HEADER SIGNALING PROTEIN 12-DEC-06 2O88
TITLE CRYSTAL STRUCTURE OF THE N114A MUTANT OF ABL-SH3 DOMAIN COMPLEXED WITH
TITLE 2 A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND
TITLE 3 INTERACTIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ABL1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 64-121;
COMPND 5 SYNONYM: P150, C- ABL, ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG
COMPND 6 1;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: P41 PEPTIDE;
COMPND 12 CHAIN: C, D;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: PBAT4;
SOURCE 6 GENE: ABL1, ABL, JTK7;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES
KEYWDS SH3 DOMAIN HIGH AFFINITY PEPTIDE COMPLEX, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CAMARA-ARTIGAS
REVDAT 3 13-JUL-11 2O88 1 VERSN
REVDAT 2 24-FEB-09 2O88 1 VERSN
REVDAT 1 01-MAY-07 2O88 0
JRNL AUTH A.CAMARA-ARTIGAS,A.PALENCIA,J.C.MARTINEZ,I.LUQUE,J.A.GAVIRA,
JRNL AUTH 2 J.M.GARCIA-RUIZ
JRNL TITL CRYSTALLIZATION BY CAPILLARY COUNTER-DIFFUSION AND STRUCTURE
JRNL TITL 2 DETERMINATION OF THE N114A MUTANT OF THE SH3 DOMAIN OF ABL
JRNL TITL 3 TYROSINE KINASE COMPLEXED WITH A HIGH-AFFINITY PEPTIDE
JRNL TITL 4 LIGAND.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 646 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17452790
JRNL DOI 10.1107/S0907444907011109
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 13178
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 647
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 745
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.2680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1037
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 19.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.18000
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): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.793
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1087 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1497 ; 1.744 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 134 ; 5.543 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 45 ;33.415 ;25.111
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 144 ;14.989 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;24.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 156 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 858 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 359 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 728 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 38 ; 0.193 ; 0.200
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): 33 ; 0.155 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.301 ; 0.200
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): 701 ; 1.067 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1110 ; 1.580 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 458 ; 2.361 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 385 ; 3.443 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 65 A 119 4
REMARK 3 1 B 65 B 119 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 428 ; 0.320 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 428 ; 0.880 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 10 4
REMARK 3 1 D 1 D 10 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 75 ; 0.090 ; 0.500
REMARK 3 MEDIUM THERMAL 2 C (A**2): 75 ; 0.490 ; 2.000
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 64 A 74
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4397 -10.1287 13.5651
REMARK 3 T TENSOR
REMARK 3 T11: -0.0901 T22: -0.1067
REMARK 3 T33: -0.2088 T12: 0.0117
REMARK 3 T13: 0.0185 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 10.5777 L22: 15.0570
REMARK 3 L33: 5.1912 L12: 5.4335
REMARK 3 L13: 0.5582 L23: 1.6293
REMARK 3 S TENSOR
REMARK 3 S11: 0.2108 S12: -0.0537 S13: 0.2719
REMARK 3 S21: -0.1049 S22: 0.0164 S23: -0.1308
REMARK 3 S31: -0.1648 S32: 0.0708 S33: -0.2273
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 75 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2682 -14.3911 9.9087
REMARK 3 T TENSOR
REMARK 3 T11: -0.0553 T22: -0.1371
REMARK 3 T33: -0.2044 T12: 0.0045
REMARK 3 T13: -0.0155 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 48.0224 L22: 6.9319
REMARK 3 L33: 2.2929 L12: 10.9001
REMARK 3 L13: -0.5203 L23: 0.4124
REMARK 3 S TENSOR
REMARK 3 S11: -0.1179 S12: 0.0138 S13: -0.6152
REMARK 3 S21: -0.2062 S22: 0.1651 S23: -0.1188
REMARK 3 S31: 0.1754 S32: 0.0346 S33: -0.0472
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 87 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1293 -2.6812 12.0597
REMARK 3 T TENSOR
REMARK 3 T11: -0.0556 T22: -0.0889
REMARK 3 T33: 0.2230 T12: -0.0114
REMARK 3 T13: 0.0008 T23: 0.1056
REMARK 3 L TENSOR
REMARK 3 L11: 35.5955 L22: 7.0815
REMARK 3 L33: 22.0563 L12: -1.1015
REMARK 3 L13: -22.6557 L23: 4.2454
REMARK 3 S TENSOR
REMARK 3 S11: -0.5677 S12: 0.1463 S13: 1.6164
REMARK 3 S21: 0.0141 S22: 0.5235 S23: 1.0688
REMARK 3 S31: -0.0925 S32: 0.3751 S33: 0.0441
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 94 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5271 -9.6135 21.3094
REMARK 3 T TENSOR
REMARK 3 T11: -0.0118 T22: -0.0573
REMARK 3 T33: -0.0345 T12: -0.0462
REMARK 3 T13: 0.0480 T23: -0.0926
REMARK 3 L TENSOR
REMARK 3 L11: 25.3671 L22: 10.7681
REMARK 3 L33: 41.2818 L12: -2.9296
REMARK 3 L13: 6.0128 L23: 10.1890
REMARK 3 S TENSOR
REMARK 3 S11: 0.4464 S12: -1.8503 S13: 0.9096
REMARK 3 S21: 1.1413 S22: -0.3908 S23: 0.8194
REMARK 3 S31: -0.1489 S32: -0.8227 S33: -0.0555
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 101 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9996 -7.1671 12.2045
REMARK 3 T TENSOR
REMARK 3 T11: -0.0709 T22: -0.1046
REMARK 3 T33: -0.1119 T12: -0.0083
REMARK 3 T13: 0.0111 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 9.8850 L22: 4.0983
REMARK 3 L33: 3.8152 L12: 4.0115
REMARK 3 L13: 1.0048 L23: -0.5144
REMARK 3 S TENSOR
REMARK 3 S11: -0.1035 S12: 0.7569 S13: 0.6059
REMARK 3 S21: -0.1611 S22: 0.3381 S23: 0.0412
REMARK 3 S31: -0.3394 S32: 0.2520 S33: -0.2346
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 : B 64 B 81
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6095 -3.5302 0.9099
REMARK 3 T TENSOR
REMARK 3 T11: -0.0941 T22: -0.2160
REMARK 3 T33: -0.1377 T12: -0.0421
REMARK 3 T13: -0.0106 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 12.0372 L22: 4.8029
REMARK 3 L33: 7.1684 L12: -3.3993
REMARK 3 L13: -1.4402 L23: 1.7441
REMARK 3 S TENSOR
REMARK 3 S11: 0.1846 S12: 0.0403 S13: 0.0348
REMARK 3 S21: 0.0249 S22: -0.2220 S23: -0.0663
REMARK 3 S31: 0.0141 S32: -0.0185 S33: 0.0374
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 82 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1139 -6.8420 2.5733
REMARK 3 T TENSOR
REMARK 3 T11: -0.0532 T22: -0.0997
REMARK 3 T33: -0.0679 T12: -0.0486
REMARK 3 T13: -0.0053 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 26.8715 L22: 1.5272
REMARK 3 L33: 21.8163 L12: 3.9249
REMARK 3 L13: -5.3275 L23: -1.4058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0417 S12: -0.2506 S13: -0.5805
REMARK 3 S21: 0.2184 S22: -0.3299 S23: 0.2437
REMARK 3 S31: 0.5753 S32: -0.7375 S33: 0.2882
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 88 B 93
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4538 -2.2689 10.6468
REMARK 3 T TENSOR
REMARK 3 T11: 0.0043 T22: -0.0930
REMARK 3 T33: -0.1136 T12: 0.0057
REMARK 3 T13: -0.0413 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 17.8597 L22: 14.5382
REMARK 3 L33: 4.7684 L12: 12.3674
REMARK 3 L13: -3.7376 L23: 1.8282
REMARK 3 S TENSOR
REMARK 3 S11: -0.6034 S12: -0.2560 S13: 0.0842
REMARK 3 S21: 0.2484 S22: 0.2853 S23: 0.0928
REMARK 3 S31: -0.2949 S32: -0.1054 S33: 0.3181
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 94 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7512 4.9652 3.5082
REMARK 3 T TENSOR
REMARK 3 T11: -0.0737 T22: -0.1112
REMARK 3 T33: -0.0602 T12: -0.0463
REMARK 3 T13: 0.0085 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 15.5422 L22: 24.1529
REMARK 3 L33: 10.4564 L12: -5.3586
REMARK 3 L13: 3.7590 L23: -0.2282
REMARK 3 S TENSOR
REMARK 3 S11: 0.1257 S12: -0.1782 S13: 1.2270
REMARK 3 S21: 0.1030 S22: -0.2405 S23: -0.0016
REMARK 3 S31: -0.6917 S32: 0.6493 S33: 0.1148
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 102 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0019 -3.7559 4.8880
REMARK 3 T TENSOR
REMARK 3 T11: -0.0692 T22: -0.1536
REMARK 3 T33: -0.1833 T12: -0.0227
REMARK 3 T13: 0.0063 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 7.3843 L22: 6.3706
REMARK 3 L33: 3.6019 L12: -3.6985
REMARK 3 L13: 0.5729 L23: -2.0850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: -0.2128 S13: -0.2745
REMARK 3 S21: 0.3101 S22: -0.1401 S23: 0.2659
REMARK 3 S31: 0.1505 S32: -0.0734 S33: 0.1042
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 : C 1 C 10
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6057 -17.4357 20.3005
REMARK 3 T TENSOR
REMARK 3 T11: -0.0397 T22: -0.0989
REMARK 3 T33: -0.0641 T12: -0.0396
REMARK 3 T13: -0.0004 T23: 0.0680
REMARK 3 L TENSOR
REMARK 3 L11: 6.5322 L22: 10.9356
REMARK 3 L33: 12.0380 L12: -7.7112
REMARK 3 L13: 6.9732 L23: -8.6821
REMARK 3 S TENSOR
REMARK 3 S11: -0.1506 S12: -0.0100 S13: 0.1985
REMARK 3 S21: 0.3946 S22: -0.3414 S23: -0.4638
REMARK 3 S31: -0.0291 S32: 0.7284 S33: 0.4920
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 : D 1 D 10
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3061 4.5074 -4.7948
REMARK 3 T TENSOR
REMARK 3 T11: -0.0110 T22: -0.0772
REMARK 3 T33: -0.1117 T12: -0.0081
REMARK 3 T13: 0.0222 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 15.6762 L22: 8.6992
REMARK 3 L33: 7.0921 L12: -4.2844
REMARK 3 L13: 0.6404 L23: -4.5179
REMARK 3 S TENSOR
REMARK 3 S11: 0.2599 S12: 0.2346 S13: 0.0810
REMARK 3 S21: 0.2140 S22: 0.0660 S23: 0.4037
REMARK 3 S31: -0.2438 S32: -0.2469 S33: -0.3259
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 2O88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB040810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : BRUKER MICROSTAR MICRO-FOCUS
REMARK 200 (MONTEL OPTICS)
REMARK 200 OPTICS : BRUKER MICROSTAR MICRO-FOCUS
REMARK 200 (MONTEL OPTICS)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13236
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.06820
REMARK 200 R SYM (I) : 0.04150
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.79
REMARK 200 R MERGE FOR SHELL (I) : 0.24530
REMARK 200 R SYM FOR SHELL (I) : 0.21900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.410
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: PDB ENTRY 1BBZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUN SULPHATE, PH 7, CAPILLARY
REMARK 280 COUNTER DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.08500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.21550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.04650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.21550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.08500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.04650
REMARK 290 SMTRY3 4 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 FORMED BY THE SH3 DOMAIN (CHAIN
REMARK 300 A/B) COMPLEXED WITH THE ACETYLATED PEPTIDE P41 (CHAIN C/D)
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: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 ASN B 120
REMARK 465 SER B 121
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 ASP A 71 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
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 SO4 B 122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 122
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BBZ RELATED DB: PDB
REMARK 900 WT STRUCTURE
DBREF 2O88 A 64 121 UNP P00519 ABL1_HUMAN 64 121
DBREF 2O88 B 64 121 UNP P00519 ABL1_HUMAN 64 121
DBREF 2O88 C 0 10 PDB 2O88 2O88 0 10
DBREF 2O88 D 0 10 PDB 2O88 2O88 0 10
SEQADV 2O88 ALA A 114 UNP P00519 ASN 114 ENGINEERED
SEQADV 2O88 ALA B 114 UNP P00519 ASN 114 ENGINEERED
SEQRES 1 A 58 ASN LEU PHE VAL ALA LEU TYR ASP PHE VAL ALA SER GLY
SEQRES 2 A 58 ASP ASN THR LEU SER ILE THR LYS GLY GLU LYS LEU ARG
SEQRES 3 A 58 VAL LEU GLY TYR ASN HIS ASN GLY GLU TRP CYS GLU ALA
SEQRES 4 A 58 GLN THR LYS ASN GLY GLN GLY TRP VAL PRO SER ALA TYR
SEQRES 5 A 58 ILE THR PRO VAL ASN SER
SEQRES 1 B 58 ASN LEU PHE VAL ALA LEU TYR ASP PHE VAL ALA SER GLY
SEQRES 2 B 58 ASP ASN THR LEU SER ILE THR LYS GLY GLU LYS LEU ARG
SEQRES 3 B 58 VAL LEU GLY TYR ASN HIS ASN GLY GLU TRP CYS GLU ALA
SEQRES 4 B 58 GLN THR LYS ASN GLY GLN GLY TRP VAL PRO SER ALA TYR
SEQRES 5 B 58 ILE THR PRO VAL ASN SER
SEQRES 1 C 11 ACE ALA PRO SER TYR SER PRO PRO PRO PRO PRO
SEQRES 1 D 11 ACE ALA PRO SER TYR SER PRO PRO PRO PRO PRO
HET ACE C 0 3
HET ACE D 0 3
HET SO4 B 122 5
HET SO4 A 122 5
HETNAM ACE ACETYL GROUP
HETNAM SO4 SULFATE ION
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *67(H2 O)
SHEET 1 A 5 GLY A 107 PRO A 112 0
SHEET 2 A 5 TRP A 99 THR A 104 -1 N CYS A 100 O VAL A 111
SHEET 3 A 5 LYS A 87 TYR A 93 -1 N LEU A 91 O GLU A 101
SHEET 4 A 5 LEU A 65 ALA A 68 -1 N PHE A 66 O LEU A 88
SHEET 5 A 5 ILE A 116 PRO A 118 -1 O THR A 117 N VAL A 67
SHEET 1 B 5 GLY B 107 PRO B 112 0
SHEET 2 B 5 TRP B 99 THR B 104 -1 N ALA B 102 O GLY B 109
SHEET 3 B 5 LYS B 87 TYR B 93 -1 N LEU B 91 O GLU B 101
SHEET 4 B 5 PHE B 66 ALA B 68 -1 N PHE B 66 O LEU B 88
SHEET 5 B 5 ILE B 116 PRO B 118 -1 O THR B 117 N VAL B 67
LINK C ACE C 0 N ALA C 1 1555 1555 1.33
LINK C ACE D 0 N ALA D 1 1555 1555 1.33
SITE 1 AC1 6 ARG A 89 ASN B 94 HIS B 95 HOH B 143
SITE 2 AC1 6 ACE D 0 ALA D 1
SITE 1 AC2 6 ASN A 94 HIS A 95 HOH A 133 ARG B 89
SITE 2 AC2 6 ACE C 0 ALA C 1
CRYST1 48.170 50.093 56.431 90.00 90.00 90.00 P 21 21 21 8
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 0.020760 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019963 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
