HEADER HYDROLASE 04-FEB-13 3ZM2
TITLE CATALYTIC DOMAIN OF HUMAN SHP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 248-527;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1D, PTP-1D, PROTEIN-TYROSINE
COMPND 6 PHOSPHATASE 2C, PTP-2C, SH-PTP2, SHP-2, SHP2, SH-PTP3;
COMPND 7 EC: 3.1.3.48;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: SCS1 ROSETTA T1R;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7HT (MODIFIED PET)
KEYWDS HYDROLASE, PTP1B
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BOHM,A.SCHUETZ,Y.ROSKE,U.HEINEMANN
REVDAT 4 20-DEC-23 3ZM2 1 REMARK
REVDAT 3 13-MAY-15 3ZM2 1 JRNL
REVDAT 2 29-APR-15 3ZM2 1 JRNL
REVDAT 1 23-APR-14 3ZM2 0
JRNL AUTH S.GROSSKOPF,C.ECKERT,C.ARKONA,S.RADETZKI,K.BOHM,U.HEINEMANN,
JRNL AUTH 2 G.WOLBER,J.VON KRIES,W.BIRCHMEIER,J.RADEMANN
JRNL TITL SELECTIVE INHIBITORS OF THE PROTEIN TYROSINE PHOSPHATASE
JRNL TITL 2 SHP2 BLOCK CELLULAR MOTILITY AND GROWTH OF CANCER CELLS IN
JRNL TITL 3 VITRO AND IN VIVO.
JRNL REF CHEMMEDCHEM V. 10 815 2015
JRNL REFN ISSN 1860-7179
JRNL PMID 25877780
JRNL DOI 10.1002/CMDC.201500015
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 3 NUMBER OF REFLECTIONS : 39064
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2056
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1662
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2149
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : -0.03000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.11000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.858
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2248 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3048 ; 2.161 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 6.538 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;34.140 ;23.772
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 402 ;15.636 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;21.766 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 330 ; 0.158 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1717 ; 0.013 ; 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): 1335 ; 1.715 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2184 ; 2.716 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 913 ; 4.140 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 860 ; 5.820 ; 6.000
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 : 18
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 244 A 251
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6620 25.9180 49.1940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1037 T22: 0.1252
REMARK 3 T33: 0.0565 T12: 0.0103
REMARK 3 T13: -0.0098 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 2.0137 L22: 0.5217
REMARK 3 L33: 6.2990 L12: -0.2083
REMARK 3 L13: -3.3957 L23: 0.4690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.1629 S13: 0.0992
REMARK 3 S21: 0.0280 S22: 0.1098 S23: 0.0353
REMARK 3 S31: -0.0718 S32: 0.0861 S33: -0.1004
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 252 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8570 17.1060 40.9570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1451 T22: 0.2780
REMARK 3 T33: 0.2169 T12: -0.0573
REMARK 3 T13: 0.0598 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 1.3184 L22: 8.6678
REMARK 3 L33: 25.1328 L12: 1.7169
REMARK 3 L13: 5.0816 L23: 11.7486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0991 S12: 0.2777 S13: -0.1642
REMARK 3 S21: 0.0875 S22: 0.1389 S23: -0.1296
REMARK 3 S31: 0.7084 S32: 0.4070 S33: -0.2380
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 263 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9150 18.5570 19.6570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1076 T22: 0.0478
REMARK 3 T33: 0.0507 T12: 0.0400
REMARK 3 T13: -0.0172 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.7837 L22: 2.1172
REMARK 3 L33: 2.5395 L12: 0.4109
REMARK 3 L13: -0.4459 L23: -0.5522
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: 0.0394 S13: -0.1659
REMARK 3 S21: -0.0637 S22: -0.0839 S23: -0.2385
REMARK 3 S31: 0.3607 S32: 0.2760 S33: -0.0028
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 291 A 303
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6290 22.6270 5.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0944 T22: 0.0727
REMARK 3 T33: 0.0729 T12: -0.0027
REMARK 3 T13: -0.0097 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.1546 L22: 0.6069
REMARK 3 L33: 6.5399 L12: 0.0519
REMARK 3 L13: -0.1673 L23: -0.5802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: 0.0083 S13: -0.0293
REMARK 3 S21: 0.0284 S22: -0.0140 S23: -0.0589
REMARK 3 S31: 0.1972 S32: 0.1918 S33: 0.0504
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 304 A 325
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8850 25.4060 24.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0852 T22: 0.0768
REMARK 3 T33: 0.1051 T12: -0.0341
REMARK 3 T13: 0.0058 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.7213 L22: 3.2462
REMARK 3 L33: 3.0409 L12: -1.0128
REMARK 3 L13: 1.0543 L23: 0.1033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: -0.1355 S13: -0.1414
REMARK 3 S21: 0.2532 S22: 0.0132 S23: 0.3869
REMARK 3 S31: 0.1559 S32: -0.4135 S33: 0.0205
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 326 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1110 30.6140 20.3900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0630 T22: 0.0534
REMARK 3 T33: 0.0609 T12: 0.0057
REMARK 3 T13: -0.0091 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 4.1549 L22: 1.1131
REMARK 3 L33: 4.1761 L12: -0.7321
REMARK 3 L13: -2.4778 L23: 0.5646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: 0.1317 S13: 0.1047
REMARK 3 S21: -0.0836 S22: 0.0241 S23: -0.0691
REMARK 3 S31: 0.0020 S32: 0.1393 S33: -0.0617
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 337 A 361
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3910 35.2390 18.0860
REMARK 3 T TENSOR
REMARK 3 T11: 0.0516 T22: 0.0489
REMARK 3 T33: 0.0598 T12: 0.0042
REMARK 3 T13: 0.0029 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.1264 L22: 0.7048
REMARK 3 L33: 1.3681 L12: -0.0531
REMARK 3 L13: -0.0398 L23: 0.0917
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: 0.0481 S13: -0.0047
REMARK 3 S21: -0.0483 S22: -0.0081 S23: -0.0088
REMARK 3 S31: 0.0174 S32: 0.0137 S33: 0.0159
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 362 A 371
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9190 38.1090 20.9910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0554 T22: 0.0961
REMARK 3 T33: 0.0691 T12: -0.0129
REMARK 3 T13: 0.0181 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 5.7026 L22: 2.7202
REMARK 3 L33: 1.1577 L12: -0.6966
REMARK 3 L13: 0.9247 L23: 0.1579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0124 S12: -0.1852 S13: -0.0699
REMARK 3 S21: 0.1159 S22: 0.0066 S23: -0.1445
REMARK 3 S31: 0.0271 S32: 0.0937 S33: -0.0191
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 372 A 386
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9720 44.5930 8.9500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.0845
REMARK 3 T33: 0.0511 T12: -0.0079
REMARK 3 T13: 0.0158 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.6042 L22: 8.2347
REMARK 3 L33: 2.5568 L12: 1.0649
REMARK 3 L13: 0.5848 L23: 2.1685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: 0.1344 S13: 0.0568
REMARK 3 S21: -0.2829 S22: -0.0448 S23: 0.0413
REMARK 3 S31: -0.1870 S32: 0.0670 S33: 0.0485
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 387 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8360 49.4380 23.2760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.0437
REMARK 3 T33: 0.0694 T12: -0.0095
REMARK 3 T13: -0.0021 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.1644 L22: 2.0372
REMARK 3 L33: 4.5706 L12: -0.0885
REMARK 3 L13: 1.2275 L23: -0.9466
REMARK 3 S TENSOR
REMARK 3 S11: -0.0804 S12: -0.0493 S13: 0.1142
REMARK 3 S21: 0.1661 S22: -0.0569 S23: -0.0366
REMARK 3 S31: -0.4421 S32: -0.0032 S33: 0.1374
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 402 A 416
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1790 41.1050 11.1560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0797 T22: 0.0817
REMARK 3 T33: 0.0794 T12: 0.0123
REMARK 3 T13: -0.0147 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 2.5660 L22: 3.5946
REMARK 3 L33: 8.5718 L12: -0.9258
REMARK 3 L13: 0.2905 L23: 1.6859
REMARK 3 S TENSOR
REMARK 3 S11: 0.0960 S12: 0.3447 S13: -0.0854
REMARK 3 S21: -0.5293 S22: -0.1205 S23: 0.1126
REMARK 3 S31: -0.2016 S32: -0.3303 S33: 0.0245
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 417 A 432
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4680 41.8350 33.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0751 T22: 0.0527
REMARK 3 T33: 0.1569 T12: -0.0282
REMARK 3 T13: -0.0393 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 1.3852 L22: 0.1847
REMARK 3 L33: 4.6738 L12: -0.3906
REMARK 3 L13: 1.7917 L23: -0.9184
REMARK 3 S TENSOR
REMARK 3 S11: -0.0447 S12: 0.0475 S13: 0.1054
REMARK 3 S21: 0.0483 S22: -0.0676 S23: -0.0411
REMARK 3 S31: -0.2105 S32: 0.3720 S33: 0.1123
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 433 A 447
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5080 42.6150 32.4000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0654 T22: 0.0639
REMARK 3 T33: 0.1233 T12: 0.0074
REMARK 3 T13: 0.0359 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 3.2765 L22: 0.5275
REMARK 3 L33: 5.3334 L12: -0.5059
REMARK 3 L13: 3.7322 L23: 0.1186
REMARK 3 S TENSOR
REMARK 3 S11: -0.0885 S12: -0.1883 S13: 0.1131
REMARK 3 S21: 0.0117 S22: -0.0554 S23: 0.0088
REMARK 3 S31: -0.1224 S32: -0.3529 S33: 0.1438
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 448 A 476
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1460 33.3110 29.4960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0403 T22: 0.0392
REMARK 3 T33: 0.0504 T12: -0.0060
REMARK 3 T13: 0.0016 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.8441 L22: 0.8145
REMARK 3 L33: 1.3266 L12: -0.1535
REMARK 3 L13: 0.2230 L23: -0.1560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: -0.0169 S13: 0.0087
REMARK 3 S21: 0.0141 S22: 0.0043 S23: 0.0402
REMARK 3 S31: -0.0125 S32: -0.0551 S33: -0.0102
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 477 A 487
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1020 33.1010 42.8930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.2807
REMARK 3 T33: 0.1905 T12: -0.0279
REMARK 3 T13: 0.0598 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 3.9736 L22: 5.3745
REMARK 3 L33: 8.6549 L12: 1.2251
REMARK 3 L13: -1.9247 L23: -3.3967
REMARK 3 S TENSOR
REMARK 3 S11: -0.1033 S12: -0.2099 S13: -0.3273
REMARK 3 S21: 0.1832 S22: 0.2073 S23: 0.7613
REMARK 3 S31: 0.2359 S32: -1.1442 S33: -0.1039
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 488 A 503
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1540 22.5390 36.6670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0742 T22: 0.0445
REMARK 3 T33: 0.0659 T12: -0.0120
REMARK 3 T13: -0.0133 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.0302 L22: 1.9385
REMARK 3 L33: 5.8795 L12: 0.1301
REMARK 3 L13: -0.2369 L23: 0.4175
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.1119 S13: -0.0528
REMARK 3 S21: 0.1722 S22: 0.0336 S23: 0.1338
REMARK 3 S31: 0.2488 S32: -0.2389 S33: -0.0328
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 504 A 519
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3240 31.2090 42.2960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0601 T22: 0.0557
REMARK 3 T33: 0.0469 T12: -0.0087
REMARK 3 T13: -0.0084 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 3.3450 L22: 3.5428
REMARK 3 L33: 3.2109 L12: -0.6630
REMARK 3 L13: -0.8445 L23: 1.1164
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: -0.1548 S13: -0.0110
REMARK 3 S21: 0.1679 S22: 0.0741 S23: -0.0732
REMARK 3 S31: 0.1075 S32: 0.0837 S33: -0.0316
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 520 A 524
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6340 41.3750 46.0050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2294 T22: 0.3696
REMARK 3 T33: 0.2611 T12: 0.2029
REMARK 3 T13: 0.1213 T23: -0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 10.8240 L22: 4.4779
REMARK 3 L33: 1.8909 L12: -6.0831
REMARK 3 L13: -2.8222 L23: 0.4829
REMARK 3 S TENSOR
REMARK 3 S11: -0.2741 S12: -0.9871 S13: 1.0061
REMARK 3 S21: 0.6289 S22: 0.8905 S23: -0.2235
REMARK 3 S31: -0.4403 S32: -0.1402 S33: -0.6163
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. RESIDUES 256-261, 314-323 AND 408-410 ARE DISORDERED.
REMARK 4
REMARK 4 3ZM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1290055670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.240
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 3B7O
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-22% (W/V) PEG3350 0.1-0.2 M SODIUM
REMARK 280 CITRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 GLN A 256
REMARK 465 GLN A 257
REMARK 465 GLU A 258
REMARK 465 CYS A 259
REMARK 465 LYS A 260
REMARK 465 LEU A 261
REMARK 465 GLU A 312A
REMARK 465 PHE A 312B
REMARK 465 GLU A 312C
REMARK 465 LYS A 317
REMARK 465 CYS A 318
REMARK 465 ASN A 319
REMARK 465 ASN A 320
REMARK 465 SER A 321
REMARK 465 LYS A 322
REMARK 465 PRO A 323
REMARK 465 GLN A 408
REMARK 465 GLY A 409
REMARK 465 ASN A 410
REMARK 465 GLN A 526
REMARK 465 ARG A 527
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 CD2 LEU A 439 CE2 PHE A 469 1.43
REMARK 500 CD ARG A 421 O HOH A 2150 1.79
REMARK 500 CD2 LEU A 439 CZ PHE A 469 1.81
REMARK 500 OG SER A 264 OD2 ASP A 286 2.06
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 ARG A 351 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 384 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 384 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 413 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 431 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 465 CG - CD - NE ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A 512 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 512 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
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 LYS A 389 134.24 -179.14
REMARK 500 VAL A 406 -36.82 -37.77
REMARK 500 ILE A 463 -39.46 -130.82
REMARK 500 VAL A 505 99.63 71.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZM0 RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HUMAN SHP2
REMARK 900 RELATED ID: 3ZM1 RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HUMAN SHP2
REMARK 900 RELATED ID: 3ZM3 RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HUMAN SHP2
DBREF 3ZM2 A 248 527 UNP Q06124 PTN11_HUMAN 248 527
SEQADV 3ZM2 GLY A 244 UNP Q06124 EXPRESSION TAG
SEQADV 3ZM2 ALA A 245 UNP Q06124 EXPRESSION TAG
SEQADV 3ZM2 HIS A 246 UNP Q06124 EXPRESSION TAG
SEQADV 3ZM2 MET A 247 UNP Q06124 EXPRESSION TAG
SEQRES 1 A 284 GLY ALA HIS MET TRP GLU GLU PHE GLU THR LEU GLN GLN
SEQRES 2 A 284 GLN GLU CYS LYS LEU LEU TYR SER ARG LYS GLU GLY GLN
SEQRES 3 A 284 ARG GLN GLU ASN LYS ASN LYS ASN ARG TYR LYS ASN ILE
SEQRES 4 A 284 LEU PRO PHE ASP HIS THR ARG VAL VAL LEU HIS ASP GLY
SEQRES 5 A 284 ASP PRO ASN GLU PRO VAL SER ASP TYR ILE ASN ALA ASN
SEQRES 6 A 284 ILE ILE MET PRO GLU PHE GLU THR LYS CYS ASN ASN SER
SEQRES 7 A 284 LYS PRO LYS LYS SER TYR ILE ALA THR GLN GLY CYS LEU
SEQRES 8 A 284 GLN ASN THR VAL ASN ASP PHE TRP ARG MET VAL PHE GLN
SEQRES 9 A 284 GLU ASN SER ARG VAL ILE VAL MET THR THR LYS GLU VAL
SEQRES 10 A 284 GLU ARG GLY LYS SER LYS CYS VAL LYS TYR TRP PRO ASP
SEQRES 11 A 284 GLU TYR ALA LEU LYS GLU TYR GLY VAL MET ARG VAL ARG
SEQRES 12 A 284 ASN VAL LYS GLU SER ALA ALA HIS ASP TYR THR LEU ARG
SEQRES 13 A 284 GLU LEU LYS LEU SER LYS VAL GLY GLN GLY ASN THR GLU
SEQRES 14 A 284 ARG THR VAL TRP GLN TYR HIS PHE ARG THR TRP PRO ASP
SEQRES 15 A 284 HIS GLY VAL PRO SER ASP PRO GLY GLY VAL LEU ASP PHE
SEQRES 16 A 284 LEU GLU GLU VAL HIS HIS LYS GLN GLU SER ILE MET ASP
SEQRES 17 A 284 ALA GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY
SEQRES 18 A 284 ARG THR GLY THR PHE ILE VAL ILE ASP ILE LEU ILE ASP
SEQRES 19 A 284 ILE ILE ARG GLU LYS GLY VAL ASP CYS ASP ILE ASP VAL
SEQRES 20 A 284 PRO LYS THR ILE GLN MET VAL ARG SER GLN ARG SER GLY
SEQRES 21 A 284 MET VAL GLN THR GLU ALA GLN TYR ARG PHE ILE TYR MET
SEQRES 22 A 284 ALA VAL GLN HIS TYR ILE GLU THR LEU GLN ARG
FORMUL 2 HOH *205(H2 O)
HELIX 1 1 GLU A 250 GLN A 255 5 6
HELIX 2 2 LYS A 266 ARG A 270 5 5
HELIX 3 3 ARG A 270 ASN A 277 5 8
HELIX 4 4 PHE A 285 HIS A 287 5 3
HELIX 5 5 LEU A 334 ASN A 336 5 3
HELIX 6 6 THR A 337 GLU A 348 1 12
HELIX 7 7 PRO A 432 SER A 448 1 17
HELIX 8 8 ILE A 463 GLY A 483 1 21
HELIX 9 9 ASP A 489 SER A 499 1 11
HELIX 10 10 THR A 507 LEU A 525 1 19
SHEET 1 AA 9 ARG A 289 VAL A 291 0
SHEET 2 AA 9 TYR A 304 ILE A 310 -1 N ILE A 305 O VAL A 290
SHEET 3 AA 9 TYR A 327 GLN A 331 -1 O TYR A 327 N ILE A 310
SHEET 4 AA 9 VAL A 455 CYS A 459 1 O VAL A 455 N ILE A 328
SHEET 5 AA 9 VAL A 352 MET A 355 1 O VAL A 352 N VAL A 456
SHEET 6 AA 9 ARG A 413 PHE A 420 1 O TRP A 416 N ILE A 353
SHEET 7 AA 9 TYR A 396 LYS A 405 -1 O THR A 397 N HIS A 419
SHEET 8 AA 9 MET A 383 ALA A 392 -1 O ARG A 384 N SER A 404
SHEET 9 AA 9 LEU A 377 TYR A 380 -1 O LYS A 378 N VAL A 385
SHEET 1 AB 2 VAL A 360 GLU A 361 0
SHEET 2 AB 2 LYS A 364 SER A 365 -1 O LYS A 364 N GLU A 361
CRYST1 40.123 42.061 49.287 72.04 80.39 74.65 P 1 1
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 0.024923 -0.006842 -0.002414 0.00000
SCALE2 0.000000 0.024654 -0.007131 0.00000
SCALE3 0.000000 0.000000 0.021421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
