93 -121.76 REMARK 500 PRO H 126 -153.01 -61.81 REMARK 500 ASP H 144 78.63 65.04 REMARK 500 PHE H 146 135.95 -178.07 REMARK 500 PRO H 147 -151.52 -94.89 REMARK 500 SER H 177 135.99 -173.00 REMARK 500 SER H 188 23.85 -143.08 REMARK 500 ASN H 199 83.93 -154.47 REMARK 500 LYS H 214 -146.55 -98.81 REMARK 500 SER H 215 64.78 69.56 REMARK 500 ARG L 30 -124.66 48.94 REMARK 500 ALA L 51 -59.11 66.91 REMARK 500 SER L 52 35.72 -140.99 REMARK 500 PRO L 59 157.93 -44.94 REMARK 500 SER L 114 108.25 -58.40 REMARK 500 ASN L 138 78.94 34.86 REMARK 500 ARG L 202 -31.65 -34.50 REMARK 500 PRO L 204 122.22 -38.86 REMARK 500 PHE L 209 -158.46 177.96 REMARK 500 ARG L 211 30.92 -79.80 REMARK 500 ASN A 88 -12.56 69.61 REMARK 500 ASP A 107 -164.37 -77.99 REMARK 500 ILE A 108 113.13 75.72 REMARK 500 LEU A 111 118.81 66.03 REMARK 500 REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 497 DISTANCE = 5.52 ANGSTROMS REMARK 525 HOH A 498 DISTANCE = 5.56 ANGSTROMS REMARK 525 HOH C 241 DISTANCE = 5.87 ANGSTROMS REMARK 525 HOH G 493 DISTANCE = 5.02 ANGSTROMS REMARK 525 HOH L 225 DISTANCE = 7.26 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 588 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 730 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 734 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 741 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 762 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 776 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 789 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 795 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 839 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 856 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 886 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 892 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 948 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG G 963 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 588 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 730 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 734 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 741 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 762 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 776 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 789 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 795 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 839 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 856 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 886 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 892 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 948 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 963 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3IDX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HIV-GP120 CORE IN COMPLEX WITH CD4- REMARK 900 BINDING SITE ANTIBODY B13. IN SPACE GROUP C222