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PDBsum entry 2ixp

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Isomerase/isomerase inhibitor PDB id
2ixp
Jmol
Contents
Protein chains
310 a.a.
Ligands
SIN-ALA-ALA-PRO-
LYS-NIT
×4
SO4 ×4
Metals
_CL ×2
HEADER    ISOMERASE/ISOMERASE INHIBITOR           09-JUL-06   2IXP
TITLE     CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA1 PTPA1 IN
TITLE    2 COMPLEX WITH MODEL SUBSTRATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A ACTIVATOR 1;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: 1-317;
COMPND   5 SYNONYM: PTPA1, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PTPA-1, PPIASE
COMPND   6  PTPA-1, ROTAMASE PTPA-1, PHOSPHOTYROSYL PHOSPHATASE ACTIVATOR 1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: SIN-ALA-ALA-PRO-LYS-NIT;
COMPND  10 CHAIN: F, G, H, I;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: GOLD;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET9;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES
KEYWDS    PP2A PHOSPHATASE ACTIVATOR PROLYL ISOMERASE PTPA, PROLYL CONTAINING
KEYWDS   2 PEPTIDE SUBSTRATE ANALOG, NUCLEAR PROTEIN, ISOMERASE-ISOMERASE
KEYWDS   3 INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.LEULLIOT,G.VICENTINI,J.JORDENS,S.QUEVILLON-CHERUEL,M.SCHILTZ,
AUTHOR   2 D.BARFORD,H.VAN TILBEURGH,J.GORIS
REVDAT   4   13-JUL-11 2IXP    1       VERSN
REVDAT   3   24-FEB-09 2IXP    1       VERSN
REVDAT   2   09-AUG-06 2IXP    1       JRNL
REVDAT   1   31-JUL-06 2IXP    0
JRNL        AUTH   N.LEULLIOT,G.VICENTINI,J.JORDENS,S.QUEVILLON-CHERUEL,
JRNL        AUTH 2 M.SCHILTZ,D.BARFORD,H.VAN TILBEURGH,J.GORIS
JRNL        TITL   CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR:
JRNL        TITL 2 IMPLICATIONS FOR ITS PP2A-SPECIFIC PPIASE ACTIVITY
JRNL        REF    MOL.CELL                      V.  23   413 2006
JRNL        REFN                   ISSN 1097-2765
JRNL        PMID   16885030
JRNL        DOI    10.1016/J.MOLCEL.2006.07.008
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.12
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 40651
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) : 0.233
REMARK   3   R VALUE            (WORKING SET) : 0.229
REMARK   3   FREE R VALUE                     : 0.302
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2158
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) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2963
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190
REMARK   3   BIN FREE R VALUE SET COUNT          : 146
REMARK   3   BIN FREE R VALUE                    : 0.4130
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 10372
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 22
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : UNVERIFIED
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 2.49
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.01000
REMARK   3    B22 (A**2) : 3.01000
REMARK   3    B33 (A**2) : -4.51000
REMARK   3    B12 (A**2) : 1.50000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.435
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.362
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.408
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10720 ; 0.026 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14564 ; 2.466 ; 1.953
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1258 ; 9.045 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   486 ;40.375 ;23.210
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1726 ;23.401 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    52 ;23.245 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1558 ; 0.174 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8176 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5792 ; 0.290 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7237 ; 0.343 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   426 ; 0.196 ; 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):    44 ; 0.292 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.290 ; 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):  6515 ; 1.354 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10276 ; 0.215 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4886 ; 0.729 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4288 ; 1.195 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
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     2        A   317
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4370 -12.4800  -0.2710
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1076 T22:   0.0560
REMARK   3      T33:  -0.0920 T12:  -0.0899
REMARK   3      T13:   0.0157 T23:  -0.0504
REMARK   3    L TENSOR
REMARK   3      L11:   3.8353 L22:   1.7190
REMARK   3      L33:   3.1437 L12:  -0.5808
REMARK   3      L13:  -0.4596 L23:  -0.2374
REMARK   3    S TENSOR
REMARK   3      S11:   0.0752 S12:   0.1545 S13:  -0.0240
REMARK   3      S21:  -0.2282 S22:  -0.0088 S23:   0.1590
REMARK   3      S31:  -0.2569 S32:  -0.4970 S33:  -0.0663
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 :   B     2        B   317
REMARK   3    ORIGIN FOR THE GROUP (A): -64.2150 -13.8900  27.1960
REMARK   3    T TENSOR
REMARK   3      T11:  -0.2040 T22:   0.0620
REMARK   3      T33:  -0.0933 T12:   0.0326
REMARK   3      T13:   0.0325 T23:   0.0341
REMARK   3    L TENSOR
REMARK   3      L11:   1.6175 L22:   2.5444
REMARK   3      L33:   4.9432 L12:  -0.3863
REMARK   3      L13:   0.1238 L23:  -0.4793
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0648 S12:  -0.0109 S13:  -0.2131
REMARK   3      S21:   0.0132 S22:   0.0636 S23:  -0.0574
REMARK   3      S31:   0.1631 S32:   0.3638 S33:   0.0012
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 :   C     2        C   317
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6970 -26.5640 -26.5770
REMARK   3    T TENSOR
REMARK   3      T11:   0.0106 T22:  -0.1937
REMARK   3      T33:  -0.0818 T12:  -0.0938
REMARK   3      T13:   0.0427 T23:   0.0026
REMARK   3    L TENSOR
REMARK   3      L11:   1.9105 L22:   2.2595
REMARK   3      L33:   4.5937 L12:  -0.2723
REMARK   3      L13:  -0.2655 L23:   0.2481
REMARK   3    S TENSOR
REMARK   3      S11:   0.0269 S12:  -0.1176 S13:  -0.1490
REMARK   3      S21:  -0.0942 S22:  -0.0147 S23:  -0.1616
REMARK   3      S31:   0.3798 S32:  -0.0474 S33:  -0.0123
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 :   D     2        D   317
REMARK   3    ORIGIN FOR THE GROUP (A): -64.4130  14.0990   0.8010
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0649 T22:   0.0241
REMARK   3      T33:  -0.0893 T12:  -0.1258
REMARK   3      T13:  -0.0315 T23:   0.0586
REMARK   3    L TENSOR
REMARK   3      L11:   1.4343 L22:   3.6419
REMARK   3      L33:   3.2273 L12:   0.6097
REMARK   3      L13:  -0.4330 L23:  -0.3232
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0424 S12:  -0.0399 S13:   0.1671
REMARK   3      S21:   0.2671 S22:   0.1345 S23:  -0.0803
REMARK   3      S31:  -0.5074 S32:   0.0776 S33:  -0.0921
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS.
REMARK   4
REMARK   4 2IXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-06.
REMARK 100 THE PDBE ID CODE IS EBI-29335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-3
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93
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 : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42938
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.20000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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   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 2IXO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8MM PEPTIDE, 1M AMMONIUM SULFATE, 3%
REMARK 280  GLYCEROL, 0.1M ADA PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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      273.75067
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      136.87533
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      205.31300
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       68.43767
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      342.18833
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F, G
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, H, I
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 400
REMARK 400 COMPOUND
REMARK 400 THE PEPTIDE IS A PROLINE CONTAINING SUBTSTRATE PEPTIDE ANALOG
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     PRO A    88
REMARK 465     GLY A    89
REMARK 465     PRO A    90
REMARK 465     ARG A    91
REMARK 465     ARG A    92
REMARK 465     TYR A    93
REMARK 465     HIS A   318
REMARK 465     HIS A   319
REMARK 465     HIS A   320
REMARK 465     HIS A   321
REMARK 465     HIS A   322
REMARK 465     HIS A   323
REMARK 465     MET B     1
REMARK 465     HIS B   318
REMARK 465     HIS B   319
REMARK 465     HIS B   320
REMARK 465     HIS B   321
REMARK 465     HIS B   322
REMARK 465     HIS B   323
REMARK 465     MET C     1
REMARK 465     HIS C   318
REMARK 465     HIS C   319
REMARK 465     HIS C   320
REMARK 465     HIS C   321
REMARK 465     HIS C   322
REMARK 465     HIS C   323
REMARK 465     MET D     1
REMARK 465     PRO D    88
REMARK 465     GLY D    89
REMARK 465     PRO D    90
REMARK 465     ARG D    91
REMARK 465     ARG D    92
REMARK 465     TYR D    93
REMARK 465     HIS D   318
REMARK 465     HIS D   319
REMARK 465     HIS D   320
REMARK 465     HIS D   321
REMARK 465     HIS D   322
REMARK 465     HIS D   323
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   OD2  ASP B   223     OG   SER B   281              2.17
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    ARG A 185   CB    ARG A 185   CG      0.223
REMARK 500    ARG A 185   CG    ARG A 185   CD      0.155
REMARK 500    PHE A 263   CZ    PHE A 263   CE2     0.123
REMARK 500    CYS B  98   CB    CYS B  98   SG     -0.122
REMARK 500    CYS C  98   CB    CYS C  98   SG     -0.147
REMARK 500    GLU C 194   CG    GLU C 194   CD      0.137
REMARK 500    LYS C 236   CD    LYS C 236   CE      0.150
REMARK 500    GLU D 194   CG    GLU D 194   CD      0.106
REMARK 500    PHE D 254   CB    PHE D 254   CG     -0.103
REMARK 500    LYS G   5   C     LYS G   5   O       0.212
REMARK 500    LYS H   5   C     LYS H   5   O       0.172
REMARK 500    LYS I   5   C     LYS I   5   O       0.223
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    PRO A 230   C   -  N   -  CA  ANGL. DEV. = -10.0 DEGREES
REMARK 500    LEU A 238   CB  -  CG  -  CD2 ANGL. DEV. =  10.7 DEGREES
REMARK 500    ASP A 272   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG B  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    PRO B  90   C   -  N   -  CA  ANGL. DEV. =  13.8 DEGREES
REMARK 500    LEU B 222   CA  -  CB  -  CG  ANGL. DEV. =  19.0 DEGREES
REMARK 500    ASP C  28   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP C  28   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ASP C  54   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    VAL C 211   CB  -  CA  -  C   ANGL. DEV. = -11.9 DEGREES
REMARK 500    LEU C 222   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    LEU C 228   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES
REMARK 500    LYS C 236   CD  -  CE  -  NZ  ANGL. DEV. =  19.9 DEGREES
REMARK 500    LEU D  87   CA  -  CB  -  CG  ANGL. DEV. =  18.6 DEGREES
REMARK 500    ASP D 106   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    PRO D 110   C   -  N   -  CA  ANGL. DEV. = -10.0 DEGREES
REMARK 500    ARG D 185   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG D 185   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    LEU D 189   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES
REMARK 500    LEU D 234   CA  -  CB  -  CG  ANGL. DEV. = -13.9 DEGREES
REMARK 500    LYS I   5   CB  -  CA  -  C   ANGL. DEV. =  14.9 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    ASP A   7       60.65    -54.12
REMARK 500    HIS A  10      -21.38   -152.02
REMARK 500    THR A  15      120.17    -39.22
REMARK 500    ASP A  22     -164.44   -160.68
REMARK 500    PHE A  29      -34.13    -32.17
REMARK 500    ASP A  54       59.09   -144.56
REMARK 500    THR A  84       73.24   -150.27
REMARK 500    PRO A  86      151.84    -47.08
REMARK 500    LEU A  96      -23.99      8.31
REMARK 500    GLU A 120       23.09    -76.62
REMARK 500    HIS A 122      -18.71    -45.85
REMARK 500    GLN A 129      -41.72    -29.11
REMARK 500    ASN A 134      -15.71   -166.76
REMARK 500    SER A 135       -3.21    -57.81
REMARK 500    SER A 139      -47.32    -25.74
REMARK 500    HIS A 167       54.11     26.59
REMARK 500    PHE A 174     -101.84    -73.84
REMARK 500    LEU A 175      -62.80      1.32
REMARK 500    THR A 192       49.92     78.65
REMARK 500    VAL A 201      -17.21    -41.84
REMARK 500    LEU A 214      -74.68    -47.52
REMARK 500    ASP A 223      -81.29    -11.38
REMARK 500    LEU A 234        0.44    -66.79
REMARK 500    THR A 276      -54.36   -124.65
REMARK 500    VAL A 293      -73.83    -69.43
REMARK 500    GLN A 303      -48.58    -18.94
REMARK 500    HIS A 304       41.57    -99.17
REMARK 500    ASN A 316     -154.92    -84.05
REMARK 500    ARG B  19      -42.25   -137.28
REMARK 500    SER B  50        8.82    -68.51
REMARK 500    CYS B  52       64.78   -114.91
REMARK 500    SER B  62     -167.62    -76.99
REMARK 500    HIS B  79      -30.32    -32.76
REMARK 500    ILE B  81      -43.81    -27.36
REMARK 500    PRO B  88      165.99    -49.38
REMARK 500    PRO B  90       77.68    -42.49
REMARK 500    ARG B  91      -26.01    -22.75
REMARK 500    ALA B  97       -7.29    -36.01
REMARK 500    GLU B 123       22.33    -70.35
REMARK 500    GLU B 127      -70.71    -80.68
REMARK 500    SER B 139      -70.36      0.16
REMARK 500    THR B 140       -2.99   -159.88
REMARK 500    LEU B 142       35.08     74.01
REMARK 500    VAL B 201      -25.75    -29.49
REMARK 500    HIS B 209      -54.92   -139.41
REMARK 500    GLN B 218      -23.08    -36.11
REMARK 500    ASP B 223      -81.51    -24.78
REMARK 500    GLN B 225       31.60    -93.50
REMARK 500    LYS B 243      -28.04    -39.72
REMARK 500    GLN B 250      -51.69    -24.10
REMARK 500
REMARK 500 THIS ENTRY HAS     107 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER B  138     SER B  139                  149.44
REMARK 500 VAL D   17     LYS D   18                  143.46
REMARK 500 GLU D  257     VAL D  258                 -146.57
REMARK 500 GLY D  261     PRO D  262                  140.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR A  25        24.7      L          L   OUTSIDE RANGE
REMARK 500    LEU A  27        23.5      L          L   OUTSIDE RANGE
REMARK 500    VAL A  67        24.2      L          L   OUTSIDE RANGE
REMARK 500    LEU A 109        24.5      L          L   OUTSIDE RANGE
REMARK 500    ASP A 223        24.7      L          L   OUTSIDE RANGE
REMARK 500    ASP B   4        24.4      L          L   OUTSIDE RANGE
REMARK 500    GLU B  83        23.7      L          L   OUTSIDE RANGE
REMARK 500    ARG B  92        21.5      L          L   OUTSIDE RANGE
REMARK 500    LEU B 222        22.5      L          L   OUTSIDE RANGE
REMARK 500    ASP B 223        20.3      L          L   OUTSIDE RANGE
REMARK 500    GLU B 257        20.5      L          L   OUTSIDE RANGE
REMARK 500    VAL B 295        20.4      L          L   OUTSIDE RANGE
REMARK 500    ASP C   4        24.7      L          L   OUTSIDE RANGE
REMARK 500    LEU C 222        20.6      L          L   OUTSIDE RANGE
REMARK 500    ASP C 223        19.5      L          L   OUTSIDE RANGE
REMARK 500    SER C 237        24.7      L          L   OUTSIDE RANGE
REMARK 500    LYS C 243        25.0      L          L   OUTSIDE RANGE
REMARK 500    ASN D  95        21.6      L          L   OUTSIDE RANGE
REMARK 500    VAL D 156        17.9      L          L   OUTSIDE RANGE
REMARK 500    LEU D 222        24.1      L          L   OUTSIDE RANGE
REMARK 500    ASP D 223        23.0      L          L   OUTSIDE RANGE
REMARK 500    LYS D 282        24.5      L          L   OUTSIDE RANGE
REMARK 500    VAL D 295        21.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF RESIDUES 1319 TO 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN F OF SIN-ALA-ALA-PRO-LYS-
REMARK 800  NIT
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN G OF SIN-ALA-ALA-PRO-LYS-
REMARK 800  NIT
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN H OF SIN-ALA-ALA-PRO-LYS-
REMARK 800  NIT
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF SIN-ALA-ALA-PRO-LYS-
REMARK 800  NIT
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IXN   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA2
REMARK 900 PTPA2
REMARK 900 RELATED ID: 2IXO   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA1
REMARK 900 PTPA1
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-317 AND C-TERMINAL HIS TAG
DBREF  2IXP A    1   317  UNP    P40454   PTPA1_YEAST      1    317
DBREF  2IXP A  318   323  PDB    2IXP     2IXP           318    323
DBREF  2IXP B    1   317  UNP    P40454   PTPA1_YEAST      1    317
DBREF  2IXP B  318   323  PDB    2IXP     2IXP           318    323
DBREF  2IXP C    1   317  UNP    P40454   PTPA1_YEAST      1    317
DBREF  2IXP C  318   323  PDB    2IXP     2IXP           318    323
DBREF  2IXP D    1   317  UNP    P40454   PTPA1_YEAST      1    317
DBREF  2IXP D  318   323  PDB    2IXP     2IXP           318    323
DBREF  2IXP F    1     6  PDB    2IXP     2IXP             1      6
DBREF  2IXP G    1     6  PDB    2IXP     2IXP             1      6
DBREF  2IXP H    1     6  PDB    2IXP     2IXP             1      6
DBREF  2IXP I    1     6  PDB    2IXP     2IXP             1      6
SEQRES   1 A  323  MET SER LEU ASP ARG VAL ASP TRP PRO HIS ALA THR PHE
SEQRES   2 A  323  SER THR PRO VAL LYS ARG ILE PHE ASP THR GLN THR THR
SEQRES   3 A  323  LEU ASP PHE GLN SER SER LEU ALA ILE HIS ARG ILE LYS
SEQRES   4 A  323  TYR HIS LEU HIS LYS TYR THR THR LEU ILE SER HIS CYS
SEQRES   5 A  323  SER ASP PRO ASP PRO HIS ALA THR ALA SER SER ILE ALA
SEQRES   6 A  323  MET VAL ASN GLY LEU MET GLY VAL LEU ASP LYS LEU ALA
SEQRES   7 A  323  HIS LEU ILE ASP GLU THR PRO PRO LEU PRO GLY PRO ARG
SEQRES   8 A  323  ARG TYR GLY ASN LEU ALA CYS ARG GLU TRP HIS HIS LYS
SEQRES   9 A  323  LEU ASP GLU ARG LEU PRO GLN TRP LEU GLN GLU MET LEU
SEQRES  10 A  323  PRO SER GLU TYR HIS GLU VAL VAL PRO GLU LEU GLN TYR
SEQRES  11 A  323  TYR LEU GLY ASN SER PHE GLY SER SER THR ARG LEU ASP
SEQRES  12 A  323  TYR GLY THR GLY HIS GLU LEU SER PHE MET ALA THR VAL
SEQRES  13 A  323  ALA ALA LEU ASP MET LEU GLY MET PHE PRO HIS MET ARG
SEQRES  14 A  323  GLY ALA ASP VAL PHE LEU LEU PHE ASN LYS TYR TYR THR
SEQRES  15 A  323  ILE MET ARG ARG LEU ILE LEU THR TYR THR LEU GLU PRO
SEQRES  16 A  323  ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP HIS PHE
SEQRES  17 A  323  HIS LEU VAL TYR ILE LEU GLY SER SER GLN TRP GLN LEU
SEQRES  18 A  323  LEU ASP ALA GLN ALA PRO LEU GLN PRO ARG GLU ILE LEU
SEQRES  19 A  323  ASP LYS SER LEU VAL ARG GLU TYR LYS ASP THR ASN PHE
SEQRES  20 A  323  TYR CYS GLN GLY ILE ASN PHE ILE ASN GLU VAL LYS MET
SEQRES  21 A  323  GLY PRO PHE GLU GLU HIS SER PRO ILE LEU TYR ASP ILE
SEQRES  22 A  323  ALA VAL THR VAL PRO ARG TRP SER LYS VAL CYS LYS GLY
SEQRES  23 A  323  LEU LEU LYS MET TYR SER VAL GLU VAL LEU LYS LYS PHE
SEQRES  24 A  323  PRO VAL VAL GLN HIS PHE TRP PHE GLY THR GLY PHE PHE
SEQRES  25 A  323  PRO TRP VAL ASN ILE HIS HIS HIS HIS HIS HIS
SEQRES   1 B  323  MET SER LEU ASP ARG VAL ASP TRP PRO HIS ALA THR PHE
SEQRES   2 B  323  SER THR PRO VAL LYS ARG ILE PHE ASP THR GLN THR THR
SEQRES   3 B  323  LEU ASP PHE GLN SER SER LEU ALA ILE HIS ARG ILE LYS
SEQRES   4 B  323  TYR HIS LEU HIS LYS TYR THR THR LEU ILE SER HIS CYS
SEQRES   5 B  323  SER ASP PRO ASP PRO HIS ALA THR ALA SER SER ILE ALA
SEQRES   6 B  323  MET VAL ASN GLY LEU MET GLY VAL LEU ASP LYS LEU ALA
SEQRES   7 B  323  HIS LEU ILE ASP GLU THR PRO PRO LEU PRO GLY PRO ARG
SEQRES   8 B  323  ARG TYR GLY ASN LEU ALA CYS ARG GLU TRP HIS HIS LYS
SEQRES   9 B  323  LEU ASP GLU ARG LEU PRO GLN TRP LEU GLN GLU MET LEU
SEQRES  10 B  323  PRO SER GLU TYR HIS GLU VAL VAL PRO GLU LEU GLN TYR
SEQRES  11 B  323  TYR LEU GLY ASN SER PHE GLY SER SER THR ARG LEU ASP
SEQRES  12 B  323  TYR GLY THR GLY HIS GLU LEU SER PHE MET ALA THR VAL
SEQRES  13 B  323  ALA ALA LEU ASP MET LEU GLY MET PHE PRO HIS MET ARG
SEQRES  14 B  323  GLY ALA ASP VAL PHE LEU LEU PHE ASN LYS TYR TYR THR
SEQRES  15 B  323  ILE MET ARG ARG LEU ILE LEU THR TYR THR LEU GLU PRO
SEQRES  16 B  323  ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP HIS PHE
SEQRES  17 B  323  HIS LEU VAL TYR ILE LEU GLY SER SER GLN TRP GLN LEU
SEQRES  18 B  323  LEU ASP ALA GLN ALA PRO LEU GLN PRO ARG GLU ILE LEU
SEQRES  19 B  323  ASP LYS SER LEU VAL ARG GLU TYR LYS ASP THR ASN PHE
SEQRES  20 B  323  TYR CYS GLN GLY ILE ASN PHE ILE ASN GLU VAL LYS MET
SEQRES  21 B  323  GLY PRO PHE GLU GLU HIS SER PRO ILE LEU TYR ASP ILE
SEQRES  22 B  323  ALA VAL THR VAL PRO ARG TRP SER LYS VAL CYS LYS GLY
SEQRES  23 B  323  LEU LEU LYS MET TYR SER VAL GLU VAL LEU LYS LYS PHE
SEQRES  24 B  323  PRO VAL VAL GLN HIS PHE TRP PHE GLY THR GLY PHE PHE
SEQRES  25 B  323  PRO TRP VAL ASN ILE HIS HIS HIS HIS HIS HIS
SEQRES   1 C  323  MET SER LEU ASP ARG VAL ASP TRP PRO HIS ALA THR PHE
SEQRES   2 C  323  SER THR PRO VAL LYS ARG ILE PHE ASP THR GLN THR THR
SEQRES   3 C  323  LEU ASP PHE GLN SER SER LEU ALA ILE HIS ARG ILE LYS
SEQRES   4 C  323  TYR HIS LEU HIS LYS TYR THR THR LEU ILE SER HIS CYS
SEQRES   5 C  323  SER ASP PRO ASP PRO HIS ALA THR ALA SER SER ILE ALA
SEQRES   6 C  323  MET VAL ASN GLY LEU MET GLY VAL LEU ASP LYS LEU ALA
SEQRES   7 C  323  HIS LEU ILE ASP GLU THR PRO PRO LEU PRO GLY PRO ARG
SEQRES   8 C  323  ARG TYR GLY ASN LEU ALA CYS ARG GLU TRP HIS HIS LYS
SEQRES   9 C  323  LEU ASP GLU ARG LEU PRO GLN TRP LEU GLN GLU MET LEU
SEQRES  10 C  323  PRO SER GLU TYR HIS GLU VAL VAL PRO GLU LEU GLN TYR
SEQRES  11 C  323  TYR LEU GLY ASN SER PHE GLY SER SER THR ARG LEU ASP
SEQRES  12 C  323  TYR GLY THR GLY HIS GLU LEU SER PHE MET ALA THR VAL
SEQRES  13 C  323  ALA ALA LEU ASP MET LEU GLY MET PHE PRO HIS MET ARG
SEQRES  14 C  323  GLY ALA ASP VAL PHE LEU LEU PHE ASN LYS TYR TYR THR
SEQRES  15 C  323  ILE MET ARG ARG LEU ILE LEU THR TYR THR LEU GLU PRO
SEQRES  16 C  323  ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP HIS PHE
SEQRES  17 C  323  HIS LEU VAL TYR ILE LEU GLY SER SER GLN TRP GLN LEU
SEQRES  18 C  323  LEU ASP ALA GLN ALA PRO LEU GLN PRO ARG GLU ILE LEU
SEQRES  19 C  323  ASP LYS SER LEU VAL ARG GLU TYR LYS ASP THR ASN PHE
SEQRES  20 C  323  TYR CYS GLN GLY ILE ASN PHE ILE ASN GLU VAL LYS MET
SEQRES  21 C  323  GLY PRO PHE GLU GLU HIS SER PRO ILE LEU TYR ASP ILE
SEQRES  22 C  323  ALA VAL THR VAL PRO ARG TRP SER LYS VAL CYS LYS GLY
SEQRES  23 C  323  LEU LEU LYS MET TYR SER VAL GLU VAL LEU LYS LYS PHE
SEQRES  24 C  323  PRO VAL VAL GLN HIS PHE TRP PHE GLY THR GLY PHE PHE
SEQRES  25 C  323  PRO TRP VAL ASN ILE HIS HIS HIS HIS HIS HIS
SEQRES   1 D  323  MET SER LEU ASP ARG VAL ASP TRP PRO HIS ALA THR PHE
SEQRES   2 D  323  SER THR PRO VAL LYS ARG ILE PHE ASP THR GLN THR THR
SEQRES   3 D  323  LEU ASP PHE GLN SER SER LEU ALA ILE HIS ARG ILE LYS
SEQRES   4 D  323  TYR HIS LEU HIS LYS TYR THR THR LEU ILE SER HIS CYS
SEQRES   5 D  323  SER ASP PRO ASP PRO HIS ALA THR ALA SER SER ILE ALA
SEQRES   6 D  323  MET VAL ASN GLY LEU MET GLY VAL LEU ASP LYS LEU ALA
SEQRES   7 D  323  HIS LEU ILE ASP GLU THR PRO PRO LEU PRO GLY PRO ARG
SEQRES   8 D  323  ARG TYR GLY ASN LEU ALA CYS ARG GLU TRP HIS HIS LYS
SEQRES   9 D  323  LEU ASP GLU ARG LEU PRO GLN TRP LEU GLN GLU MET LEU
SEQRES  10 D  323  PRO SER GLU TYR HIS GLU VAL VAL PRO GLU LEU GLN TYR
SEQRES  11 D  323  TYR LEU GLY ASN SER PHE GLY SER SER THR ARG LEU ASP
SEQRES  12 D  323  TYR GLY THR GLY HIS GLU LEU SER PHE MET ALA THR VAL
SEQRES  13 D  323  ALA ALA LEU ASP MET LEU GLY MET PHE PRO HIS MET ARG
SEQRES  14 D  323  GLY ALA ASP VAL PHE LEU LEU PHE ASN LYS TYR TYR THR
SEQRES  15 D  323  ILE MET ARG ARG LEU ILE LEU THR TYR THR LEU GLU PRO
SEQRES  16 D  323  ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP HIS PHE
SEQRES  17 D  323  HIS LEU VAL TYR ILE LEU GLY SER SER GLN TRP GLN LEU
SEQRES  18 D  323  LEU ASP ALA GLN ALA PRO LEU GLN PRO ARG GLU ILE LEU
SEQRES  19 D  323  ASP LYS SER LEU VAL ARG GLU TYR LYS ASP THR ASN PHE
SEQRES  20 D  323  TYR CYS GLN GLY ILE ASN PHE ILE ASN GLU VAL LYS MET
SEQRES  21 D  323  GLY PRO PHE GLU GLU HIS SER PRO ILE LEU TYR ASP ILE
SEQRES  22 D  323  ALA VAL THR VAL PRO ARG TRP SER LYS VAL CYS LYS GLY
SEQRES  23 D  323  LEU LEU LYS MET TYR SER VAL GLU VAL LEU LYS LYS PHE
SEQRES  24 D  323  PRO VAL VAL GLN HIS PHE TRP PHE GLY THR GLY PHE PHE
SEQRES  25 D  323  PRO TRP VAL ASN ILE HIS HIS HIS HIS HIS HIS
SEQRES   1 F    6  SIN ALA ALA PRO LYS NIT
SEQRES   1 G    6  SIN ALA ALA PRO LYS NIT
SEQRES   1 H    6  SIN ALA ALA PRO LYS NIT
SEQRES   1 I    6  SIN ALA ALA PRO LYS NIT
HET    SIN  F   1       7
HET    NIT  F   6      10
HET    SIN  G   1       7
HET    NIT  G   6      10
HET    SIN  H   1       7
HET    NIT  H   6      10
HET    SIN  I   1       7
HET    NIT  I   6      10
HET    SO4  A1318       5
HET    SO4  A1320       5
HET     CL  A1321       1
HET    SO4  B1319       5
HET    SO4  D1319       5
HET     CL  D1320       1
HETNAM     SIN SUCCINIC ACID
HETNAM     NIT 4-NITROANILINE
HETNAM     SO4 SULFATE ION
HETNAM      CL CHLORIDE ION
HETSYN     NIT PARANITROANILINE
FORMUL   5  SIN    4(C4 H6 O4)
FORMUL   5  NIT    4(C6 H6 N2 O2)
FORMUL   9  SO4    4(O4 S 2-)
FORMUL  11   CL    2(CL 1-)
HELIX    1   1 ASP A   22  GLN A   30  1                                   9
HELIX    2   2 SER A   32  SER A   50  1                                  19
HELIX    3   3 ILE A   64  GLU A   83  1                                  20
HELIX    4   4 ALA A   97  LEU A  117  1                                  21
HELIX    5   5 PRO A  118  GLU A  123  5                                   6
HELIX    6   6 VAL A  124  GLY A  133  1                                  10
HELIX    7   7 GLY A  145  LEU A  162  1                                  18
HELIX    8   8 ARG A  169  THR A  192  1                                  24
HELIX    9   9 HIS A  199  GLY A  203  5                                   5
HELIX   10  10 HIS A  209  LEU A  221  1                                  13
HELIX   11  11 LEU A  222  ALA A  226  5                                   5
HELIX   12  12 GLN A  229  LEU A  234  5                                   6
HELIX   13  13 ASP A  235  LYS A  243  1                                   9
HELIX   14  14 ASN A  246  LYS A  259  1                                  14
HELIX   15  15 PRO A  262  SER A  267  1                                   6
HELIX   16  16 SER A  267  VAL A  277  1                                  11
HELIX   17  17 ARG A  279  GLU A  294  1                                  16
HELIX   18  18 LYS A  298  GLN A  303  1                                   6
HELIX   19  19 ASP B   22  PHE B   29  1                                   8
HELIX   20  20 SER B   32  SER B   50  1                                  19
HELIX   21  21 ILE B   64  GLU B   83  1                                  20
HELIX   22  22 LEU B   96  LEU B  117  1                                  22
HELIX   23  23 PRO B  118  GLU B  123  5                                   6
HELIX   24  24 VAL B  124  ASN B  134  1                                  11
HELIX   25  25 THR B  146  LEU B  162  1                                  17
HELIX   26  26 ARG B  169  THR B  192  1                                  24
HELIX   27  27 HIS B  199  GLY B  203  5                                   5
HELIX   28  28 HIS B  209  GLN B  218  1                                  10
HELIX   29  29 LEU B  222  ALA B  226  5                                   5
HELIX   30  30 ARG B  231  LEU B  234  5                                   4
HELIX   31  31 ASP B  235  LYS B  243  1                                   9
HELIX   32  32 ASN B  246  LYS B  259  1                                  14
HELIX   33  33 PRO B  262  SER B  267  1                                   6
HELIX   34  34 SER B  267  VAL B  277  1                                  11
HELIX   35  35 ARG B  279  VAL B  295  1                                  17
HELIX   36  36 LYS B  298  GLN B  303  1                                   6
HELIX   37  37 ASP C   22  PHE C   29  1                                   8
HELIX   38  38 SER C   32  SER C   50  1                                  19
HELIX   39  39 ILE C   64  HIS C   79  1                                  16
HELIX   40  40 LEU C   80  THR C   84  5                                   5
HELIX   41  41 ALA C   97  LEU C  117  1                                  21
HELIX   42  42 PRO C  118  GLU C  123  5                                   6
HELIX   43  43 VAL C  124  SER C  135  1                                  12
HELIX   44  44 GLY C  145  LEU C  162  1                                  18
HELIX   45  45 ARG C  169  TYR C  191  1                                  23
HELIX   46  46 HIS C  199  GLY C  203  5                                   5
HELIX   47  47 HIS C  209  LEU C  221  1                                  13
HELIX   48  48 LEU C  222  ALA C  226  5                                   5
HELIX   49  49 GLN C  229  LEU C  234  5                                   6
HELIX   50  50 ASP C  235  LYS C  243  1                                   9
HELIX   51  51 ASN C  246  LYS C  259  1                                  14
HELIX   52  52 PRO C  262  SER C  267  1                                   6
HELIX   53  53 SER C  267  VAL C  277  1                                  11
HELIX   54  54 ARG C  279  VAL C  295  1                                  17
HELIX   55  55 LYS C  298  GLN C  303  1                                   6
HELIX   56  56 ASP D   22  SER D   31  1                                  10
HELIX   57  57 SER D   32  SER D   50  1                                  19
HELIX   58  58 ILE D   64  THR D   84  1                                  21
HELIX   59  59 ALA D   97  LEU D  117  1                                  21
HELIX   60  60 PRO D  118  GLU D  123  5                                   6
HELIX   61  61 VAL D  124  GLY D  133  1                                  10
HELIX   62  62 THR D  146  MET D  161  1                                  16
HELIX   63  63 ARG D  169  THR D  192  1                                  24
HELIX   64  64 HIS D  199  GLY D  203  5                                   5
HELIX   65  65 HIS D  209  LEU D  221  1                                  13
HELIX   66  66 LEU D  222  ALA D  226  5                                   5
HELIX   67  67 GLN D  229  LEU D  234  5                                   6
HELIX   68  68 ASP D  235  LYS D  243  1                                   9
HELIX   69  69 ASN D  246  LYS D  259  1                                  14
HELIX   70  70 PRO D  262  SER D  267  1                                   6
HELIX   71  71 SER D  267  VAL D  277  1                                  11
HELIX   72  72 ARG D  279  VAL D  293  1                                  15
HELIX   73  73 LYS D  298  GLN D  303  1                                   6
SHEET    1  AA 2 ASP A 143  TYR A 144  0
SHEET    2  AA 2 GLU A 194  PRO A 195  1  O  GLU A 194   N  TYR A 144
SHEET    1  BA 2 TYR B 144  GLY B 145  0
SHEET    2  BA 2 PRO B 195  ALA B 196  1  N  ALA B 196   O  TYR B 144
SHEET    1  CA 2 ASP C 143  TYR C 144  0
SHEET    2  CA 2 GLU C 194  PRO C 195  1  O  GLU C 194   N  TYR C 144
SHEET    1  DA 2 ASP D 143  GLY D 145  0
SHEET    2  DA 2 GLU D 194  ALA D 196  1  O  GLU D 194   N  TYR D 144
LINK         S   SO4 D1319                 S   SO4 B1319     5445   1555  1.94
LINK         O2  SO4 D1319                 S   SO4 B1319     5445   1555  1.70
LINK         O4  SO4 D1319                 S   SO4 B1319     5445   1555  1.39
LINK         S   SO4 D1319                 O1  SO4 B1319     5445   1555  1.92
LINK         S   SO4 D1319                 O2  SO4 B1319     5445   1555  1.97
LINK         O2  SO4 D1319                 O2  SO4 B1319     5445   1555  1.81
LINK         O4  SO4 D1319                 O2  SO4 B1319     5445   1555  1.87
LINK         O2  SO4 D1319                 O3  SO4 B1319     5445   1555  1.17
LINK         S   SO4 D1319                 O1  SO4 B1319     1555   6564  1.92
LINK         S   SO4 D1319                 S   SO4 B1319     1555   6564  1.94
LINK         S   SO4 D1319                 O2  SO4 B1319     1555   6564  1.97
LINK         O2  SO4 D1319                 S   SO4 B1319     1555   6564  1.70
LINK         O2  SO4 D1319                 O2  SO4 B1319     1555   6564  1.81
LINK         O2  SO4 D1319                 O3  SO4 B1319     1555   6564  1.17
LINK         O4  SO4 D1319                 S   SO4 B1319     1555   6564  1.39
LINK         O4  SO4 D1319                 O2  SO4 B1319     1555   6564  1.87
LINK         O3  SIN F   1                 N   ALA F   2     1555   1555  1.83
LINK         C4  SIN F   1                 N   ALA F   2     1555   1555  1.47
LINK         C   LYS F   5                 N1  NIT F   6     1555   1555  1.88
LINK         C4  SIN G   1                 N   ALA G   2     1555   1555  1.36
LINK         C   LYS G   5                 N1  NIT G   6     1555   1555  1.44
LINK         O3  SIN H   1                 N   ALA H   2     1555   1555  2.03
LINK         C4  SIN H   1                 N   ALA H   2     1555   1555  1.20
LINK         C   LYS H   5                 N1  NIT H   6     1555   1555  1.43
LINK         C4  SIN I   1                 N   ALA I   2     1555   1555  1.19
LINK         C   LYS I   5                 N1  NIT I   6     1555   1555  1.32
CISPEP   1 TRP A    8    PRO A    9          0        -1.41
CISPEP   2 TRP B    8    PRO B    9          0        -5.59
CISPEP   3 TRP C    8    PRO C    9          0        20.17
CISPEP   4 TRP D    8    PRO D    9          0        -0.50
SITE     1 AC1  3 ARG A 169  ALA A 171  ARG C 169
SITE     1 AC2  3 ASP A  22  THR A  23  LYS F   5
SITE     1 AC3  1 MET A 260
SITE     1 AC4  5 ARG B 169  ALA B 171  ARG D 169  ALA D 171
SITE     2 AC4  5 SO4 D1319
SITE     1 AC5  1 MET D 260
SITE     1 AC6  5 ARG B 169  ALA B 171  SO4 B1319  ARG D 169
SITE     2 AC6  5 ALA D 171
SITE     1 AC7 11 THR A  23  LYS A 298  PHE A 299  PRO A 300
SITE     2 AC7 11 SO4 A1320  VAL C 201  TRP C 202  ILE C 269
SITE     3 AC7 11 ASP C 272  ILE C 273  GLY C 286
SITE     1 AC8 12 VAL A 201  TRP A 202  ILE A 269  ASP A 272
SITE     2 AC8 12 ILE A 273  GLY A 286  LEU A 287  THR C  23
SITE     3 AC8 12 LYS C 298  PHE C 299  PRO C 300  ARG D 279
SITE     1 AC9 13 PRO A 278  ARG A 279  THR B  23  LYS B 297
SITE     2 AC9 13 LYS B 298  PHE B 299  PRO B 300  TRP D 202
SITE     3 AC9 13 ILE D 269  ASP D 272  ILE D 273  GLY D 286
SITE     4 AC9 13 LEU D 287
SITE     1 BC1 10 VAL B 201  TRP B 202  PRO B 268  ASP B 272
SITE     2 BC1 10 ILE B 273  GLY B 286  LYS D 297  LYS D 298
SITE     3 BC1 10 PHE D 299  PRO D 300
CRYST1   86.886   86.886  410.626  90.00  90.00 120.00 P 65         24
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      0.011509  0.006645  0.000000        0.00000
SCALE2      0.000000  0.013290  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002435        0.00000
      
PROCHECK
Go to PROCHECK summary
 References