HEADER METAL BINDING PROTEIN 28-JAN-10 3LLE
TITLE X-RAY STRUCTURE OF BOVINE SC0322,CA(2+)-S100B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100 CALCIUM-BINDING PROTEIN B, S-100 PROTEIN SUBUNIT BETA,
COMPND 5 S-100 PROTEIN BETA CHAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: S100B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS EF HAND, ALPHA HELICAL, METAL-BINDING, NUCLEUS, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.H.CHARPENTIER,D.J.WEBER,P.W.WILDER
REVDAT 2 01-NOV-17 3LLE 1 REMARK
REVDAT 1 29-DEC-10 3LLE 0
JRNL AUTH P.T.WILDER,T.H.CHARPENTIER,M.A.LIRIANO,K.GIANNI,K.M.VARNEY,
JRNL AUTH 2 E.POZHARSKI,A.COOP,E.A.TOTH,A.D.MACKERELL,D.J.WEBER
JRNL TITL IN VITRO SCREENING AND STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 INHIBITORS OF THE S100B-P53 INTERACTION.
JRNL REF INT.J.HIGH THROUGHPUT SCREEN V.2010 109 2010
JRNL REFN ESSN 1179-1381
JRNL PMID 21132089
JRNL DOI 10.2147/IJHTS.S8210
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 19136
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 982
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1202
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.33000
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): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.262
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1568 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2117 ; 2.461 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 188 ; 4.931 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;28.007 ;26.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;16.694 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;17.470 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 231 ; 0.374 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1170 ; 0.013 ; 0.020
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): 905 ; 1.063 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1458 ; 1.656 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 663 ; 2.962 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 654 ; 4.158 ; 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 0 A 5
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4260 -9.5433 -11.4779
REMARK 3 T TENSOR
REMARK 3 T11: 0.1921 T22: 0.3784
REMARK 3 T33: 0.2410 T12: 0.0612
REMARK 3 T13: -0.0243 T23: -0.0800
REMARK 3 L TENSOR
REMARK 3 L11: 14.5732 L22: 35.8949
REMARK 3 L33: 11.0363 L12: 2.3119
REMARK 3 L13: -3.4364 L23: 2.1659
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: 0.1983 S13: -0.4452
REMARK 3 S21: 0.0615 S22: 0.5273 S23: -2.1802
REMARK 3 S31: -0.2054 S32: 1.6650 S33: -0.5710
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 6 A 16
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5143 1.6537 -8.3921
REMARK 3 T TENSOR
REMARK 3 T11: 0.3235 T22: 0.0819
REMARK 3 T33: 0.0586 T12: 0.0358
REMARK 3 T13: 0.0017 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 10.4966 L22: 18.9979
REMARK 3 L33: 1.9206 L12: -12.1811
REMARK 3 L13: -3.8958 L23: 3.1706
REMARK 3 S TENSOR
REMARK 3 S11: 0.2190 S12: -0.2025 S13: 0.3631
REMARK 3 S21: -0.3985 S22: -0.0354 S23: -0.4136
REMARK 3 S31: -0.2358 S32: 0.1311 S33: -0.1836
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 17 A 40
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2031 11.3826 -10.1456
REMARK 3 T TENSOR
REMARK 3 T11: 0.2545 T22: 0.0875
REMARK 3 T33: 0.1112 T12: 0.0927
REMARK 3 T13: -0.0410 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 4.3374 L22: 5.7173
REMARK 3 L33: 8.2607 L12: -0.5632
REMARK 3 L13: -1.0772 L23: 0.5419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1466 S12: -0.4096 S13: 0.2901
REMARK 3 S21: 0.0438 S22: 0.1091 S23: 0.1737
REMARK 3 S31: -0.7929 S32: -0.1363 S33: -0.2557
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 41 A 63
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3547 11.1010 -20.8687
REMARK 3 T TENSOR
REMARK 3 T11: 0.3150 T22: 0.1040
REMARK 3 T33: 0.1508 T12: 0.1418
REMARK 3 T13: -0.0888 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 4.3903 L22: 2.4905
REMARK 3 L33: 3.4975 L12: -1.9198
REMARK 3 L13: -0.9906 L23: -0.1212
REMARK 3 S TENSOR
REMARK 3 S11: 0.2125 S12: 0.0325 S13: -0.1210
REMARK 3 S21: -0.4241 S22: -0.1034 S23: 0.1662
REMARK 3 S31: -0.3186 S32: -0.1830 S33: -0.1091
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 64 A 78
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9704 1.5252 -13.3068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.0812
REMARK 3 T33: 0.1973 T12: 0.0771
REMARK 3 T13: -0.0819 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 3.1477 L22: 7.9011
REMARK 3 L33: 9.8453 L12: -3.0397
REMARK 3 L13: 0.3400 L23: 2.4643
REMARK 3 S TENSOR
REMARK 3 S11: 0.1220 S12: -0.1431 S13: -0.3782
REMARK 3 S21: -0.1653 S22: -0.0508 S23: 0.6793
REMARK 3 S31: -0.0310 S32: -0.3535 S33: -0.0712
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 79 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3271 -4.1400 -28.9372
REMARK 3 T TENSOR
REMARK 3 T11: 1.0456 T22: 0.1696
REMARK 3 T33: 0.1852 T12: 0.0684
REMARK 3 T13: -0.0314 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 10.4751 L22: 9.1384
REMARK 3 L33: 12.6433 L12: -6.2056
REMARK 3 L13: -8.7920 L23: 7.0283
REMARK 3 S TENSOR
REMARK 3 S11: 0.0828 S12: 0.1636 S13: -0.4090
REMARK 3 S21: -2.2554 S22: -0.0313 S23: 0.0732
REMARK 3 S31: -0.6141 S32: 0.4169 S33: -0.0515
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 : B 0 B 5
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2069 3.8407 -17.8632
REMARK 3 T TENSOR
REMARK 3 T11: 0.2033 T22: 0.2159
REMARK 3 T33: 0.1456 T12: 0.0927
REMARK 3 T13: -0.0185 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 7.6917 L22: 19.8138
REMARK 3 L33: 13.9421 L12: -0.3088
REMARK 3 L13: -3.6809 L23: 2.5834
REMARK 3 S TENSOR
REMARK 3 S11: -0.1746 S12: -0.1489 S13: 0.0026
REMARK 3 S21: -0.2720 S22: 0.0269 S23: -0.9029
REMARK 3 S31: 0.2431 S32: 1.1643 S33: 0.1477
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 : B 6 B 16
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5104 -8.4679 -21.4501
REMARK 3 T TENSOR
REMARK 3 T11: 0.4885 T22: 0.2154
REMARK 3 T33: 0.0825 T12: 0.2464
REMARK 3 T13: -0.0189 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 3.9092 L22: 17.3001
REMARK 3 L33: 2.2350 L12: 6.8369
REMARK 3 L13: 2.9006 L23: 5.7377
REMARK 3 S TENSOR
REMARK 3 S11: 0.3899 S12: 0.3427 S13: -0.1489
REMARK 3 S21: -0.0903 S22: -0.2981 S23: -0.0212
REMARK 3 S31: 0.2012 S32: 0.1457 S33: -0.0918
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 : B 17 B 40
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5447 -19.2809 -20.8583
REMARK 3 T TENSOR
REMARK 3 T11: 0.4107 T22: 0.1270
REMARK 3 T33: 0.2421 T12: 0.1657
REMARK 3 T13: -0.1952 T23: -0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 4.3781 L22: 4.1504
REMARK 3 L33: 8.2432 L12: -1.3042
REMARK 3 L13: 1.4951 L23: 0.9608
REMARK 3 S TENSOR
REMARK 3 S11: 0.5167 S12: 0.4287 S13: -0.6633
REMARK 3 S21: -0.6583 S22: -0.2935 S23: 0.3139
REMARK 3 S31: 0.6533 S32: -0.1710 S33: -0.2232
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 : B 41 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2803 -20.4962 -10.9129
REMARK 3 T TENSOR
REMARK 3 T11: 0.3148 T22: 0.1380
REMARK 3 T33: 0.3500 T12: -0.0016
REMARK 3 T13: -0.0973 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 5.6948 L22: 4.9281
REMARK 3 L33: 5.5534 L12: 0.5206
REMARK 3 L13: 3.3116 L23: 0.4132
REMARK 3 S TENSOR
REMARK 3 S11: 0.3688 S12: -0.2955 S13: -0.8466
REMARK 3 S21: -0.0854 S22: -0.0315 S23: 0.6435
REMARK 3 S31: 0.8578 S32: -0.4953 S33: -0.3373
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 : B 64 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9797 -11.5992 -18.8276
REMARK 3 T TENSOR
REMARK 3 T11: 0.2588 T22: 0.1189
REMARK 3 T33: 0.2537 T12: 0.1046
REMARK 3 T13: -0.1990 T23: -0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 3.5845 L22: 4.2428
REMARK 3 L33: 8.3659 L12: -1.2156
REMARK 3 L13: -0.8434 L23: 1.3841
REMARK 3 S TENSOR
REMARK 3 S11: 0.3609 S12: 0.3778 S13: -0.3605
REMARK 3 S21: -0.6414 S22: -0.2045 S23: 0.4533
REMARK 3 S31: 0.3530 S32: -0.2752 S33: -0.1563
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 : B 79 B 89
REMARK 3 ORIGIN FOR THE GROUP (A): -10.6577 -3.8271 -1.8767
REMARK 3 T TENSOR
REMARK 3 T11: 0.1501 T22: 0.1628
REMARK 3 T33: 0.5367 T12: 0.0715
REMARK 3 T13: 0.1236 T23: -0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 10.2794 L22: 6.2796
REMARK 3 L33: 19.8619 L12: 7.5959
REMARK 3 L13: 11.8701 L23: 6.9911
REMARK 3 S TENSOR
REMARK 3 S11: -0.1388 S12: -0.6876 S13: 1.2606
REMARK 3 S21: 0.0147 S22: -0.6473 S23: 1.3205
REMARK 3 S31: 0.0803 S32: -0.4928 S33: 0.7860
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3LLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.80000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.51900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 1.3.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, CACL2, LI2SO4, CACODYLATE
REMARK 280 BUFFER, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 114.94200
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 57.47100
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 57.47100
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 114.94200
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -184.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 HIS A 90
REMARK 465 GLU A 91
REMARK 465 HIS B 90
REMARK 465 GLU B 91
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 70 CE1 PHE A 70 CZ 0.123
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 LEU B 3 CB - CG - CD2 ANGL. DEV. = 12.5 DEGREES
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 CA B 93 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 61 OD1
REMARK 620 2 GLU B 67 O 92.3
REMARK 620 3 ASP B 65 OD1 94.5 79.4
REMARK 620 4 GLU B 72 OE1 106.8 77.7 149.1
REMARK 620 5 ASP B 63 OD1 76.2 159.8 84.9 121.3
REMARK 620 6 GLU B 72 OE2 82.4 122.9 157.5 50.8 72.7
REMARK 620 7 HOH B 112 O 166.3 92.4 73.8 86.7 95.4 105.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 93 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD1
REMARK 620 2 GLU A 67 O 162.0
REMARK 620 3 ASP A 61 OD1 83.1 87.4
REMARK 620 4 ASP A 65 OD1 82.8 81.3 85.7
REMARK 620 5 GLU A 72 OE1 120.3 77.4 110.9 152.1
REMARK 620 6 GLU A 72 OE2 73.5 122.1 91.5 156.3 49.4
REMARK 620 7 HOH A 147 O 85.0 100.7 163.0 80.8 85.6 96.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 92 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 18 O
REMARK 620 2 LYS B 26 O 94.6
REMARK 620 3 GLU B 21 O 96.6 159.9
REMARK 620 4 ASP B 23 O 79.4 82.6 83.1
REMARK 620 5 GLU B 31 OE1 103.6 79.6 113.7 162.1
REMARK 620 6 GLU B 31 OE2 81.2 125.9 72.6 146.7 50.2
REMARK 620 7 HOH B 129 O 174.0 83.8 83.3 94.6 81.8 104.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 92 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 O
REMARK 620 2 ASP A 23 O 82.6
REMARK 620 3 LYS A 26 O 89.5 80.8
REMARK 620 4 GLU A 21 O 99.7 83.9 161.0
REMARK 620 5 GLU A 31 OE2 79.3 149.5 123.1 75.3
REMARK 620 6 GLU A 31 OE1 101.8 156.9 76.6 117.1 52.4
REMARK 620 7 HOH A 104 O 168.9 87.6 83.7 84.5 111.7 85.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGE A 94
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGE B 94
DBREF 3LLE A 0 91 UNP P02638 S100B_BOVIN 1 92
DBREF 3LLE B 0 91 UNP P02638 S100B_BOVIN 1 92
SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA VAL VAL ALA LEU ILE ASP
SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP SER ASP GLY
SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 92 ALA MET ILE THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 A 92 GLU
SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA VAL VAL ALA LEU ILE ASP
SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP SER ASP GLY
SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 B 92 ALA MET ILE THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 B 92 GLU
HET CA A 92 1
HET CA A 93 1
HET SGE A 94 25
HET CA B 92 1
HET CA B 93 1
HET SGE B 94 25
HETNAM CA CALCIUM ION
HETNAM SGE 13-METHYL-13,14-DIHYDRO[1,3]BENZODIOXOLO[5,6-C][1,
HETNAM 2 SGE 3]DIOXOLO[4,5-I]PHENANTHRIDINE
FORMUL 3 CA 4(CA 2+)
FORMUL 5 SGE 2(C20 H15 N O4)
FORMUL 9 HOH *123(H2 O)
HELIX 1 1 SER A 1 GLY A 19 1 19
HELIX 2 2 LYS A 28 LEU A 40 1 13
HELIX 3 3 GLU A 49 ASP A 61 1 13
HELIX 4 4 ASP A 69 THR A 81 1 13
HELIX 5 5 THR A 82 GLU A 89 5 8
HELIX 6 6 SER B 1 GLY B 19 1 19
HELIX 7 7 LYS B 28 LEU B 40 1 13
HELIX 8 8 GLU B 49 ASP B 61 1 13
HELIX 9 9 ASP B 69 THR B 81 1 13
HELIX 10 10 CYS B 84 GLU B 89 1 6
LINK OD1 ASP B 61 CA CA B 93 1555 1555 2.12
LINK OD1 ASP A 63 CA CA A 93 1555 1555 2.21
LINK O SER B 18 CA CA B 92 1555 1555 2.27
LINK O SER A 18 CA CA A 92 1555 1555 2.29
LINK O GLU A 67 CA CA A 93 1555 1555 2.31
LINK O GLU B 67 CA CA B 93 1555 1555 2.31
LINK OD1 ASP A 61 CA CA A 93 1555 1555 2.34
LINK OD1 ASP A 65 CA CA A 93 1555 1555 2.35
LINK O LYS B 26 CA CA B 92 1555 1555 2.36
LINK OD1 ASP B 65 CA CA B 93 1555 1555 2.36
LINK O ASP A 23 CA CA A 92 1555 1555 2.39
LINK O LYS A 26 CA CA A 92 1555 1555 2.39
LINK O GLU B 21 CA CA B 92 1555 1555 2.39
LINK O GLU A 21 CA CA A 92 1555 1555 2.41
LINK OE2 GLU A 31 CA CA A 92 1555 1555 2.42
LINK O ASP B 23 CA CA B 92 1555 1555 2.43
LINK OE1 GLU A 31 CA CA A 92 1555 1555 2.48
LINK OE1 GLU B 72 CA CA B 93 1555 1555 2.48
LINK OE1 GLU A 72 CA CA A 93 1555 1555 2.50
LINK OD1 ASP B 63 CA CA B 93 1555 1555 2.52
LINK OE1 GLU B 31 CA CA B 92 1555 1555 2.55
LINK OE2 GLU B 31 CA CA B 92 1555 1555 2.55
LINK OE2 GLU B 72 CA CA B 93 1555 1555 2.59
LINK OE2 GLU A 72 CA CA A 93 1555 1555 2.69
LINK SG CYS A 84 CAG SGE A 94 1555 1555 1.77
LINK SG CYS B 84 CAG SGE B 94 1555 1555 1.89
LINK CA CA B 92 O HOH B 129 1555 1555 2.04
LINK CA CA B 93 O HOH B 112 1555 1555 2.19
LINK CA CA A 92 O HOH A 104 1555 1555 2.33
LINK CA CA A 93 O HOH A 147 1555 1555 2.37
SITE 1 AC1 6 SER A 18 GLU A 21 ASP A 23 LYS A 26
SITE 2 AC1 6 GLU A 31 HOH A 104
SITE 1 AC2 6 ASP A 61 ASP A 63 ASP A 65 GLU A 67
SITE 2 AC2 6 GLU A 72 HOH A 147
SITE 1 AC3 7 HIS A 42 PHE A 43 ALA A 83 CYS A 84
SITE 2 AC3 7 PHE A 87 PHE A 88 VAL B 8
SITE 1 AC4 6 SER B 18 GLU B 21 ASP B 23 LYS B 26
SITE 2 AC4 6 GLU B 31 HOH B 129
SITE 1 AC5 6 ASP B 61 ASP B 63 ASP B 65 GLU B 67
SITE 2 AC5 6 GLU B 72 HOH B 112
SITE 1 AC6 6 VAL A 8 HIS B 42 PHE B 43 CYS B 84
SITE 2 AC6 6 PHE B 87 PHE B 88
CRYST1 46.267 46.267 172.413 90.00 90.00 120.00 P 32 2 1 12
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 0.021614 0.012479 0.000000 0.00000
SCALE2 0.000000 0.024957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005800 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
