HEADER PROTEIN BINDING, TRANSFERASE 02-AUG-09 3IIL
TITLE THE STRUCTURE OF HCINAP-MGADP-PI COMPLEX AT 2.0 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COILIN-INTERACTING NUCLEAR ATPASE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COILIN-INTERACTING NULCEAR ATPASE PROTEIN, TAF9 RNA
COMPND 5 POLYMERASE II, TATA BOX BINDING PROTEIN (TBP)-ASSOCIATED FACTOR,
COMPND 6 32KDA, ISOFORM CRA_B, HUMAN ADENYLATE KINASE 6;
COMPND 7 EC: 2.7.4.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CINAP, TAF9, HCG_37060;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3
KEYWDS ALPHA AND BETA PROTEINS (A/B), PROTEIN BINDING, TRANSFERASE,
KEYWDS 2 PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.ZOGRAPHOS,C.E.DRAKOU,D.D.LEONIDAS
REVDAT 5 06-SEP-23 3IIL 1 REMARK SEQADV LINK
REVDAT 4 18-JAN-12 3IIL 1 JRNL
REVDAT 3 23-NOV-11 3IIL 1 JRNL
REVDAT 2 05-OCT-11 3IIL 1 JRNL VERSN REMARK
REVDAT 1 06-OCT-10 3IIL 0
JRNL AUTH C.E.DRAKOU,A.MALEKKOU,J.M.HAYES,C.W.LEDERER,D.D.LEONIDAS,
JRNL AUTH 2 N.G.OIKONOMAKOS,A.I.LAMOND,N.SANTAMA,S.E.ZOGRAPHOS
JRNL TITL HCINAP IS AN ATYPICAL MAMMALIAN NUCLEAR ADENYLATE KINASE
JRNL TITL 2 WITH AN ATPASE MOTIF: STRUCTURAL AND FUNCTIONAL STUDIES.
JRNL REF PROTEINS V. 80 206 2012
JRNL REFN ISSN 0887-3585
JRNL PMID 22038794
JRNL DOI 10.1002/PROT.23186
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20968
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1131
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1530
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1441
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 201
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 32.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.391
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1532 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2086 ; 1.258 ; 1.999
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 174 ; 4.941 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;38.786 ;25.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 265 ;14.258 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ; 7.893 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 221 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1158 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 872 ; 0.543 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1421 ; 1.033 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 660 ; 1.674 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 665 ; 2.794 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 2
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1753 17.4499 9.4335
REMARK 3 T TENSOR
REMARK 3 T11: 0.4039 T22: 0.3399
REMARK 3 T33: 0.3811 T12: -0.1547
REMARK 3 T13: 0.0242 T23: 0.0957
REMARK 3 L TENSOR
REMARK 3 L11: 5.0355 L22: 8.2790
REMARK 3 L33: 1.9270 L12: 1.8106
REMARK 3 L13: 0.2030 L23: -1.4211
REMARK 3 S TENSOR
REMARK 3 S11: -0.1159 S12: 0.6672 S13: 0.6920
REMARK 3 S21: -0.2745 S22: 0.1073 S23: -0.5041
REMARK 3 S31: -0.6611 S32: 0.5483 S33: 0.0086
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 22
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2492 -0.6883 -1.2394
REMARK 3 T TENSOR
REMARK 3 T11: 0.1537 T22: 0.1073
REMARK 3 T33: 0.1372 T12: -0.0007
REMARK 3 T13: -0.0125 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.7160 L22: 1.4318
REMARK 3 L33: 1.6328 L12: 0.5448
REMARK 3 L13: 0.2278 L23: 0.9466
REMARK 3 S TENSOR
REMARK 3 S11: -0.1382 S12: 0.0526 S13: 0.1523
REMARK 3 S21: -0.1956 S22: 0.0421 S23: 0.1241
REMARK 3 S31: -0.1604 S32: -0.1032 S33: 0.0961
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6406 5.7306 -3.1438
REMARK 3 T TENSOR
REMARK 3 T11: 0.2249 T22: 0.1331
REMARK 3 T33: 0.1651 T12: -0.0383
REMARK 3 T13: -0.0580 T23: 0.0838
REMARK 3 L TENSOR
REMARK 3 L11: 4.2586 L22: 1.6800
REMARK 3 L33: 1.5488 L12: -2.3022
REMARK 3 L13: -0.3919 L23: 0.9403
REMARK 3 S TENSOR
REMARK 3 S11: -0.2014 S12: 0.1508 S13: 0.3989
REMARK 3 S21: -0.0807 S22: 0.0274 S23: -0.0571
REMARK 3 S31: -0.2779 S32: -0.0104 S33: 0.1740
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 37 A 44
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8384 -2.0841 -11.2260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1805 T22: 0.1233
REMARK 3 T33: 0.1182 T12: -0.0344
REMARK 3 T13: 0.0639 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 2.6932 L22: 8.3703
REMARK 3 L33: 9.3711 L12: -1.3345
REMARK 3 L13: -1.0116 L23: -0.6621
REMARK 3 S TENSOR
REMARK 3 S11: 0.1710 S12: 0.3258 S13: -0.0438
REMARK 3 S21: -0.5392 S22: -0.1235 S23: 0.1565
REMARK 3 S31: -0.1339 S32: -0.0391 S33: -0.0475
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 45 A 54
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6586 -17.1267 -13.2243
REMARK 3 T TENSOR
REMARK 3 T11: 0.4400 T22: 0.4264
REMARK 3 T33: 0.4851 T12: -0.1596
REMARK 3 T13: 0.1232 T23: -0.1698
REMARK 3 L TENSOR
REMARK 3 L11: 7.1336 L22: 9.5868
REMARK 3 L33: 2.3464 L12: 3.7036
REMARK 3 L13: 1.5653 L23: -3.0495
REMARK 3 S TENSOR
REMARK 3 S11: 0.3517 S12: -0.4022 S13: -0.1561
REMARK 3 S21: -0.9587 S22: 0.0593 S23: 0.9437
REMARK 3 S31: 0.7525 S32: -0.3355 S33: -0.4110
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 55 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9147 -2.8649 -1.5906
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.1321
REMARK 3 T33: 0.1191 T12: -0.0226
REMARK 3 T13: 0.0640 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 5.1868 L22: 8.5578
REMARK 3 L33: 6.3791 L12: -0.3873
REMARK 3 L13: -2.0380 L23: 4.6386
REMARK 3 S TENSOR
REMARK 3 S11: -0.1965 S12: 0.0378 S13: -0.0078
REMARK 3 S21: -0.1627 S22: 0.0219 S23: -0.5318
REMARK 3 S31: 0.0958 S32: 0.3918 S33: 0.1746
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 69 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): 43.9241 0.2242 1.8224
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.1467
REMARK 3 T33: 0.1271 T12: -0.0187
REMARK 3 T13: 0.0196 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 4.3281 L22: 7.0718
REMARK 3 L33: 4.4438 L12: 0.4380
REMARK 3 L13: 0.7894 L23: 2.5789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: -0.0436 S13: 0.0894
REMARK 3 S21: -0.0076 S22: 0.1238 S23: -0.2281
REMARK 3 S31: -0.1516 S32: 0.2710 S33: -0.0291
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 82 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7177 -7.2040 2.0770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1597 T22: 0.0964
REMARK 3 T33: 0.1113 T12: 0.0020
REMARK 3 T13: 0.0036 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.9479 L22: 1.5383
REMARK 3 L33: 1.3104 L12: 0.5922
REMARK 3 L13: 0.1862 L23: 0.8551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: -0.0233 S13: -0.0030
REMARK 3 S21: -0.0062 S22: 0.0116 S23: 0.0558
REMARK 3 S31: 0.0516 S32: 0.0051 S33: 0.0438
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 104 A 116
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8778 -14.3174 -15.2822
REMARK 3 T TENSOR
REMARK 3 T11: 0.2230 T22: 0.1668
REMARK 3 T33: 0.0704 T12: -0.0730
REMARK 3 T13: -0.0066 T23: -0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 3.4423 L22: 8.8363
REMARK 3 L33: 6.8544 L12: -1.2482
REMARK 3 L13: -1.3447 L23: 2.8243
REMARK 3 S TENSOR
REMARK 3 S11: -0.2456 S12: 0.6731 S13: -0.2570
REMARK 3 S21: -0.5472 S22: 0.0623 S23: -0.0338
REMARK 3 S31: 0.2443 S32: 0.1629 S33: 0.1833
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 117 A 125
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7953 -19.5978 -5.5498
REMARK 3 T TENSOR
REMARK 3 T11: 0.1275 T22: 0.0988
REMARK 3 T33: 0.1744 T12: -0.0201
REMARK 3 T13: -0.0046 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 1.5941 L22: 2.5636
REMARK 3 L33: 8.2991 L12: 0.5218
REMARK 3 L13: -1.5102 L23: 1.3408
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: 0.1487 S13: -0.1423
REMARK 3 S21: -0.2089 S22: -0.0399 S23: -0.0141
REMARK 3 S31: 0.1522 S32: 0.2178 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 126 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5895 -6.4930 4.8233
REMARK 3 T TENSOR
REMARK 3 T11: 0.1482 T22: 0.1174
REMARK 3 T33: 0.1298 T12: -0.0288
REMARK 3 T13: 0.0316 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.2999 L22: 2.6364
REMARK 3 L33: 2.0314 L12: 0.0139
REMARK 3 L13: 0.3132 L23: 0.5991
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: -0.1556 S13: -0.0171
REMARK 3 S21: 0.1372 S22: -0.0718 S23: 0.2771
REMARK 3 S31: 0.0699 S32: -0.2403 S33: 0.1439
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 158 A 172
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3545 9.1625 12.5515
REMARK 3 T TENSOR
REMARK 3 T11: 0.1724 T22: 0.1004
REMARK 3 T33: 0.1312 T12: 0.0353
REMARK 3 T13: 0.0072 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 5.3688 L22: 4.1965
REMARK 3 L33: 3.7783 L12: 0.8703
REMARK 3 L13: 1.9977 L23: -0.3154
REMARK 3 S TENSOR
REMARK 3 S11: 0.1016 S12: -0.3345 S13: 0.0007
REMARK 3 S21: 0.2589 S22: -0.1095 S23: 0.2396
REMARK 3 S31: -0.0709 S32: -0.2373 S33: 0.0079
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3IIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054456.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-07
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 : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04498
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 WITH SAGITTAL FOCUSSING
REMARK 200 OPTICS : RH COATED MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22102
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 34.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1RKB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 1.5 M LI2SO4, 0.2
REMARK 280 M NACL, 0.5 MM DTT, 25 MM MGCL2, 25 MM P1,P5-DI(ADENOSINE-5')
REMARK 280 PENTAPHOSPHATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 19.34933
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 38.69867
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 29.02400
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 48.37333
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 9.67467
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLY A -7
REMARK 465 PRO A -6
REMARK 465 LEU A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
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 O HOH A 237 O HOH A 355 2.08
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 PHE A 0 15.75 59.66
REMARK 500 ASP A 52 77.86 51.41
REMARK 500 CYS A 53 148.09 -173.41
REMARK 500 CYS A 81 -2.58 -160.13
REMARK 500 SER A 146 59.71 -141.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 175 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A -1 O
REMARK 620 2 HOH A 351 O 66.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 177 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 ADP A 174 O3B 84.6
REMARK 620 3 HOH A 206 O 90.1 100.1
REMARK 620 4 HOH A 213 O 177.4 96.3 87.3
REMARK 620 5 HOH A 220 O 88.3 84.9 174.5 94.3
REMARK 620 6 HOH A 221 O 88.2 170.4 86.3 91.1 88.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LI A 173
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 181
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 182
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RKB RELATED DB: PDB
REMARK 900 THE STRUCTURE OF ADRENAL GLAND PROTEIN AD-004
REMARK 900 RELATED ID: 3IIJ RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HCINAP-ADP COMPLEX AT 1.76 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 3IIK RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HCINAP-SO4 COMPLEX AT 1.95 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 3IIM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HCINAP-DADP COMPLEX AT 2.0 ANGSTROMS RESOLUTION
DBREF 3IIL A 1 172 UNP Q5F2S9 Q5F2S9_HUMAN 1 172
SEQADV 3IIL GLY A -7 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL PRO A -6 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL LEU A -5 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL GLY A -4 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL SER A -3 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL PRO A -2 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL GLU A -1 UNP Q5F2S9 EXPRESSION TAG
SEQADV 3IIL PHE A 0 UNP Q5F2S9 EXPRESSION TAG
SEQRES 1 A 180 GLY PRO LEU GLY SER PRO GLU PHE MET LEU LEU PRO ASN
SEQRES 2 A 180 ILE LEU LEU THR GLY THR PRO GLY VAL GLY LYS THR THR
SEQRES 3 A 180 LEU GLY LYS GLU LEU ALA SER LYS SER GLY LEU LYS TYR
SEQRES 4 A 180 ILE ASN VAL GLY ASP LEU ALA ARG GLU GLU GLN LEU TYR
SEQRES 5 A 180 ASP GLY TYR ASP GLU GLU TYR ASP CYS PRO ILE LEU ASP
SEQRES 6 A 180 GLU ASP ARG VAL VAL ASP GLU LEU ASP ASN GLN MET ARG
SEQRES 7 A 180 GLU GLY GLY VAL ILE VAL ASP TYR HIS GLY CYS ASP PHE
SEQRES 8 A 180 PHE PRO GLU ARG TRP PHE HIS ILE VAL PHE VAL LEU ARG
SEQRES 9 A 180 THR ASP THR ASN VAL LEU TYR GLU ARG LEU GLU THR ARG
SEQRES 10 A 180 GLY TYR ASN GLU LYS LYS LEU THR ASP ASN ILE GLN CYS
SEQRES 11 A 180 GLU ILE PHE GLN VAL LEU TYR GLU GLU ALA THR ALA SER
SEQRES 12 A 180 TYR LYS GLU GLU ILE VAL HIS GLN LEU PRO SER ASN LYS
SEQRES 13 A 180 PRO GLU GLU LEU GLU ASN ASN VAL ASP GLN ILE LEU LYS
SEQRES 14 A 180 TRP ILE GLU GLN TRP ILE LYS ASP HIS ASN SER
HET LI A 173 1
HET ADP A 174 27
HET MG A 175 1
HET MG A 176 1
HET MG A 177 1
HET PO4 A 178 5
HET SO4 A 179 5
HET SO4 A 180 5
HET SO4 A 181 5
HET SO4 A 182 5
HETNAM LI LITHIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM SO4 SULFATE ION
FORMUL 2 LI LI 1+
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 MG 3(MG 2+)
FORMUL 7 PO4 O4 P 3-
FORMUL 8 SO4 4(O4 S 2-)
FORMUL 12 HOH *201(H2 O)
HELIX 1 1 GLY A 15 GLY A 28 1 14
HELIX 2 2 VAL A 34 GLU A 41 1 8
HELIX 3 3 ASP A 57 GLY A 72 1 16
HELIX 4 4 PRO A 85 PHE A 89 5 5
HELIX 5 5 ASP A 98 ARG A 109 1 12
HELIX 6 6 ASN A 112 PHE A 125 1 14
HELIX 7 7 GLN A 126 TYR A 136 1 11
HELIX 8 8 LYS A 137 GLU A 139 5 3
HELIX 9 9 LYS A 148 HIS A 170 1 23
SHEET 1 A 5 LYS A 30 ASN A 33 0
SHEET 2 A 5 VAL A 74 ASP A 77 1 O ILE A 75 N LYS A 30
SHEET 3 A 5 ILE A 6 THR A 9 1 N LEU A 8 O VAL A 76
SHEET 4 A 5 ILE A 91 ARG A 96 1 O PHE A 93 N LEU A 7
SHEET 5 A 5 VAL A 141 PRO A 145 1 O LEU A 144 N ARG A 96
SHEET 1 B 2 TYR A 44 ASP A 48 0
SHEET 2 B 2 CYS A 53 LEU A 56 -1 O ILE A 55 N GLY A 46
LINK O GLU A -1 MG MG A 175 1555 1555 2.27
LINK OG1 THR A 17 MG MG A 177 1555 1555 2.15
LINK LI LI A 173 O HOH A 208 1555 1555 2.14
LINK O3B ADP A 174 MG MG A 177 1555 1555 2.11
LINK MG MG A 175 O HOH A 351 1555 1555 2.60
LINK MG MG A 176 O HOH A 363 1555 1555 2.71
LINK MG MG A 177 O HOH A 206 1555 1555 2.09
LINK MG MG A 177 O HOH A 213 1555 1555 2.19
LINK MG MG A 177 O HOH A 220 1555 1555 2.18
LINK MG MG A 177 O HOH A 221 1555 1555 2.18
SITE 1 AC1 3 PRO A 12 TYR A 111 HOH A 208
SITE 1 AC2 21 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC2 21 THR A 17 THR A 18 ARG A 105 ARG A 109
SITE 3 AC2 21 SER A 146 ASN A 147 LYS A 148 PRO A 149
SITE 4 AC2 21 LEU A 152 MG A 177 HOH A 204 HOH A 213
SITE 5 AC2 21 HOH A 220 HOH A 223 HOH A 227 HOH A 231
SITE 6 AC2 21 HOH A 313
SITE 1 AC3 3 PRO A -2 GLU A -1 HOH A 351
SITE 1 AC4 3 TYR A 51 ASP A 118 HOH A 363
SITE 1 AC5 6 THR A 17 ADP A 174 HOH A 206 HOH A 213
SITE 2 AC5 6 HOH A 220 HOH A 221
SITE 1 AC6 11 PRO A 12 LYS A 16 TYR A 78 HIS A 79
SITE 2 AC6 11 HOH A 203 HOH A 206 HOH A 208 HOH A 209
SITE 3 AC6 11 HOH A 211 HOH A 213 HOH A 246
SITE 1 AC7 6 TYR A 129 HIS A 142 GLN A 143 HOH A 277
SITE 2 AC7 6 HOH A 307 HOH A 323
SITE 1 AC8 4 LYS A 137 GLU A 138 GLU A 139 HOH A 341
SITE 1 AC9 3 ASN A 112 GLU A 113 HOH A 192
SITE 1 BC1 6 ARG A 60 HIS A 170 HOH A 222 HOH A 281
SITE 2 BC1 6 HOH A 328 HOH A 380
CRYST1 99.173 99.173 58.048 90.00 90.00 120.00 P 61 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 0.010083 0.005822 0.000000 0.00000
SCALE2 0.000000 0.011643 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017227 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
