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PDBsum entry 2ikq

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Top Page protein ligands Protein-protein interface(s) links
Signaling protein, immune system PDB id
2ikq
Jmol
Contents
Protein chains
262 a.a.
Ligands
PO4 ×3
Waters ×10
HEADER    SIGNALING PROTEIN, IMMUNE SYSTEM        02-OCT-06   2IKQ
TITLE     CRYSTAL STRUCTURE OF MOUSE STS-1 PGM DOMAIN IN COMPLEX WITH PHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SUPPRESSOR OF T-CELL RECEPTOR SIGNALING 1;
COMPND   3 CHAIN: A, B, M;
COMPND   4 FRAGMENT: PHOSPHOGLYCERATE MUTASE HOMOLOGY DOMAIN, RESIDUES 373-633;
COMPND   5 SYNONYM: STS-1; CBL-INTERACTING PROTEIN P70;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: STS-1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: CODONPLUS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX-2HB
KEYWDS    PGM; ACID PHOSPHATASE; PHOSPHO-HISTIDINE ENZYME, SIGNALING PROTEIN,
KEYWDS   2 IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.CHEN,N.NASSAR
REVDAT   3   13-JUL-11 2IKQ    1       VERSN
REVDAT   2   24-FEB-09 2IKQ    1       VERSN
REVDAT   1   14-AUG-07 2IKQ    0
JRNL        AUTH   A.MIKHAILIK,B.FORD,J.KELLER,Y.CHEN,N.NASSAR,N.CARPINO
JRNL        TITL   A PHOSPHATASE ACTIVITY OF STS-1 CONTRIBUTES TO THE
JRNL        TITL 2 SUPPRESSION OF TCR SIGNALING
JRNL        REF    MOL.CELL                      V.  27   486 2007
JRNL        REFN                   ISSN 1097-2765
JRNL        PMID   17679096
JRNL        DOI    10.1016/J.MOLCEL.2007.06.015
REMARK   2
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2
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) : 2.61
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6
REMARK   3   NUMBER OF REFLECTIONS             : 24371
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) : 0.249
REMARK   3   R VALUE            (WORKING SET) : 0.248
REMARK   3   FREE R VALUE                     : 0.275
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1293
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) : 2.61
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1768
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3710
REMARK   3   BIN FREE R VALUE SET COUNT          : 90
REMARK   3   BIN FREE R VALUE                    : 0.3810
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6103
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 10
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 74.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 68.36
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -4.21000
REMARK   3    B22 (A**2) : 8.82000
REMARK   3    B33 (A**2) : -5.15000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.42000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.369
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.335
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.002
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6269 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8518 ; 1.420 ; 1.956
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   773 ; 6.359 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   273 ;37.681 ;23.663
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1051 ;19.431 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;20.943 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   939 ; 0.095 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4743 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2739 ; 0.244 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4281 ; 0.315 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   220 ; 0.157 ; 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):   130 ; 0.367 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.430 ; 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):  3962 ; 0.707 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6282 ; 1.294 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2626 ; 1.494 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2236 ; 2.312 ; 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 : 3
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B M
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A    373       A     490      1
REMARK   3           1     B    373       B     490      1
REMARK   3           1     M    373       M     490      1
REMARK   3           2     A    499       A     603      1
REMARK   3           2     B    499       B     603      1
REMARK   3           2     M    499       M     603      1
REMARK   3           3     A    611       A     626      1
REMARK   3           3     B    611       B     626      1
REMARK   3           3     M    611       M     626      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3627 ;  0.06 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3627 ;  0.07 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    M    (A):   3627 ;  0.05 ;  0.05
REMARK   3   TIGHT THERMAL      1    A (A**2):   3627 ;  0.12 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   3627 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      1    M (A**2):   3627 ;  0.07 ;  0.50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : A M
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A    604       A     610      1
REMARK   3           1     M    604       M     610      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    A    (A):     87 ;  0.02 ;  0.05
REMARK   3   TIGHT THERMAL      2    A (A**2):     87 ;  0.06 ;  0.50
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
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    604       A     610      6
REMARK   3           1     B    604       B     610      6
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   3    A    (A):     87 ;  0.37 ;  5.00
REMARK   3   LOOSE THERMAL      3    A (A**2):     87 ;  3.62 ; 10.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 2IKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB039692.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X26C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25668
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.609
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : 0.63000
REMARK 200  R SYM                      (I) : 0.63000
REMARK 200   FOR THE DATA SET  : 30.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.61
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.55600
REMARK 200  R SYM FOR SHELL            (I) : 0.55600
REMARK 200   FOR SHELL         : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1H0Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.1 M HEPES, 0.3 M NA
REMARK 280  ACETATE, 0.2 M NA/K PHOSPHATE, PH 7.0, VAPOR DIFFUSION,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       58.48000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.33550
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.48000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.33550
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: SUBUNITS A AND B FORM A DIMER.
REMARK 300 SUBUNIT C DIMERIZES WITH ITS SYMMETRY GENERATED BY THE 2-FOLD AXIS:
REMARK 300 -X, Y, -Z
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       18.96043
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -99.48838
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     GLY A   369
REMARK 465     PRO A   370
REMARK 465     GLN A   371
REMARK 465     THR A   634
REMARK 465     LEU A   635
REMARK 465     LEU A   636
REMARK 465     GLN A   637
REMARK 465     GLU A   638
REMARK 465     GLY B   369
REMARK 465     PRO B   370
REMARK 465     GLN B   371
REMARK 465     GLY B   628
REMARK 465     PHE B   629
REMARK 465     ASN B   630
REMARK 465     TRP B   631
REMARK 465     ARG B   632
REMARK 465     GLU B   633
REMARK 465     THR B   634
REMARK 465     LEU B   635
REMARK 465     LEU B   636
REMARK 465     GLN B   637
REMARK 465     GLU B   638
REMARK 465     GLY M   369
REMARK 465     PRO M   370
REMARK 465     GLN M   371
REMARK 465     LYS M   372
REMARK 465     TRP M   631
REMARK 465     ARG M   632
REMARK 465     GLU M   633
REMARK 465     THR M   634
REMARK 465     LEU M   635
REMARK 465     LEU M   636
REMARK 465     GLN M   637
REMARK 465     GLU M   638
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     GLU A 633    CG   CD   OE1  OE2
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    GLY B   578     OH   TYR M   391     1565     1.90
REMARK 500   ND2  ASN A   540     CE1  PHE A   629     4545     1.96
REMARK 500   OH   TYR B   391     ND2  ASN M   540     3555     2.05
REMARK 500   OG   SER B   498     O    GLY M   609     3555     2.15
REMARK 500   OG   SER B   532     NZ   LYS M   554     3555     2.16
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    ASP A 427       78.18   -155.33
REMARK 500    ALA A 511      -24.35    -38.58
REMARK 500    ASN A 558      -95.37    -75.36
REMARK 500    ALA A 564     -121.81   -145.15
REMARK 500    SER A 584       -0.80    -59.45
REMARK 500    LEU A 597       19.88     50.99
REMARK 500    ASP B 427       76.85   -155.54
REMARK 500    ALA B 511      -23.88    -39.48
REMARK 500    ASN B 558      -94.84    -75.14
REMARK 500    ALA B 564     -121.01   -146.92
REMARK 500    SER B 584       -0.86    -59.56
REMARK 500    LEU B 597       19.71     50.17
REMARK 500    ASP M 427       76.79   -155.84
REMARK 500    ALA M 511      -24.00    -39.83
REMARK 500    ASN M 558      -95.81    -76.17
REMARK 500    ALA M 564     -122.37   -146.28
REMARK 500    SER M 584       -0.11    -59.69
REMARK 500    LEU M 597       19.12     51.30
REMARK 500    PHE M 629      -69.29   -143.68
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 PO4 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 M 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H0Q   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE APO-STS-1 PGM DOMAIN
DBREF  2IKQ A  369   638  UNP    Q8BGG7   STS1_MOUSE     369    638
DBREF  2IKQ B  369   638  UNP    Q8BGG7   STS1_MOUSE     369    638
DBREF  2IKQ M  369   638  UNP    Q8BGG7   STS1_MOUSE     369    638
SEQRES   1 A  270  GLY PRO GLN LYS ARG CYS LEU PHE VAL CYS ARG HIS GLY
SEQRES   2 A  270  GLU ARG MET ASP VAL VAL PHE GLY LYS TYR TRP LEU SER
SEQRES   3 A  270  GLN CYS PHE ASP ALA LYS GLY ARG TYR ILE ARG THR ASN
SEQRES   4 A  270  LEU ASN MET PRO HIS SER LEU PRO GLN ARG SER GLY GLY
SEQRES   5 A  270  PHE ARG ASP TYR GLU LYS ASP ALA PRO ILE THR VAL PHE
SEQRES   6 A  270  GLY CYS MET GLN ALA ARG LEU VAL GLY GLU ALA LEU LEU
SEQRES   7 A  270  GLU SER ASN THR VAL ILE ASP HIS VAL TYR CYS SER PRO
SEQRES   8 A  270  SER LEU ARG CYS VAL GLN THR ALA HIS ASN ILE LEU LYS
SEQRES   9 A  270  GLY LEU GLN GLN ASP ASN HIS LEU LYS ILE ARG VAL GLU
SEQRES  10 A  270  PRO GLY LEU PHE GLU TRP THR LYS TRP VAL ALA GLY SER
SEQRES  11 A  270  THR LEU PRO ALA TRP ILE PRO PRO SER GLU LEU ALA ALA
SEQRES  12 A  270  ALA ASN LEU SER VAL ASP THR THR TYR ARG PRO HIS ILE
SEQRES  13 A  270  PRO VAL SER LYS LEU ALA ILE SER GLU SER TYR ASP THR
SEQRES  14 A  270  TYR ILE ASN ARG SER PHE GLN VAL THR LYS GLU ILE ILE
SEQRES  15 A  270  SER GLU CYS LYS SER LYS GLY ASN ASN ILE LEU ILE VAL
SEQRES  16 A  270  ALA HIS ALA SER SER LEU GLU ALA CYS THR CYS GLN LEU
SEQRES  17 A  270  GLN GLY LEU SER PRO GLN ASN SER LYS ASP PHE VAL GLN
SEQRES  18 A  270  MET VAL ARG LYS ILE PRO TYR LEU GLY PHE CYS SER CYS
SEQRES  19 A  270  GLU GLU LEU GLY GLU THR GLY ILE TRP GLN LEU THR ASP
SEQRES  20 A  270  PRO PRO ILE LEU PRO LEU THR HIS GLY PRO THR GLY GLY
SEQRES  21 A  270  PHE ASN TRP ARG GLU THR LEU LEU GLN GLU
SEQRES   1 B  270  GLY PRO GLN LYS ARG CYS LEU PHE VAL CYS ARG HIS GLY
SEQRES   2 B  270  GLU ARG MET ASP VAL VAL PHE GLY LYS TYR TRP LEU SER
SEQRES   3 B  270  GLN CYS PHE ASP ALA LYS GLY ARG TYR ILE ARG THR ASN
SEQRES   4 B  270  LEU ASN MET PRO HIS SER LEU PRO GLN ARG SER GLY GLY
SEQRES   5 B  270  PHE ARG ASP TYR GLU LYS ASP ALA PRO ILE THR VAL PHE
SEQRES   6 B  270  GLY CYS MET GLN ALA ARG LEU VAL GLY GLU ALA LEU LEU
SEQRES   7 B  270  GLU SER ASN THR VAL ILE ASP HIS VAL TYR CYS SER PRO
SEQRES   8 B  270  SER LEU ARG CYS VAL GLN THR ALA HIS ASN ILE LEU LYS
SEQRES   9 B  270  GLY LEU GLN GLN ASP ASN HIS LEU LYS ILE ARG VAL GLU
SEQRES  10 B  270  PRO GLY LEU PHE GLU TRP THR LYS TRP VAL ALA GLY SER
SEQRES  11 B  270  THR LEU PRO ALA TRP ILE PRO PRO SER GLU LEU ALA ALA
SEQRES  12 B  270  ALA ASN LEU SER VAL ASP THR THR TYR ARG PRO HIS ILE
SEQRES  13 B  270  PRO VAL SER LYS LEU ALA ILE SER GLU SER TYR ASP THR
SEQRES  14 B  270  TYR ILE ASN ARG SER PHE GLN VAL THR LYS GLU ILE ILE
SEQRES  15 B  270  SER GLU CYS LYS SER LYS GLY ASN ASN ILE LEU ILE VAL
SEQRES  16 B  270  ALA HIS ALA SER SER LEU GLU ALA CYS THR CYS GLN LEU
SEQRES  17 B  270  GLN GLY LEU SER PRO GLN ASN SER LYS ASP PHE VAL GLN
SEQRES  18 B  270  MET VAL ARG LYS ILE PRO TYR LEU GLY PHE CYS SER CYS
SEQRES  19 B  270  GLU GLU LEU GLY GLU THR GLY ILE TRP GLN LEU THR ASP
SEQRES  20 B  270  PRO PRO ILE LEU PRO LEU THR HIS GLY PRO THR GLY GLY
SEQRES  21 B  270  PHE ASN TRP ARG GLU THR LEU LEU GLN GLU
SEQRES   1 M  270  GLY PRO GLN LYS ARG CYS LEU PHE VAL CYS ARG HIS GLY
SEQRES   2 M  270  GLU ARG MET ASP VAL VAL PHE GLY LYS TYR TRP LEU SER
SEQRES   3 M  270  GLN CYS PHE ASP ALA LYS GLY ARG TYR ILE ARG THR ASN
SEQRES   4 M  270  LEU ASN MET PRO HIS SER LEU PRO GLN ARG SER GLY GLY
SEQRES   5 M  270  PHE ARG ASP TYR GLU LYS ASP ALA PRO ILE THR VAL PHE
SEQRES   6 M  270  GLY CYS MET GLN ALA ARG LEU VAL GLY GLU ALA LEU LEU
SEQRES   7 M  270  GLU SER ASN THR VAL ILE ASP HIS VAL TYR CYS SER PRO
SEQRES   8 M  270  SER LEU ARG CYS VAL GLN THR ALA HIS ASN ILE LEU LYS
SEQRES   9 M  270  GLY LEU GLN GLN ASP ASN HIS LEU LYS ILE ARG VAL GLU
SEQRES  10 M  270  PRO GLY LEU PHE GLU TRP THR LYS TRP VAL ALA GLY SER
SEQRES  11 M  270  THR LEU PRO ALA TRP ILE PRO PRO SER GLU LEU ALA ALA
SEQRES  12 M  270  ALA ASN LEU SER VAL ASP THR THR TYR ARG PRO HIS ILE
SEQRES  13 M  270  PRO VAL SER LYS LEU ALA ILE SER GLU SER TYR ASP THR
SEQRES  14 M  270  TYR ILE ASN ARG SER PHE GLN VAL THR LYS GLU ILE ILE
SEQRES  15 M  270  SER GLU CYS LYS SER LYS GLY ASN ASN ILE LEU ILE VAL
SEQRES  16 M  270  ALA HIS ALA SER SER LEU GLU ALA CYS THR CYS GLN LEU
SEQRES  17 M  270  GLN GLY LEU SER PRO GLN ASN SER LYS ASP PHE VAL GLN
SEQRES  18 M  270  MET VAL ARG LYS ILE PRO TYR LEU GLY PHE CYS SER CYS
SEQRES  19 M  270  GLU GLU LEU GLY GLU THR GLY ILE TRP GLN LEU THR ASP
SEQRES  20 M  270  PRO PRO ILE LEU PRO LEU THR HIS GLY PRO THR GLY GLY
SEQRES  21 M  270  PHE ASN TRP ARG GLU THR LEU LEU GLN GLU
HET    PO4  A 101       5
HET    PO4  B 102       5
HET    PO4  M 103       5
HETNAM     PO4 PHOSPHATE ION
FORMUL   4  PO4    3(O4 P 3-)
FORMUL   7  HOH   *10(H2 O)
HELIX    1   1 ARG A  383  PHE A  388  1                                   6
HELIX    2   2 TYR A  391  PHE A  397  1                                   7
HELIX    3   3 GLY A  420  ASP A  427  5                                   8
HELIX    4   4 THR A  431  SER A  448  1                                  18
HELIX    5   5 SER A  460  LEU A  474  1                                  15
HELIX    6   6 PRO A  486  PHE A  489  5                                   4
HELIX    7   7 TRP A  491  VAL A  495  5                                   5
HELIX    8   8 PRO A  505  ALA A  511  1                                   7
HELIX    9   9 PRO A  525  LEU A  529  5                                   5
HELIX   10  10 SER A  534  CYS A  553  1                                  20
HELIX   11  11 HIS A  565  CYS A  574  1                                  10
HELIX   12  12 GLN A  575  GLY A  578  5                                   4
HELIX   13  13 ASN A  583  ARG A  592  1                                  10
HELIX   14  14 ARG B  383  PHE B  388  1                                   6
HELIX   15  15 TYR B  391  PHE B  397  1                                   7
HELIX   16  16 GLY B  420  ASP B  427  5                                   8
HELIX   17  17 THR B  431  SER B  448  1                                  18
HELIX   18  18 SER B  460  LEU B  474  1                                  15
HELIX   19  19 PRO B  486  PHE B  489  5                                   4
HELIX   20  20 TRP B  491  VAL B  495  5                                   5
HELIX   21  21 PRO B  505  ALA B  511  1                                   7
HELIX   22  22 PRO B  525  LEU B  529  5                                   5
HELIX   23  23 SER B  534  CYS B  553  1                                  20
HELIX   24  24 HIS B  565  CYS B  574  1                                  10
HELIX   25  25 GLN B  575  GLY B  578  5                                   4
HELIX   26  26 ASN B  583  ARG B  592  1                                  10
HELIX   27  27 ARG M  383  PHE M  388  1                                   6
HELIX   28  28 TYR M  391  PHE M  397  1                                   7
HELIX   29  29 GLY M  420  ASP M  427  5                                   8
HELIX   30  30 THR M  431  SER M  448  1                                  18
HELIX   31  31 SER M  460  LEU M  474  1                                  15
HELIX   32  32 PRO M  486  PHE M  489  5                                   4
HELIX   33  33 TRP M  491  VAL M  495  5                                   5
HELIX   34  34 PRO M  505  ALA M  511  1                                   7
HELIX   35  35 PRO M  525  LEU M  529  5                                   5
HELIX   36  36 SER M  534  CYS M  553  1                                  20
HELIX   37  37 HIS M  565  CYS M  574  1                                  10
HELIX   38  38 GLN M  575  GLY M  578  5                                   4
HELIX   39  39 ASN M  583  ARG M  592  1                                  10
SHEET    1   A 6 ARG A 483  VAL A 484  0
SHEET    2   A 6 HIS A 454  CYS A 457  1  N  VAL A 455   O  ARG A 483
SHEET    3   A 6 ILE A 560  ALA A 564  1  O  LEU A 561   N  TYR A 456
SHEET    4   A 6 CYS A 374  ARG A 379  1  N  CYS A 374   O  ILE A 560
SHEET    5   A 6 PHE A 599  LEU A 605 -1  O  CYS A 602   N  LEU A 375
SHEET    6   A 6 ILE A 610  THR A 614 -1  O  GLN A 612   N  GLU A 603
SHEET    1   B 6 ARG B 483  VAL B 484  0
SHEET    2   B 6 HIS B 454  CYS B 457  1  N  VAL B 455   O  ARG B 483
SHEET    3   B 6 ILE B 560  ALA B 564  1  O  LEU B 561   N  TYR B 456
SHEET    4   B 6 CYS B 374  ARG B 379  1  N  CYS B 374   O  ILE B 560
SHEET    5   B 6 PHE B 599  LEU B 605 -1  O  CYS B 602   N  LEU B 375
SHEET    6   B 6 ILE B 610  THR B 614 -1  O  GLN B 612   N  GLU B 603
SHEET    1   C 6 ARG M 483  VAL M 484  0
SHEET    2   C 6 HIS M 454  CYS M 457  1  N  VAL M 455   O  ARG M 483
SHEET    3   C 6 ILE M 560  ALA M 564  1  O  LEU M 561   N  TYR M 456
SHEET    4   C 6 CYS M 374  ARG M 379  1  N  CYS M 374   O  ILE M 560
SHEET    5   C 6 PHE M 599  LEU M 605 -1  O  CYS M 602   N  LEU M 375
SHEET    6   C 6 ILE M 610  THR M 614 -1  O  GLN M 612   N  GLU M 603
SITE     1 AC1  7 ARG A 379  HIS A 380  ARG A 383  ARG A 462
SITE     2 AC1  7 GLU A 490  HIS A 565  ALA A 566
SITE     1 AC2  7 ARG B 379  HIS B 380  ARG B 383  ARG B 462
SITE     2 AC2  7 GLU B 490  HIS B 565  ALA B 566
SITE     1 AC3  8 HOH M  10  ARG M 379  HIS M 380  ARG M 383
SITE     2 AC3  8 ARG M 462  GLU M 490  HIS M 565  ALA M 566
CRYST1  116.960   74.671  101.279  90.00 100.79  90.00 C 1 2 1      12
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008550  0.000000  0.001629        0.00000
SCALE2      0.000000  0.013392  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010051        0.00000
      
PROCHECK
Go to PROCHECK summary
 References