HEADER TYROSINE PHOSPHATASE 01-DEC-97 2SHP
TITLE TYROSINE PHOSPHATASE SHP-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHP-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SYP, SHPTP-2;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: 562
KEYWDS TYROSINE PHOSPHATASE, INSULIN SIGNALING, SH2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.HOF,S.PLUSKEY,S.DHE-PAGANON,M.J.ECK,S.E.SHOELSON
REVDAT 5 03-APR-24 2SHP 1 REMARK
REVDAT 4 21-FEB-24 2SHP 1 REMARK
REVDAT 3 03-NOV-21 2SHP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2SHP 1 VERSN
REVDAT 1 16-FEB-99 2SHP 0
JRNL AUTH P.HOF,S.PLUSKEY,S.DHE-PAGANON,M.J.ECK,S.E.SHOELSON
JRNL TITL CRYSTAL STRUCTURE OF THE TYROSINE PHOSPHATASE SHP-2.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 92 441 1998
JRNL REFN ISSN 0092-8674
JRNL PMID 9491886
JRNL DOI 10.1016/S0092-8674(00)80938-1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 62840
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2164
REMARK 3 BIN R VALUE (WORKING SET) : 0.2477
REMARK 3 BIN FREE R VALUE : 0.2863
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7918
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 777
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.546
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : CTAB.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : CTAB.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DATA USED AND MAPS 1SIGMA CUTOFF, R
REMARK 3 -VALUES 2SIGMA CUTOFF, 2 MOLECULES IN THE ASYMMETRIC UNIT
REMARK 4
REMARK 4 2SHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178627.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 71634
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06170
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT, NCS
REMARK 200 AVERAGING
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PTP1B AND N-TERMINAL SH2 DOMAINS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 107.25000
REMARK 290 SMTRY3 2 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 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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 MET A 1
REMARK 465 ASP A 156
REMARK 465 LYS A 157
REMARK 465 GLY A 158
REMARK 465 GLU A 159
REMARK 465 SER A 160
REMARK 465 LEU A 236
REMARK 465 ALA A 237
REMARK 465 GLU A 238
REMARK 465 THR A 239
REMARK 465 THR A 240
REMARK 465 ASP A 241
REMARK 465 LYS A 242
REMARK 465 VAL A 243
REMARK 465 LYS A 244
REMARK 465 GLN A 245
REMARK 465 GLY A 295
REMARK 465 ASP A 296
REMARK 465 PRO A 297
REMARK 465 ASN A 298
REMARK 465 GLU A 299
REMARK 465 PRO A 300
REMARK 465 VAL A 301
REMARK 465 GLU A 313
REMARK 465 PHE A 314
REMARK 465 GLU A 315
REMARK 465 THR A 316
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 MET B 1
REMARK 465 ASP B 156
REMARK 465 LYS B 157
REMARK 465 GLY B 158
REMARK 465 GLU B 159
REMARK 465 SER B 160
REMARK 465 LEU B 236
REMARK 465 ALA B 237
REMARK 465 GLU B 238
REMARK 465 THR B 239
REMARK 465 THR B 240
REMARK 465 ASP B 241
REMARK 465 LYS B 242
REMARK 465 VAL B 243
REMARK 465 LYS B 244
REMARK 465 GLN B 245
REMARK 465 GLY B 295
REMARK 465 ASP B 296
REMARK 465 PRO B 297
REMARK 465 ASN B 298
REMARK 465 GLU B 299
REMARK 465 PRO B 300
REMARK 465 VAL B 301
REMARK 465 GLU B 313
REMARK 465 PHE B 314
REMARK 465 GLU B 315
REMARK 465 THR B 316
REMARK 465 LYS B 317
REMARK 465 CYS B 318
REMARK 465 ASN B 319
REMARK 465 ASN B 320
REMARK 465 SER B 321
REMARK 465 LYS B 322
REMARK 465 PRO B 323
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 235 CG CD CE NZ
REMARK 470 ASP A 294 CG OD1 OD2
REMARK 470 LYS B 235 CG CD CE NZ
REMARK 470 ASP B 294 CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER B 513 OG
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 HH22 ARG A 399 HD1 HIS A 419 1.09
REMARK 500 HH22 ARG B 399 HD1 HIS B 419 1.09
REMARK 500 HZ2 LYS A 325 HD1 HIS A 443 1.16
REMARK 500 HZ2 LYS B 325 HD1 HIS B 443 1.16
REMARK 500 HZ1 LYS A 276 H2 HOH A 3243 1.22
REMARK 500 HH22 ARG B 4 H1 HOH B 3405 1.25
REMARK 500 HZ1 LYS A 358 H1 HOH A 3118 1.26
REMARK 500 HH21 ARG A 480 H2 HOH A 3712 1.33
REMARK 500 HH21 ARG B 47 H2 HOH B 3618 1.34
REMARK 500 HE21 GLN A 271 HZ1 LYS A 274 1.34
REMARK 500 H2 HOH B 3694 O HOH B 3720 1.50
REMARK 500 O HOH A 3138 H2 HOH A 3641 1.55
REMARK 500 O HOH A 3423 H1 HOH A 3672 1.57
REMARK 500 H1 HOH B 3040 O HOH B 3195 1.57
REMARK 500 H2 HOH B 3476 O HOH B 3587 1.58
REMARK 500 H2 HOH B 3095 O HOH B 3556 1.58
REMARK 500 H2 HOH A 3272 O HOH A 3402 1.59
REMARK 500 H1 HOH B 3337 O HOH B 3379 1.59
REMARK 500 H1 HOH B 3478 O HOH B 3721 1.59
REMARK 500 H1 HOH A 3069 O HOH A 3369 1.60
REMARK 500 H2 HOH B 3191 O HOH B 3585 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 3261 H1 HOH B 3595 2646 1.54
REMARK 500 O HOH A 3464 H2 HOH B 3407 1556 1.59
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 333 CB CYS A 333 SG -0.099
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 ARG A 4 4.60 53.95
REMARK 500 ASN A 37 134.87 171.38
REMARK 500 GLU A 90 -109.18 -87.73
REMARK 500 ASN A 92 118.94 58.40
REMARK 500 ASP A 94 95.42 -41.99
REMARK 500 HIS A 116 37.89 35.05
REMARK 500 SER A 142 -96.71 -55.86
REMARK 500 LYS A 164 -75.67 -15.92
REMARK 500 SER A 165 -96.95 74.00
REMARK 500 THR A 205 86.92 -58.20
REMARK 500 LEU A 206 -18.23 156.71
REMARK 500 LYS A 369 108.64 -56.36
REMARK 500 TYR A 375 -9.70 82.27
REMARK 500 CYS A 459 -127.55 -133.16
REMARK 500 SER A 460 -74.69 -85.23
REMARK 500 ILE A 463 -32.65 -131.82
REMARK 500 VAL A 505 113.18 68.49
REMARK 500 ARG B 4 4.45 53.77
REMARK 500 ASN B 37 134.91 171.37
REMARK 500 GLU B 90 -109.60 -89.41
REMARK 500 ASN B 92 120.49 58.73
REMARK 500 ASP B 94 96.61 -38.35
REMARK 500 HIS B 116 38.08 34.94
REMARK 500 SER B 142 -95.12 -55.95
REMARK 500 LYS B 164 -75.78 -16.23
REMARK 500 SER B 165 -96.29 74.63
REMARK 500 THR B 205 86.59 -57.51
REMARK 500 LEU B 206 -19.39 155.92
REMARK 500 LYS B 369 108.18 -56.44
REMARK 500 TYR B 375 -9.20 82.90
REMARK 500 CYS B 459 -130.92 -132.70
REMARK 500 SER B 460 -73.47 -82.92
REMARK 500 ILE B 463 -32.59 -132.63
REMARK 500 VAL B 505 115.84 67.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 62 0.08 SIDE CHAIN
REMARK 500 ARG A 289 0.09 SIDE CHAIN
REMARK 500 ARG A 351 0.11 SIDE CHAIN
REMARK 500 ARG A 399 0.11 SIDE CHAIN
REMARK 500 ARG A 465 0.07 SIDE CHAIN
REMARK 500 ARG A 498 0.08 SIDE CHAIN
REMARK 500 TYR B 62 0.08 SIDE CHAIN
REMARK 500 ARG B 289 0.09 SIDE CHAIN
REMARK 500 ARG B 351 0.10 SIDE CHAIN
REMARK 500 ARG B 399 0.11 SIDE CHAIN
REMARK 500 ARG B 498 0.07 SIDE CHAIN
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 CAT A 1800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAT B 2800
DBREF 2SHP A 1 525 UNP Q06124 PTN11_HUMAN 1 525
DBREF 2SHP B 1 525 UNP Q06124 PTN11_HUMAN 1 525
SEQADV 2SHP LYS A 2 UNP Q06124 THR 2 ENGINEERED MUTATION
SEQADV 2SHP LEU A 41 UNP Q06124 PHE 41 ENGINEERED MUTATION
SEQADV 2SHP SER A 513 UNP Q06124 PHE 513 ENGINEERED MUTATION
SEQADV 2SHP LYS B 2 UNP Q06124 THR 2 ENGINEERED MUTATION
SEQADV 2SHP LEU B 41 UNP Q06124 PHE 41 ENGINEERED MUTATION
SEQADV 2SHP SER B 513 UNP Q06124 PHE 513 ENGINEERED MUTATION
SEQRES 1 A 525 MET LYS SER ARG ARG TRP PHE HIS PRO ASN ILE THR GLY
SEQRES 2 A 525 VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP
SEQRES 3 A 525 GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY
SEQRES 4 A 525 ASP LEU THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR
SEQRES 5 A 525 HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU
SEQRES 6 A 525 TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL
SEQRES 7 A 525 GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS
SEQRES 8 A 525 ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN CYS
SEQRES 9 A 525 ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS LEU
SEQRES 10 A 525 SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS GLY
SEQRES 11 A 525 LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER HIS
SEQRES 12 A 525 PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP ASP
SEQRES 13 A 525 LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR HIS
SEQRES 14 A 525 VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL GLY
SEQRES 15 A 525 GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL GLU
SEQRES 16 A 525 HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY THR
SEQRES 17 A 525 VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG ILE
SEQRES 18 A 525 ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU SER
SEQRES 19 A 525 LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY PHE
SEQRES 20 A 525 TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS LYS
SEQRES 21 A 525 LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU ASN
SEQRES 22 A 525 LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP
SEQRES 23 A 525 HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN GLU
SEQRES 24 A 525 PRO VAL SER ASP TYR ILE ASN ALA ASN ILE ILE MET PRO
SEQRES 25 A 525 GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS LYS
SEQRES 26 A 525 SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR VAL
SEQRES 27 A 525 ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER ARG
SEQRES 28 A 525 VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY LYS
SEQRES 29 A 525 SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA LEU
SEQRES 30 A 525 LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS GLU
SEQRES 31 A 525 SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS LEU
SEQRES 32 A 525 SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL TRP
SEQRES 33 A 525 GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL PRO
SEQRES 34 A 525 SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU VAL
SEQRES 35 A 525 HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO VAL
SEQRES 36 A 525 VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR
SEQRES 37 A 525 PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG GLU
SEQRES 38 A 525 LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR ILE
SEQRES 39 A 525 GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN THR
SEQRES 40 A 525 GLU ALA GLN TYR ARG SER ILE TYR MET ALA VAL GLN HIS
SEQRES 41 A 525 TYR ILE GLU THR LEU
SEQRES 1 B 525 MET LYS SER ARG ARG TRP PHE HIS PRO ASN ILE THR GLY
SEQRES 2 B 525 VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP
SEQRES 3 B 525 GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY
SEQRES 4 B 525 ASP LEU THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR
SEQRES 5 B 525 HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU
SEQRES 6 B 525 TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL
SEQRES 7 B 525 GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS
SEQRES 8 B 525 ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN CYS
SEQRES 9 B 525 ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS LEU
SEQRES 10 B 525 SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS GLY
SEQRES 11 B 525 LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER HIS
SEQRES 12 B 525 PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP ASP
SEQRES 13 B 525 LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR HIS
SEQRES 14 B 525 VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL GLY
SEQRES 15 B 525 GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL GLU
SEQRES 16 B 525 HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY THR
SEQRES 17 B 525 VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG ILE
SEQRES 18 B 525 ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU SER
SEQRES 19 B 525 LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY PHE
SEQRES 20 B 525 TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS LYS
SEQRES 21 B 525 LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU ASN
SEQRES 22 B 525 LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP
SEQRES 23 B 525 HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN GLU
SEQRES 24 B 525 PRO VAL SER ASP TYR ILE ASN ALA ASN ILE ILE MET PRO
SEQRES 25 B 525 GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS LYS
SEQRES 26 B 525 SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR VAL
SEQRES 27 B 525 ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER ARG
SEQRES 28 B 525 VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY LYS
SEQRES 29 B 525 SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA LEU
SEQRES 30 B 525 LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS GLU
SEQRES 31 B 525 SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS LEU
SEQRES 32 B 525 SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL TRP
SEQRES 33 B 525 GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL PRO
SEQRES 34 B 525 SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU VAL
SEQRES 35 B 525 HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO VAL
SEQRES 36 B 525 VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR
SEQRES 37 B 525 PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG GLU
SEQRES 38 B 525 LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR ILE
SEQRES 39 B 525 GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN THR
SEQRES 40 B 525 GLU ALA GLN TYR ARG SER ILE TYR MET ALA VAL GLN HIS
SEQRES 41 B 525 TYR ILE GLU THR LEU
HET CAT A1800 16
HET CAT B2800 16
HETNAM CAT DODECANE-TRIMETHYLAMINE
FORMUL 3 CAT 2(C15 H34 N 1+)
FORMUL 5 HOH *777(H2 O)
HELIX 1 1 GLY A 13 ARG A 23 1 11
HELIX 2 2 LEU A 74 GLU A 83 1 10
HELIX 3 3 GLY A 119 LYS A 129 1 11
HELIX 4 4 LEU A 190 LYS A 199 1 10
HELIX 5 5 ALA A 223 SER A 234 5 12
HELIX 6 6 PHE A 247 LEU A 261 1 15
HELIX 7 7 LYS A 266 GLN A 269 1 4
HELIX 8 8 GLN A 271 LYS A 276 5 6
HELIX 9 9 GLN A 335 GLN A 347 5 13
HELIX 10 10 PRO A 432 GLU A 447 1 16
HELIX 11 11 ARG A 465 LYS A 482 1 18
HELIX 12 12 VAL A 490 ARG A 498 1 9
HELIX 13 13 GLU A 508 GLU A 523 1 16
HELIX 14 14 GLY B 13 ARG B 23 1 11
HELIX 15 15 LEU B 74 GLU B 83 1 10
HELIX 16 16 GLY B 119 LYS B 129 1 11
HELIX 17 17 LEU B 190 LYS B 199 1 10
HELIX 18 18 ALA B 223 SER B 234 5 12
HELIX 19 19 PHE B 247 LEU B 261 1 15
HELIX 20 20 LYS B 266 GLN B 269 1 4
HELIX 21 21 GLN B 271 LYS B 276 5 6
HELIX 22 22 VAL B 338 GLU B 348 1 11
HELIX 23 23 PRO B 432 GLU B 447 1 16
HELIX 24 24 ARG B 465 LYS B 482 1 18
HELIX 25 25 VAL B 490 ARG B 498 1 9
HELIX 26 26 GLU B 508 GLU B 523 1 16
SHEET 1 A 3 PHE A 29 PRO A 33 0
SHEET 2 A 3 ASP A 40 ARG A 47 -1 N SER A 44 O LEU A 30
SHEET 3 A 3 ALA A 50 GLN A 57 -1 N ILE A 56 O LEU A 41
SHEET 1 B 3 PHE A 135 GLU A 139 0
SHEET 2 B 3 PHE A 147 THR A 153 -1 N SER A 150 O LEU A 136
SHEET 3 B 3 LYS A 166 ILE A 172 -1 N ILE A 172 O PHE A 147
SHEET 1 C 2 ARG A 173 GLN A 175 0
SHEET 2 C 2 LYS A 178 ASP A 180 -1 N ASP A 180 O ARG A 173
SHEET 1 D 8 ALA A 307 MET A 311 0
SHEET 2 D 8 SER A 326 THR A 330 -1 N ALA A 329 O ASN A 308
SHEET 3 D 8 VAL A 455 HIS A 458 1 N VAL A 455 O ILE A 328
SHEET 4 D 8 VAL A 352 MET A 355 1 N VAL A 354 O VAL A 456
SHEET 5 D 8 ARG A 413 PHE A 420 1 N TRP A 416 O ILE A 353
SHEET 6 D 8 TYR A 396 LYS A 405 -1 N LEU A 403 O ARG A 413
SHEET 7 D 8 MET A 383 ALA A 392 -1 N SER A 391 O LEU A 398
SHEET 8 D 8 LEU A 377 TYR A 380 -1 N TYR A 380 O MET A 383
SHEET 1 E 3 PHE B 29 PRO B 33 0
SHEET 2 E 3 ASP B 40 ARG B 47 -1 N SER B 44 O LEU B 30
SHEET 3 E 3 ALA B 50 GLN B 57 -1 N ILE B 56 O LEU B 41
SHEET 1 F 3 PHE B 135 GLU B 139 0
SHEET 2 F 3 PHE B 147 THR B 153 -1 N SER B 150 O LEU B 136
SHEET 3 F 3 LYS B 166 ILE B 172 -1 N ILE B 172 O PHE B 147
SHEET 1 G 2 ARG B 173 GLN B 175 0
SHEET 2 G 2 LYS B 178 ASP B 180 -1 N ASP B 180 O ARG B 173
SHEET 1 H 8 ALA B 307 ILE B 310 0
SHEET 2 H 8 TYR B 327 THR B 330 -1 N ALA B 329 O ASN B 308
SHEET 3 H 8 VAL B 455 HIS B 458 1 N VAL B 455 O ILE B 328
SHEET 4 H 8 VAL B 352 MET B 355 1 N VAL B 354 O VAL B 456
SHEET 5 H 8 ARG B 413 PHE B 420 1 N TRP B 416 O ILE B 353
SHEET 6 H 8 TYR B 396 LYS B 405 -1 N LEU B 403 O ARG B 413
SHEET 7 H 8 MET B 383 ALA B 392 -1 N SER B 391 O LEU B 398
SHEET 8 H 8 LEU B 377 TYR B 380 -1 N TYR B 380 O MET B 383
SITE 1 AC1 9 THR A 356 PHE A 420 TRP A 423 PRO A 429
SITE 2 AC1 9 VAL A 435 PHE A 438 PHE A 469 ILE A 472
SITE 3 AC1 9 SER A 513
SITE 1 AC2 12 THR B 356 PHE B 420 TRP B 423 PRO B 429
SITE 2 AC2 12 SER B 430 PRO B 432 VAL B 435 PHE B 438
SITE 3 AC2 12 PHE B 469 ILE B 472 SER B 513 MET B 516
CRYST1 45.900 214.500 55.700 90.00 96.30 90.00 P 1 21 1 4
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 0.021786 0.000000 0.002405 0.00000
SCALE2 0.000000 0.004662 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018062 0.00000
MTRIX1 1 -0.965419 -0.014739 -0.260285 48.63360 1
MTRIX2 1 0.010936 -0.999811 0.016053 -24.79685 1
MTRIX3 1 -0.260473 0.012651 0.965398 -15.83565 1
(ATOM LINES ARE NOT SHOWN.)
END
