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PDBsum entry 5rub

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Top Page protein Protein-protein interface(s) links
Lyase(carbon-carbon) PDB id
5rub
Jmol
Contents
Protein chains
436 a.a. *
Waters ×736
* Residue conservation analysis
HEADER    LYASE(CARBON-CARBON)                    29-MAY-90   5RUB
TITLE     CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF RIBULOSE-1,5-
TITLE    2 BISPHOSPHATE CARBOXYLASE FROM RHODOSPIRILLUM RUBRUM AT 1.7
TITLE    3 ANGSTROMS RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RUBISCO (RIBULOSE-1,5-BISPHOSPHATE
COMPND   3 CARBOXYLASE(SLASH)OXYGENASE);
COMPND   4 CHAIN: A, B;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE   3 ORGANISM_TAXID: 1085
KEYWDS    LYASE(CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST
REVDAT   3   24-FEB-09 5RUB    1       VERSN
REVDAT   2   01-APR-03 5RUB    1       JRNL
REVDAT   1   15-OCT-91 5RUB    0
SPRSDE     15-OCT-91 5RUB      2RUB
JRNL        AUTH   G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST
JRNL        TITL   CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM
JRNL        TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 A RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 211   989 1990
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   2107319
JRNL        DOI    10.1016/0022-2836(90)90088-4
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND
REMARK   1  TITL 3 ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION
REMARK   1  REF    BIOCHEMISTRY                  V.  30   904 1991
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1 REFERENCE 2
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A
REMARK   1  TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL
REMARK   1  TITL 4 1,5-BISPHOSPHATE
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  7078 1989
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 3
REMARK   1  AUTH   I.ANDERSSON,S.KNIGHT,G.SCHNEIDER,Y.LINDQVIST,
REMARK   1  AUTH 2 T.LUNDQVIST,C.-I.BRANDEN,G.H.LORIMER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE ACTIVE SITE OF
REMARK   1  TITL 2 RIBULOSE-BISPHOSPHATE CARBOXYLASE
REMARK   1  REF    NATURE                        V. 337   229 1989
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 4
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS
REMARK   1  TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE
REMARK   1  REF    J.BIOL.CHEM.                  V. 263  3643 1988
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 5
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE
REMARK   1  TITL 3 CARBOXYLASE(SLASH)OXYGENASE FROM RHODOSPIRILLUM
REMARK   1  TITL 4 RUBRUM AT 2.9 ANGSTROMS RESOLUTION
REMARK   1  REF    EMBO J.                       V.   5  3409 1986
REMARK   1  REFN                   ISSN 0261-4189
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 76452
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6641
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 736
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.018 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.047 ; 0.040
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.050 ; 0.050
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.013 ; 0.020
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.163 ; 0.150
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.196 ; 0.500
REMARK   3    MULTIPLE TORSION                (A) : 0.256 ; 0.500
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : 0.283 ; 0.500
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 2.300 ; 3.000
REMARK   3    STAGGERED                 (DEGREES) : 19.900; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.958 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.682 ; 1.500
REMARK   3   SIDE-CHAIN BOND               (A**2) : 0.944 ; 1.000
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 1.647 ; 1.500
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 5RUB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       35.30000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 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     THR A   -23
REMARK 465     MET A   -22
REMARK 465     ILE A   -21
REMARK 465     THR A   -20
REMARK 465     ASN A   -19
REMARK 465     SER A   -18
REMARK 465     PRO A   -17
REMARK 465     ASP A   -16
REMARK 465     ARG A   -15
REMARK 465     TRP A   -14
REMARK 465     GLY A   -13
REMARK 465     TYR A   -12
REMARK 465     SER A   -11
REMARK 465     ALA A   -10
REMARK 465     PRO A    -9
REMARK 465     HIS A    -8
REMARK 465     ARG A    -7
REMARK 465     THR A    -6
REMARK 465     SER A    -5
REMARK 465     ARG A    -4
REMARK 465     GLU A    -3
REMARK 465     SER A    -2
REMARK 465     PRO A    -1
REMARK 465     PRO A     0
REMARK 465     MET A     1
REMARK 465     ASN A    54
REMARK 465     VAL A    55
REMARK 465     GLU A    56
REMARK 465     VAL A    57
REMARK 465     CYS A    58
REMARK 465     THR A    59
REMARK 465     THR A    60
REMARK 465     ASP A    61
REMARK 465     ASP A    62
REMARK 465     PHE A    63
REMARK 465     THR A    64
REMARK 465     MET A   325
REMARK 465     GLY A   326
REMARK 465     PHE A   327
REMARK 465     GLY A   328
REMARK 465     LYS A   329
REMARK 465     MET A   330
REMARK 465     GLU A   331
REMARK 465     GLY A   332
REMARK 465     GLU A   333
REMARK 465     GLU A   458
REMARK 465     ASP A   459
REMARK 465     THR A   460
REMARK 465     ARG A   461
REMARK 465     SER A   462
REMARK 465     ALA A   463
REMARK 465     LEU A   464
REMARK 465     PRO A   465
REMARK 465     ALA A   466
REMARK 465     THR B   -23
REMARK 465     MET B   -22
REMARK 465     ILE B   -21
REMARK 465     THR B   -20
REMARK 465     ASN B   -19
REMARK 465     SER B   -18
REMARK 465     PRO B   -17
REMARK 465     ASP B   -16
REMARK 465     ARG B   -15
REMARK 465     TRP B   -14
REMARK 465     GLY B   -13
REMARK 465     TYR B   -12
REMARK 465     SER B   -11
REMARK 465     ALA B   -10
REMARK 465     PRO B    -9
REMARK 465     HIS B    -8
REMARK 465     ARG B    -7
REMARK 465     THR B    -6
REMARK 465     SER B    -5
REMARK 465     ARG B    -4
REMARK 465     GLU B    -3
REMARK 465     SER B    -2
REMARK 465     PRO B    -1
REMARK 465     PRO B     0
REMARK 465     MET B     1
REMARK 465     THR B    53
REMARK 465     ASN B    54
REMARK 465     VAL B    55
REMARK 465     GLU B    56
REMARK 465     VAL B    57
REMARK 465     CYS B    58
REMARK 465     THR B    59
REMARK 465     THR B    60
REMARK 465     ASP B    61
REMARK 465     ASP B    62
REMARK 465     PHE B    63
REMARK 465     THR B   324
REMARK 465     MET B   325
REMARK 465     GLY B   326
REMARK 465     PHE B   327
REMARK 465     GLY B   328
REMARK 465     LYS B   329
REMARK 465     MET B   330
REMARK 465     GLU B   331
REMARK 465     GLY B   332
REMARK 465     GLU B   333
REMARK 465     SER B   334
REMARK 465     SER B   335
REMARK 465     GLU B   458
REMARK 465     ASP B   459
REMARK 465     THR B   460
REMARK 465     ARG B   461
REMARK 465     SER B   462
REMARK 465     ALA B   463
REMARK 465     LEU B   464
REMARK 465     PRO B   465
REMARK 465     ALA B   466
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     ASP A    2   N     CB
REMARK 480     THR A   51   CA
REMARK 480     THR A   53   CA
REMARK 480     ARG A   65   CG    CD    NE    CZ    NH1   NH2
REMARK 480     SER A  334   CB    OG
REMARK 480     SER A  335   CB    OG
REMARK 480     GLY A  456   C     O
REMARK 480     VAL A  457   C     O
REMARK 480     ASP B    2   N     CA    C     O
REMARK 480     GLY B   52   O
REMARK 480     THR B   64   N
REMARK 480     GLN B  298   CD    OE1   NE2
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   NH2  ARG B    65     O    HOH B   647              1.72
REMARK 500   O    HOH B   786     O    HOH B   801              1.86
REMARK 500   O    ASP B     2     O    HOH B   745              1.87
REMARK 500   O    HOH A   564     O    HOH A   620              1.90
REMARK 500   O    HOH A   522     O    HOH A   757              1.92
REMARK 500   O    ASN B   111     N    GLN B   113              2.00
REMARK 500   O    GLU B    76     O    HOH B   591              2.02
REMARK 500   NH1  ARG B   411     O    HOH B   815              2.05
REMARK 500   NH2  ARG A   133     O    HOH A   510              2.06
REMARK 500   O    HOH B   494     O    HOH B   844              2.08
REMARK 500   O    HOH A   491     O    HOH A   492              2.09
REMARK 500   O    HOH B   846     O    HOH B   848              2.11
REMARK 500   N    ARG A    65     O    HOH A   506              2.11
REMARK 500   O    HOH B   547     O    HOH B   587              2.12
REMARK 500   O    HOH A   507     O    HOH A   640              2.14
REMARK 500   O    HOH A   611     O    HOH B   469              2.14
REMARK 500   OE2  GLU A    73     O    HOH A   472              2.15
REMARK 500   O    HOH B   714     O    HOH B   816              2.15
REMARK 500   O    HOH B   797     O    HOH B   844              2.15
REMARK 500   NH1  ARG B   452     O    HOH B   860              2.15
REMARK 500   O    HOH B   707     O    HOH B   848              2.15
REMARK 500   OG   SER A   334     O    HOH A   762              2.15
REMARK 500   OE1  GLU B   130     O    HOH B   532              2.16
REMARK 500   O    HOH A   500     O    HOH A   546              2.16
REMARK 500   NH1  ARG B   133     O    HOH B   717              2.17
REMARK 500   O    HOH B   598     O    HOH B   599              2.18
REMARK 500   OD2  ASP A   188     O    HOH A   481              2.19
REMARK 500   O    HOH B   801     O    HOH B   802              2.19
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    GLY A   359     NZ   LYS A   431     2646     1.94
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    GLU A 221   CD    GLU A 221   OE1    -0.069
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    ASP A   2   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES
REMARK 500    ASP A   2   CB  -  CG  -  OD1 ANGL. DEV. =   9.5 DEGREES
REMARK 500    ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    VAL A   8   CA  -  CB  -  CG2 ANGL. DEV. =   9.1 DEGREES
REMARK 500    GLU A  14   CG  -  CD  -  OE1 ANGL. DEV. =  15.7 DEGREES
REMARK 500    GLU A  14   CG  -  CD  -  OE2 ANGL. DEV. = -12.9 DEGREES
REMARK 500    ASP A  16   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES
REMARK 500    ASP A  16   CB  -  CG  -  OD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500    ALA A  34   N   -  CA  -  CB  ANGL. DEV. =  -9.1 DEGREES
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES
REMARK 500    TYR A  72   CB  -  CG  -  CD2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    TYR A  72   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG A  92   NE  -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ASP A 117   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP A 125   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TYR A 127   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    TYR A 127   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    GLU A 130   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.1 DEGREES
REMARK 500    ARG A 133   CD  -  NE  -  CZ  ANGL. DEV. =  24.4 DEGREES
REMARK 500    ARG A 133   NE  -  CZ  -  NH1 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ARG A 133   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    VAL A 141   N   -  CA  -  CB  ANGL. DEV. = -14.6 DEGREES
REMARK 500    ARG A 152   NH1 -  CZ  -  NH2 ANGL. DEV. =  13.0 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.6 DEGREES
REMARK 500    ARG A 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    GLU A 194   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES
REMARK 500    GLU A 194   OE1 -  CD  -  OE2 ANGL. DEV. = -15.4 DEGREES
REMARK 500    GLU A 194   CG  -  CD  -  OE1 ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG A 205   CD  -  NE  -  CZ  ANGL. DEV. = -10.7 DEGREES
REMARK 500    ARG A 205   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 206   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES
REMARK 500    ASP A 213   CB  -  CG  -  OD1 ANGL. DEV. =   7.7 DEGREES
REMARK 500    ASP A 213   CB  -  CG  -  OD2 ANGL. DEV. =  -8.2 DEGREES
REMARK 500    ARG A 216   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 216   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ASP A 236   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    GLU A 239   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES
REMARK 500    ARG A 276   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG A 277   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG A 278   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 288   N   -  CA  -  CB  ANGL. DEV. = -11.3 DEGREES
REMARK 500    ARG A 288   CD  -  NE  -  CZ  ANGL. DEV. =  -9.3 DEGREES
REMARK 500    ARG A 288   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 288   NE  -  CZ  -  NH2 ANGL. DEV. =   9.2 DEGREES
REMARK 500    GLN A 298   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES
REMARK 500    ARG A 313   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     142 ANGLE DEVIATIONS.
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    GLN A   3       65.19    145.81
REMARK 500    SER A   4       36.99    -78.43
REMARK 500    SER A   5      -31.92   -162.40
REMARK 500    LYS A  33      162.24    -41.85
REMARK 500    ALA A  34       92.38    -55.97
REMARK 500    SER A  50      -94.55   -138.19
REMARK 500    MET A 109       12.94   -145.51
REMARK 500    MET A 115      172.26    -57.28
REMARK 500    ASN A 198       51.36   -113.19
REMARK 500    ALA A 202       70.40   -152.64
REMARK 500    ALA A 289      124.72    -28.05
REMARK 500    SER A 335      117.34    100.93
REMARK 500    ASP A 445      -71.69    -36.74
REMARK 500    GLN B   3       86.49    -36.13
REMARK 500    SER B  50     -104.83   -127.32
REMARK 500    ARG B  65       52.84   -100.17
REMARK 500    ASN B 112       -4.24    -24.70
REMARK 500    MET B 115     -145.50    -89.89
REMARK 500    TYR B 120      148.71   -170.27
REMARK 500    ASN B 198       45.37   -109.09
REMARK 500    ALA B 202       67.89   -157.67
REMARK 500    ALA B 289      129.08    -35.29
REMARK 500    PRO B 297       31.17    -82.02
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    ARG B 277         0.13    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 524        DISTANCE =  6.51 ANGSTROMS
REMARK 525    HOH B 545        DISTANCE =  5.65 ANGSTROMS
REMARK 525    HOH B 569        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH B 602        DISTANCE =  5.00 ANGSTROMS
REMARK 525    HOH A 621        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH B 624        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH B 652        DISTANCE =  8.27 ANGSTROMS
REMARK 525    HOH A 671        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH B 692        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH B 693        DISTANCE =  7.15 ANGSTROMS
REMARK 525    HOH B 696        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH A 698        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH A 700        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH B 719        DISTANCE =  6.88 ANGSTROMS
REMARK 525    HOH A 738        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH B 757        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH B 761        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH B 772        DISTANCE =  8.48 ANGSTROMS
REMARK 525    HOH B 774        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH A 779        DISTANCE =  5.45 ANGSTROMS
REMARK 525    HOH B 785        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH B 798        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH A 799        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A 800        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH B 805        DISTANCE =  8.59 ANGSTROMS
REMARK 525    HOH B 813        DISTANCE =  7.65 ANGSTROMS
REMARK 525    HOH B 836        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH B 849        DISTANCE =  6.31 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS
REMARK 700 BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS.  THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND
REMARK 700 LAST STRANDS ARE IDENTICAL.
DBREF  5RUB A    1   466  UNP    P04718   RBL2_RHORU       1    466
DBREF  5RUB B    1   466  UNP    P04718   RBL2_RHORU       1    466
SEQADV 5RUB ASP A   91  UNP  P04718    HIS    91 CONFLICT
SEQADV 5RUB ASP B   91  UNP  P04718    HIS    91 CONFLICT
SEQRES   1 A  490  THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER
SEQRES   2 A  490  ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP
SEQRES   3 A  490  GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU
SEQRES   4 A  490  ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR
SEQRES   5 A  490  ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR
SEQRES   6 A  490  ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN
SEQRES   7 A  490  VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL
SEQRES   8 A  490  ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU
SEQRES   9 A  490  THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN
SEQRES  10 A  490  ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR
SEQRES  11 A  490  LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU
SEQRES  12 A  490  TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR
SEQRES  13 A  490  ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA
SEQRES  14 A  490  LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY
SEQRES  15 A  490  LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU
SEQRES  16 A  490  ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP
SEQRES  17 A  490  LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY
SEQRES  18 A  490  ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU
SEQRES  19 A  490  VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY
SEQRES  20 A  490  GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP
SEQRES  21 A  490  PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU
SEQRES  22 A  490  THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL
SEQRES  23 A  490  ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA
SEQRES  24 A  490  ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG
SEQRES  25 A  490  ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG
SEQRES  26 A  490  GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU
SEQRES  27 A  490  GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE
SEQRES  28 A  490  GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA
SEQRES  29 A  490  TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR
SEQRES  30 A  490  ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE
SEQRES  31 A  490  ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE
SEQRES  32 A  490  PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA
SEQRES  33 A  490  GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA
SEQRES  34 A  490  GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG
SEQRES  35 A  490  ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS
SEQRES  36 A  490  GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA
SEQRES  37 A  490  ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL
SEQRES  38 A  490  GLU ASP THR ARG SER ALA LEU PRO ALA
SEQRES   1 B  490  THR MET ILE THR ASN SER PRO ASP ARG TRP GLY TYR SER
SEQRES   2 B  490  ALA PRO HIS ARG THR SER ARG GLU SER PRO PRO MET ASP
SEQRES   3 B  490  GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS GLU GLU
SEQRES   4 B  490  ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS ALA TYR
SEQRES   5 B  490  ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL ALA THR
SEQRES   6 B  490  ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY THR ASN
SEQRES   7 B  490  VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG GLY VAL
SEQRES   8 B  490  ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG GLU LEU
SEQRES   9 B  490  THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP ARG ASN
SEQRES  10 B  490  ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE LEU THR
SEQRES  11 B  490  LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP VAL GLU
SEQRES  12 B  490  TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU ALA TYR
SEQRES  13 B  490  ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE SER ALA
SEQRES  14 B  490  LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP GLY GLY
SEQRES  15 B  490  LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU GLY LEU
SEQRES  16 B  490  ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA PHE TRP
SEQRES  17 B  490  LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO GLN GLY
SEQRES  18 B  490  ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE ALA LEU
SEQRES  19 B  490  VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU THR GLY
SEQRES  20 B  490  GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA ASP ASP
SEQRES  21 B  490  PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL LEU GLU
SEQRES  22 B  490  THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU LEU VAL
SEQRES  23 B  490  ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR THR ALA
SEQRES  24 B  490  ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR HIS ARG
SEQRES  25 B  490  ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER LYS ARG
SEQRES  26 B  490  GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA ARG LEU
SEQRES  27 B  490  GLN GLY ALA SER GLY ILE HIS THR GLY THR MET GLY PHE
SEQRES  28 B  490  GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA ILE ALA
SEQRES  29 B  490  TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO PHE TYR
SEQRES  30 B  490  ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR PRO ILE
SEQRES  31 B  490  ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO GLY PHE
SEQRES  32 B  490  PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU THR ALA
SEQRES  33 B  490  GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO VAL ALA
SEQRES  34 B  490  GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA TRP ARG
SEQRES  35 B  490  ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU HIS LYS
SEQRES  36 B  490  GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY ASP ALA
SEQRES  37 B  490  ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU GLY VAL
SEQRES  38 B  490  GLU ASP THR ARG SER ALA LEU PRO ALA
FORMUL   3  HOH   *736(H2 O)
HELIX    1 AHA GLU A   14  GLY A   20  1                                   7
HELIX    2 AHB TYR A   38  SER A   49  1                                  12
HELIX    3 AHC ILE A  101  MET A  109  1                                   9
HELIX    4 AHD GLU A  130  ARG A  133  1                                   4
HELIX    5 AHE SER A  144  LEU A  150  1                                   7
HELIX    6 AH1 PRO A  173  TRP A  184  1                                  12
HELIX    7 AH2 LEU A  204  THR A  222  1                                  19
HELIX    8 AH3 ASP A  235  PHE A  251  1                                  17
HELIX    9 AH4 ALA A  269  ARG A  278  1                                  10
HELIX   10 AHF GLY A  292  THR A  295  1                                   4
HELIX   11 AH5 ALA A  305  GLN A  315  1                                  11
HELIX   12 AH6 ARG A  337  THR A  344  1                                   8
HELIX   13 AH7 MET A  376  LEU A  383  1                                   8
HELIX   14 AH8 PRO A  403  ASP A  419  1                                  17
HELIX   15 AHG VAL A  423  GLU A  429  1                                   7
HELIX   16 AHH LYS A  431  PHE A  440  1                                  10
HELIX   17 AHI GLY A  442  TYR A  448  1                                   7
HELIX   18 AHJ TRP A  451  LEU A  455  1                                   5
HELIX   19 AHA GLU B   14  GLY B   20  1                                   7
HELIX   20 AHB TYR B   38  SER B   49  1                                  12
HELIX   21 AHC ILE B  101  MET B  109  1                                   9
HELIX   22 AHD GLU B  130  ARG B  133  1                                   4
HELIX   23 AHE SER B  144  LEU B  150  1                                   7
HELIX   24 AH1 PRO B  173  TRP B  184  1                                  12
HELIX   25 AH2 LEU B  204  THR B  222  1                                  19
HELIX   26 AH3 ASP B  235  PHE B  251  1                                  17
HELIX   27 AH4 ALA B  269  ARG B  278  1                                  10
HELIX   28 AHF GLY B  292  THR B  295  1                                   4
HELIX   29 AH5 ALA B  305  GLN B  315  1                                  11
HELIX   30 AH6 ARG B  337  THR B  344  1                                   8
HELIX   31 AH7 MET B  376  LEU B  383  1                                   8
HELIX   32 AH8 PRO B  403  ASP B  419  1                                  17
HELIX   33 AHG VAL B  423  GLU B  429  1                                   7
HELIX   34 AHH LYS B  431  PHE B  440  1                                  10
HELIX   35 AHI GLY B  442  TYR B  448  1                                   7
HELIX   36 AHJ TRP B  451  LEU B  455  1                                   5
SHEET    1 ANT 5 VAL A   8  LEU A  10  0
SHEET    2 ANT 5 LEU A  70  ASP A  75  1
SHEET    3 ANT 5 GLU A  79  PRO A  86 -1
SHEET    4 ANT 5 HIS A  23  PRO A  32 -1
SHEET    5 ANT 5 ASP A 117  TYR A 127 -1
SHEET    1 ACT 9 VAL A 160  ILE A 164  0
SHEET    2 ACT 9 PHE A 189  LYS A 191  1
SHEET    3 ACT 9 LEU A 227  ASN A 231  1
SHEET    4 ACT 9 VAL A 258  ASP A 263  1
SHEET    5 ACT 9 LEU A 284  HIS A 287  1
SHEET    6 ACT 9 GLY A 319  HIS A 321  1
SHEET    7 ACT 9 THR A 364  GLY A 369  1
SHEET    8 ACT 9 ILE A 389  ALA A 392  1
SHEET    9 ACT 9 VAL A 160  ILE A 164  1
SHEET    1 BNT 5 VAL B   8  LEU B  10  0
SHEET    2 BNT 5 LEU B  70  ASP B  75  1
SHEET    3 BNT 5 GLU B  79  PRO B  86 -1
SHEET    4 BNT 5 HIS B  23  PRO B  32 -1
SHEET    5 BNT 5 ASP B 117  TYR B 127 -1
SHEET    1 BCT 9 VAL B 160  ILE B 164  0
SHEET    2 BCT 9 PHE B 189  LYS B 191  1
SHEET    3 BCT 9 LEU B 227  ASN B 231  1
SHEET    4 BCT 9 VAL B 258  ASP B 263  1
SHEET    5 BCT 9 LEU B 284  HIS B 287  1
SHEET    6 BCT 9 GLY B 319  HIS B 321  1
SHEET    7 BCT 9 THR B 364  GLY B 369  1
SHEET    8 BCT 9 ILE B 389  ALA B 392  1
SHEET    9 BCT 9 VAL B 160  ILE B 164  1
CISPEP   1 LYS A  166    PRO A  167          0         0.50
CISPEP   2 LYS B  166    PRO B  167          0         1.17
CRYST1   65.500   70.600  104.100  90.00  92.10  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.036668        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000672        0.00000
SCALE1      0.015267  0.000000  0.000560        0.00000
SCALE2      0.000000  0.014164  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009613        0.00000
MTRIX1   1  0.373740 -0.056207  0.940855        6.14161    1
MTRIX2   1 -0.073400 -0.996800 -0.033512       17.87800    1
MTRIX3   1  0.909789 -0.054363 -0.376740       -7.57091    1
      
PROCHECK
Go to PROCHECK summary
 References