REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) 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 : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4 REMARK 3 NUMBER OF REFLECTIONS : 17901 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130 REMARK 3 FREE R VALUE TEST SET COUNT : 968 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 19.9969 - 5.8866 0.85 2518 151 0.2252 0.2838 REMARK 3 2 5.8866 - 4.6922 0.90 2612 135 0.1722 0.2451 REMARK 3 3 4.6922 - 4.1049 0.86 2498 132 0.1564 0.2259 REMARK 3 4 4.1049 - 3.7323 0.90 2584 158 0.1779 0.2710 REMARK 3 5 3.7323 - 3.4662 0.88 2523 137 0.2033 0.2460 REMARK 3 6 3.4662 - 3.2628 0.89 2575 114 0.2224 0.2869 REMARK 3 7 3.2628 - 3.1000 0.90 2591 141 0.2614 0.3167 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 0.60 REMARK 3 SHRINKAGE RADIUS : 0.27 REMARK 3 K_SOL : 0.30 REMARK 3 B_SOL : 58.17 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.830 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -15.73960 REMARK 3 B22 (A**2) : 6.80060 REMARK 3 B33 (A**2) : 8.93910 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -9.55300 REMARK 3 B23 (A**2) : -0.00000 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 : 0.008 5768 REMARK 3 ANGLE : 1.278 7850 REMARK 3 CHIRALITY : 0.084 902 REMARK 3 PLANARITY : 0.006 980 REMARK 3 DIHEDRAL : 17.053 2007 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 62.7650 -8.8708 36.3356 REMARK 3 T TENSOR REMARK 3 T11: -0.4586 T22: 0.8223 REMARK 3 T33: -0.0638 T12: 0.0402 REMARK 3 T13: -0.2764 T23: -0.1037 REMARK 3 L TENSOR REMARK 3 L11: 0.9795 L22: 1.4776 REMARK 3 L33: 1.7749 L12: 0.0699 REMARK 3 L13: -0.6019 L23: 0.3411 REMARK 3 S TENSOR REMARK 3 S11: 0.0755 S12: -0.6853 S13: -0.0693 REMARK 3 S21: 0.5246 S22: 0.1228 S23: -0.6416 REMARK 3 S31: -0.0417 S32: 0.8520 S33: 0.0461 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'C' REMARK 3 ORIGIN FOR THE GROUP (A): 19.7508 1.4067 0.0609 REMARK 3 T TENSOR REMARK 3 T11: 0.3953 T22: 0.2013 REMARK 3 T33: 0.4645 T12: -0.0364 REMARK 3 T13: 0.0060 T23: 0.0775 REMARK 3 L TENSOR REMARK 3 L11: 4.9038 L22: 0.8705 REMARK 3 L33: 1.1396 L12: 0.7196 REMARK 3 L13: 1.6861 L23: 0.2871 REMARK 3 S TENSOR REMARK 3 S11: -0.2429 S12: 0.1178 S13: 0.6495 REMARK 3 S21: -0.0755 S22: -0.0260 S23: 0.0882 REMARK 3 S31: -0.2084 S32: 0.0898 S33: 0.2253 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'B' REMARK 3 ORIGIN FOR THE GROUP (A): 20.4190 -15.9471 -4.7868 REMARK 3 T TENSOR REMARK 3 T11: 0.3184 T22: 0.3262 REMARK 3 T33: 0.3417 T12: 0.0975 REMARK 3 T13: 0.0384 T23: -0.0099 REMARK 3 L TENSOR REMARK 3 L11: 3.9493 L22: 1.3228 REMARK 3 L33: 2.8884 L12: 0.2629 REMARK 3 L13: 2.6339 L23: 0.5871 REMARK 3 S TENSOR REMARK 3 S11: 0.1956 S12: 0.7483 S13: -0.0005 REMARK 3 S21: -0.2767 S22: -0.0522 S23: 0.0071 REMARK 3 S31: 0.0717 S32: 0.4044 S33: -0.1589 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 3VGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-11. REMARK 100 THE RCSB ID CODE IS RCSB095008. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-MAR-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18451 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 71.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.8 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.10900 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) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.40 REMARK 200 R MERGE FOR SHELL (I) : 0.63600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 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 1VGA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1M MES, 0.2M MAGNESIUM REMARK 280 CHLORIDE, 0.5% OCTHYL THIOGLUCOSIDE , PH 6.5, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.15650 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.88300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.15650 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.88300 REMARK 290 SMTRY3 4 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH C 231 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 PRO A 2 REMARK 465 ILE A 3 REMARK 465 MET A 4 REMARK 465 GLY A 5 REMARK 465 PRO A 149 REMARK 465 LYS A 150 REMARK 465 GLU A 151 REMARK 465 GLY A 152 REMARK 465 LYS A 153 REMARK 465 GLN A 154 REMARK 465 HIS A 155 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 HIS A 317 REMARK 465 HIS A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 GLU B 213 REMARK 465 CYS B 214 REMARK 465 CYS C 139 REMARK 465 GLY C 140 REMARK 465 ASP C 141 REMARK 465 THR C 142 REMARK 465 SER C 143 REMARK 465 PRO C 226 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 220 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 212 O CG OD1 ND2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 GLY C 225 O 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 CB CYS A 259 SG CYS A 262 1.74 REMARK 500 O ILE B 29 O SER B 31 2.16 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 LEU A 58 -66.94 -107.33 REMARK 500 CYS A 146 -75.80 -91.82 REMARK 500 GLU A 161 66.70 39.13 REMARK 500 PHE A 182 -74.28 -97.37 REMARK 500 VAL A 186 -62.49 -128.54 REMARK 500 LEU A 216 149.82 72.33 REMARK 500 PRO A 260 43.66 -76.92 REMARK 500 ASP A 261 -61.07 -134.66 REMARK 500 PRO A 266 -172.50 -66.33 REMARK 500 SER A 305 -71.71 -117.90 REMARK 500 TYR B 30 -124.64 62.87 REMARK 500 SER B 32 9.31 98.46 REMARK 500 LEU B 47 -64.15 -108.49 REMARK 500 ALA B 51 -26.10 77.37 REMARK 500 SER B 67 166.32 179.98 REMARK 500 ARG B 77 73.91 45.00 REMARK 500 LYS B 169 -70.14 -99.03 REMARK 500 ASN B 190 -61.17 -90.48 REMARK 500 LYS C 43 -73.96 -130.27 REMARK 500 ALA C 92 -177.43 -173.36 REMARK 500 PRO C 137 -166.29 -68.26 REMARK 500 SER C 171 -70.30 -100.31 REMARK 500 SER C 183 -115.27 51.57 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZMA A 401 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3VG9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN REMARK 900 ALLOSTERIC INVERSE-AGONIST ANTIBODY AT 2.7 A RESOLUTION