HEADER HYDROLASE 01-FEB-11 3QKP
TITLE PROTEIN TYROSINE PHOSPHATASE 1B - APO W179F MUTANT WITH OPEN WPD-LOOP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-321;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTP1B, PTPN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-19B
KEYWDS HYDROLASE, P-LOOP, WPD-LOOP, PROTEIN PHOSPHATASE, EGFR RECEPTOR,
KEYWDS 2 PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.S.BRANDAO,S.J.JOHNSON,A.C.HENGGE
REVDAT 3 13-SEP-23 3QKP 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3QKP 1 REMARK
REVDAT 1 08-AUG-12 3QKP 0
JRNL AUTH T.A.BRANDAO,S.J.JOHNSON,A.C.HENGGE
JRNL TITL THE MOLECULAR DETAILS OF WPD-LOOP MOVEMENT DIFFER IN THE
JRNL TITL 2 PROTEIN-TYROSINE PHOSPHATASES YOPH AND PTP1B.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 525 53 2012
JRNL REFN ISSN 0003-9861
JRNL PMID 22698963
JRNL DOI 10.1016/J.ABB.2012.06.002
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 29632
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1496
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.2339 - 4.5512 0.99 2751 130 0.1761 0.1865
REMARK 3 2 4.5512 - 3.6133 0.99 2648 132 0.1613 0.2064
REMARK 3 3 3.6133 - 3.1568 0.99 2579 144 0.1852 0.2294
REMARK 3 4 3.1568 - 2.8683 1.00 2610 138 0.1921 0.2401
REMARK 3 5 2.8683 - 2.6627 0.99 2564 141 0.2013 0.2619
REMARK 3 6 2.6627 - 2.5058 0.99 2548 120 0.2005 0.2709
REMARK 3 7 2.5058 - 2.3803 0.99 2558 137 0.2206 0.2235
REMARK 3 8 2.3803 - 2.2767 0.98 2511 151 0.2594 0.2630
REMARK 3 9 2.2767 - 2.1891 0.93 2381 121 0.4201 0.5289
REMARK 3 10 2.1891 - 2.1135 0.98 2536 130 0.2575 0.2915
REMARK 3 11 2.1135 - 2.0500 0.97 2450 152 0.2956 0.3534
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 54.36
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08180
REMARK 3 B22 (A**2) : 0.08180
REMARK 3 B33 (A**2) : -0.16360
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2442
REMARK 3 ANGLE : 1.104 3286
REMARK 3 CHIRALITY : 0.078 348
REMARK 3 PLANARITY : 0.004 422
REMARK 3 DIHEDRAL : 14.158 932
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:31)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5846 -12.0447 10.4011
REMARK 3 T TENSOR
REMARK 3 T11: 0.1468 T22: 0.4226
REMARK 3 T33: 0.3949 T12: 0.0492
REMARK 3 T13: -0.1159 T23: 0.0604
REMARK 3 L TENSOR
REMARK 3 L11: 0.1004 L22: 2.3828
REMARK 3 L33: 2.4095 L12: -0.3259
REMARK 3 L13: 0.1984 L23: -0.5240
REMARK 3 S TENSOR
REMARK 3 S11: -0.2213 S12: 0.1765 S13: 0.2963
REMARK 3 S21: -0.3787 S22: 0.3748 S23: 0.9488
REMARK 3 S31: -0.1369 S32: -0.8869 S33: -0.1029
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 32:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6329 -2.3319 6.5717
REMARK 3 T TENSOR
REMARK 3 T11: 0.3270 T22: 0.1068
REMARK 3 T33: 0.2544 T12: 0.0642
REMARK 3 T13: 0.0819 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.4133 L22: 0.1614
REMARK 3 L33: 0.9848 L12: 0.0610
REMARK 3 L13: 0.0595 L23: -0.3317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: 0.0566 S13: 0.0482
REMARK 3 S21: -0.3749 S22: -0.0713 S23: -0.2566
REMARK 3 S31: -0.3887 S32: -0.0315 S33: -0.0103
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 57:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9622 -3.3017 14.7417
REMARK 3 T TENSOR
REMARK 3 T11: 0.2216 T22: 0.0675
REMARK 3 T33: 0.2464 T12: -0.0128
REMARK 3 T13: -0.0221 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.4025 L22: 0.0940
REMARK 3 L33: 0.5035 L12: -0.0727
REMARK 3 L13: -0.2232 L23: -0.1007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0887 S12: 0.0639 S13: 0.3099
REMARK 3 S21: 0.0550 S22: -0.0830 S23: -0.2385
REMARK 3 S31: -0.4070 S32: 0.1450 S33: -0.0106
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 70:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3596 -16.0874 14.1392
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.1132
REMARK 3 T33: 0.1412 T12: 0.0434
REMARK 3 T13: -0.0044 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.8393 L22: 1.5987
REMARK 3 L33: 0.5627 L12: -0.2586
REMARK 3 L13: -0.5642 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: 0.0472 S13: 0.1541
REMARK 3 S21: 0.0138 S22: -0.0329 S23: -0.2024
REMARK 3 S31: -0.0014 S32: -0.0083 S33: -0.0032
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 128:147)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4449 -23.5993 15.0790
REMARK 3 T TENSOR
REMARK 3 T11: 0.1669 T22: 0.1826
REMARK 3 T33: 0.3219 T12: 0.0913
REMARK 3 T13: 0.0147 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 1.3442 L22: 1.7596
REMARK 3 L33: 1.1231 L12: -1.1197
REMARK 3 L13: -0.5529 L23: -0.3055
REMARK 3 S TENSOR
REMARK 3 S11: 0.1174 S12: -0.1243 S13: 0.3175
REMARK 3 S21: -0.1186 S22: -0.3296 S23: -0.0857
REMARK 3 S31: 0.1359 S32: 0.3562 S33: 0.1316
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 148:176)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3316 -24.9819 19.9030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2081 T22: 0.1131
REMARK 3 T33: 0.2118 T12: 0.0892
REMARK 3 T13: -0.0230 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.9638 L22: 0.5034
REMARK 3 L33: 0.8163 L12: 0.3425
REMARK 3 L13: 0.0239 L23: -0.0874
REMARK 3 S TENSOR
REMARK 3 S11: -0.1134 S12: -0.0723 S13: -0.4555
REMARK 3 S21: 0.0768 S22: 0.2070 S23: -0.3421
REMARK 3 S31: 0.1369 S32: 0.0289 S33: -0.1136
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 177:186)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7392 -26.6446 4.9073
REMARK 3 T TENSOR
REMARK 3 T11: 0.3100 T22: 0.5194
REMARK 3 T33: 0.3832 T12: -0.0181
REMARK 3 T13: 0.1343 T23: 0.0723
REMARK 3 L TENSOR
REMARK 3 L11: 5.7272 L22: 3.8412
REMARK 3 L33: 6.3682 L12: -1.6021
REMARK 3 L13: -2.3155 L23: -1.2920
REMARK 3 S TENSOR
REMARK 3 S11: 0.1356 S12: 1.4979 S13: 1.3629
REMARK 3 S21: 0.1499 S22: -0.3997 S23: -0.2730
REMARK 3 S31: 0.2681 S32: -0.9146 S33: 0.2153
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 187:198)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3754 -27.7287 18.6201
REMARK 3 T TENSOR
REMARK 3 T11: 0.3176 T22: 0.0704
REMARK 3 T33: 0.1634 T12: 0.0217
REMARK 3 T13: 0.0466 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.9843 L22: 2.1171
REMARK 3 L33: 3.4305 L12: 0.9333
REMARK 3 L13: -0.6925 L23: 0.9408
REMARK 3 S TENSOR
REMARK 3 S11: -0.2025 S12: -0.1972 S13: 0.0498
REMARK 3 S21: 0.2514 S22: -0.0481 S23: 0.4992
REMARK 3 S31: 0.6876 S32: 0.1274 S33: 0.2402
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 199:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3567 -17.7466 20.2070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1932 T22: 0.1264
REMARK 3 T33: 0.1360 T12: 0.0360
REMARK 3 T13: 0.0059 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.8611 L22: 1.0775
REMARK 3 L33: 0.6123 L12: -0.3083
REMARK 3 L13: -0.5983 L23: -0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: -0.0757 S13: 0.1279
REMARK 3 S21: -0.0833 S22: 0.0215 S23: 0.0583
REMARK 3 S31: 0.1815 S32: 0.0805 S33: -0.0334
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 235:291)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8569 -18.3298 19.2554
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.1019
REMARK 3 T33: 0.0952 T12: -0.0057
REMARK 3 T13: 0.0072 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 3.0001 L22: 0.5326
REMARK 3 L33: 2.3076 L12: 0.4277
REMARK 3 L13: -0.7421 L23: 0.2142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.0067 S13: -0.0192
REMARK 3 S21: 0.1057 S22: -0.0978 S23: 0.0133
REMARK 3 S31: 0.1296 S32: -0.3587 S33: 0.1023
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QKP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063766.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC BLUE OPTICS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29808
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.64900
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
REMARK 200 STARTING MODEL: PDB ENTRY 2CM2 WITH THE ACTIVE SITE WATER
REMARK 200 MOLECULES REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL OF PROTEIN SOLUTION (12 MG/ML
REMARK 280 PTP1B W179F IN 10 MM TRIS PH 7.5, 25 MM NACL, 0.2 MM EDTA AND 3
REMARK 280 MM DTT), 0.5 UL SUCROSE 30 % (W/V) AND 3 UL OF PRECIPITANT
REMARK 280 SOLUTION (0.1 M HEPES PH 7.5, 0.2 M MAGNESIUM ACETATE AND 15-20 %
REMARK 280 POLYETHYLENE GLYCOL 8000). THE WELL SOLUTION WAS 500 UL OF
REMARK 280 PRECIPITANT SOLUTION., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 34.84500
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 69.69000
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 69.69000
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 34.84500
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 LYS A 292
REMARK 465 GLU A 293
REMARK 465 LEU A 294
REMARK 465 SER A 295
REMARK 465 HIS A 296
REMARK 465 GLU A 297
REMARK 465 ASP A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 PRO A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
REMARK 465 GLU A 304
REMARK 465 HIS A 305
REMARK 465 ILE A 306
REMARK 465 PRO A 307
REMARK 465 PRO A 308
REMARK 465 PRO A 309
REMARK 465 PRO A 310
REMARK 465 ARG A 311
REMARK 465 PRO A 312
REMARK 465 PRO A 313
REMARK 465 LYS A 314
REMARK 465 ARG A 315
REMARK 465 ILE A 316
REMARK 465 LEU A 317
REMARK 465 GLU A 318
REMARK 465 PRO A 319
REMARK 465 HIS A 320
REMARK 465 ASN A 321
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 HIS A 60 39.65 -92.77
REMARK 500 ASP A 63 -77.26 -63.31
REMARK 500 CYS A 215 -133.97 -128.15
REMARK 500 ILE A 219 -32.07 -137.06
REMARK 500 ASP A 240 78.02 -154.08
REMARK 500 ILE A 261 105.49 77.05
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 TRS A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 324
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CM2 RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B APO FORM
REMARK 900 RELATED ID: 3F99 RELATED DB: PDB
REMARK 900 W354F YERSINIA ENTEROCOLITICA PTPASE APO FORM
REMARK 900 RELATED ID: 3QKN RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B - F182Q MUTANT BOUND WITH HEPES
REMARK 900 RELATED ID: 3QKO RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B - APO R221K MUTANT WITH CLOSED WPD-
REMARK 900 LOOP
REMARK 900 RELATED ID: 3QKQ RELATED DB: PDB
REMARK 900 PROTEIN TYROSINE PHOSPHATASE 1B - W179F MUTANT BOUND WITH VANADATE
DBREF 3QKP A 1 321 UNP P18031 PTN1_HUMAN 1 321
SEQADV 3QKP PHE A 179 UNP P18031 TRP 179 ENGINEERED MUTATION
SEQRES 1 A 321 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 A 321 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 A 321 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 A 321 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 A 321 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 A 321 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 A 321 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 A 321 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 A 321 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 A 321 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 A 321 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 A 321 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 A 321 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 A 321 GLU ILE LEU HIS PHE HIS TYR THR THR PHE PRO ASP PHE
SEQRES 15 A 321 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 A 321 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 A 321 GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG
SEQRES 18 A 321 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 A 321 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 A 321 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 A 321 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 A 321 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 A 321 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP LEU
SEQRES 24 A 321 GLU PRO PRO PRO GLU HIS ILE PRO PRO PRO PRO ARG PRO
SEQRES 25 A 321 PRO LYS ARG ILE LEU GLU PRO HIS ASN
HET TRS A 322 8
HET GOL A 323 6
HET GOL A 324 6
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 TRS C4 H12 N O3 1+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *239(H2 O)
HELIX 1 1 MET A 1 SER A 13 1 13
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 CYS A 32 LEU A 37 1 6
HELIX 4 4 PRO A 38 ASN A 44 5 7
HELIX 5 5 PHE A 52 HIS A 54 5 3
HELIX 6 6 THR A 91 GLN A 102 1 12
HELIX 7 7 PRO A 188 SER A 201 1 14
HELIX 8 8 GLY A 220 LYS A 239 1 20
HELIX 9 9 ASP A 245 ARG A 254 1 10
HELIX 10 10 THR A 263 MET A 282 1 20
HELIX 11 11 SER A 286 TRP A 291 1 6
SHEET 1 A 9 ARG A 56 LYS A 58 0
SHEET 2 A 9 TYR A 66 MET A 74 -1 O ALA A 69 N ILE A 57
SHEET 3 A 9 ARG A 79 THR A 84 -1 O TYR A 81 N ILE A 72
SHEET 4 A 9 VAL A 211 HIS A 214 1 O VAL A 213 N ILE A 82
SHEET 5 A 9 GLY A 106 MET A 109 1 N VAL A 108 O VAL A 212
SHEET 6 A 9 THR A 168 TYR A 176 1 O PHE A 174 N VAL A 107
SHEET 7 A 9 TYR A 153 ASN A 162 -1 N THR A 154 O HIS A 175
SHEET 8 A 9 LEU A 140 ILE A 149 -1 N ASP A 148 O VAL A 155
SHEET 9 A 9 MET A 133 PHE A 135 -1 N MET A 133 O LEU A 142
SHEET 1 B 2 MET A 114 GLU A 115 0
SHEET 2 B 2 SER A 118 LEU A 119 -1 O SER A 118 N GLU A 115
SITE 1 AC1 5 HIS A 54 GLU A 129 GLU A 130 HOH A 441
SITE 2 AC1 5 HOH A 538
SITE 1 AC2 3 PRO A 89 HOH A 389 HOH A 396
SITE 1 AC3 4 SER A 146 VAL A 155 GLN A 157 HOH A 559
CRYST1 88.282 88.282 104.535 90.00 90.00 120.00 P 31 2 1 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 0.011327 0.006540 0.000000 0.00000
SCALE2 0.000000 0.013080 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009566 0.00000
(ATOM LINES ARE NOT SHOWN.)
END