longtext: 2PSF-pdb

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HEADER    OXIDOREDUCTASE                          06-MAY-07   2PSF
TITLE     CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT
TITLE    2 PROTEIN FROM RENILLA RENIFORMIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RENILLA-LUCIFERIN 2-MONOOXYGENASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: RENILLA-TYPE LUCIFERASE;
COMPND   5 EC: 1.13.12.5;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;
SOURCE   3 ORGANISM_COMMON: SEA PANSY;
SOURCE   4 GENE: RLUC;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: LMG194;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS    ALPHA/BETA-HYDROLASE, LUCIFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.M.LOENING,T.D.FENN,S.S.GAMBHIR
REVDAT   1   22-MAY-07 2PSF    0
JRNL        AUTH   A.M.LOENING,T.D.FENN,S.S.GAMBHIR
JRNL        TITL   CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN
JRNL        TITL 2 FLUORESCENT PROTEIN FROM RENILLA RENIFORMIS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 1.40 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) : 1.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3
REMARK   3   NUMBER OF REFLECTIONS             : 111557
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) : 0.174
REMARK   3   R VALUE            (WORKING SET) : 0.173
REMARK   3   FREE R VALUE                     : 0.194
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5879
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.40
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.44
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7585
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.47
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800
REMARK   3   BIN FREE R VALUE SET COUNT          : 406
REMARK   3   BIN FREE R VALUE                    : 0.2890
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   ALL ATOMS                : 5773
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.56
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.06000
REMARK   3    B22 (A**2) : -0.28000
REMARK   3    B33 (A**2) : 0.22000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.063
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.063
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.980
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5127 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  3578 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6942 ; 1.209 ; 1.951
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8697 ; 0.882 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   606 ; 5.522 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   250 ;34.561 ;24.040
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   898 ;12.162 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;14.842 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   723 ; 0.078 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5645 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  1063 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1084 ; 0.213 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3870 ; 0.193 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2515 ; 0.184 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2440 ; 0.083 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   552 ; 0.113 ; 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):     7 ; 0.126 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.186 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    48 ; 0.107 ; 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):  3949 ; 0.710 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1213 ; 0.121 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4928 ; 0.807 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2514 ; 1.584 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2014 ; 2.159 ; 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 : 0
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
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     3        A   309
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7062  10.7135  10.6740
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1185 T22:  -0.1306
REMARK   3      T33:  -0.1229 T12:   0.0066
REMARK   3      T13:   0.0076 T23:   0.0072
REMARK   3    L TENSOR
REMARK   3      L11:   0.5407 L22:   0.9246
REMARK   3      L33:   1.2508 L12:  -0.0927
REMARK   3      L13:   0.0429 L23:   0.1969
REMARK   3    S TENSOR
REMARK   3      S11:   0.0211 S12:   0.0105 S13:   0.0475
REMARK   3      S21:   0.0113 S22:   0.0046 S23:  -0.0319
REMARK   3      S31:  -0.1100 S32:   0.0357 S33:  -0.0258
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    10        B   310
REMARK   3    ORIGIN FOR THE GROUP (A):  36.8687 -24.9450 -12.8322
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1195 T22:  -0.1257
REMARK   3      T33:  -0.1093 T12:   0.0062
REMARK   3      T13:  -0.0064 T23:  -0.0044
REMARK   3    L TENSOR
REMARK   3      L11:   0.8653 L22:   1.4255
REMARK   3      L33:   1.2525 L12:   0.2394
REMARK   3      L13:  -0.0018 L23:  -0.0027
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0112 S12:  -0.0082 S13:  -0.1398
REMARK   3      S21:   0.0386 S22:   0.0439 S23:  -0.0838
REMARK   3      S31:   0.1235 S32:   0.0184 S33:  -0.0327
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2PSF COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK   4
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-05-18)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .
REMARK 100 THE RCSB ID CODE IS RCSB042732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-SEP-2005
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.40
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.2.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
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   : 111557
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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   (%): 41.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4M SODIUM ACETATE, 20% W/V PEG
REMARK 280  3350, 1.8MM N-DECYL-BETA-D-THIOMALTOSIDE, PH 7.4, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-Y,-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       40.58900
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.18950
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.13950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.18950
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.58900
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.13950
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A     2
REMARK 465     GLU A   310
REMARK 465     GLN A   311
REMARK 465     GLY B     2
REMARK 465     SER B     3
REMARK 465     LYS B     4
REMARK 465     VAL B     5
REMARK 465     TYR B     6
REMARK 465     ASP B     7
REMARK 465     PRO B     8
REMARK 465     GLU B     9
REMARK 465     GLN B   311
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
REMARK 500   NZ   LYS B   193     O    HOH     771              1.99
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    PRO A   8   CB    PRO A   8   CG    -0.046
REMARK 500    GLU A  68   CB    GLU A  68   CG    -0.063
REMARK 500    MET A 295   SD    MET A 295   CE     0.052
REMARK 500    GLU B  68   CB    GLU B  68   CG    -0.062
REMARK 500    ILE B  79   CG1   ILE B  79   CD1    0.047
REMARK 500    PRO B 111   CB    PRO B 111   CG    -0.054
REMARK 500    MET B 295   SD    MET B 295   CE     0.081
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    TYR A 240   CA  -  CB  -  CG  ANGL. DEV. =  7.9 DEGREES
REMARK 500    LEU A 287   CA  -  CB  -  CG  ANGL. DEV. =  9.9 DEGREES
REMARK 500    ILE B 159   N   -  CA  -  C   ANGL. DEV. =  7.9 DEGREES
REMARK 500    TYR B 240   CA  -  CB  -  CG  ANGL. DEV. =  7.3 DEGREES
REMARK 500    LEU B 287   CA  -  CB  -  CG  ANGL. DEV. = 10.8 DEGREES
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  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A  40      -51.20     70.84
REMARK 500    LEU B  30     -118.80     53.87
REMARK 500    GLU B  40      -49.60     73.83
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH   699        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH   732        DISTANCE =  6.54 ANGSTROMS
REMARK 525    HOH   760        DISTANCE =  6.98 ANGSTROMS
REMARK 525    HOH   770        DISTANCE =  5.44 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PSD   RELATED DB: PDB
REMARK 900 RELATED ID: 2PSE   RELATED DB: PDB
REMARK 900 RELATED ID: 2PSH   RELATED DB: PDB
REMARK 900 RELATED ID: 2PSJ   RELATED DB: PDB
REMARK 900 RELATED ID: 2PSL   RELATED DB: PDB
DBREF  2PSF A    3   311  UNP    P27652   LUCI_RENRE       3    311
DBREF  2PSF B    3   311  UNP    P27652   LUCI_RENRE       3    311
SEQADV 2PSF GLY A    2  UNP  P27652              CLONING ARTIFACT
SEQADV 2PSF THR A   55  UNP  P27652    ALA    55 ENGINEERED
SEQADV 2PSF ALA A  124  UNP  P27652    CYS   124 ENGINEERED
SEQADV 2PSF ALA A  130  UNP  P27652    SER   130 ENGINEERED
SEQADV 2PSF ARG A  136  UNP  P27652    LYS   136 ENGINEERED
SEQADV 2PSF MET A  143  UNP  P27652    ALA   143 ENGINEERED
SEQADV 2PSF VAL A  185  UNP  P27652    MET   185 ENGINEERED
SEQADV 2PSF LEU A  253  UNP  P27652    MET   253 ENGINEERED
SEQADV 2PSF LEU A  287  UNP  P27652    SER   287 ENGINEERED
SEQADV 2PSF GLY B    2  UNP  P27652              CLONING ARTIFACT
SEQADV 2PSF THR B   55  UNP  P27652    ALA    55 ENGINEERED
SEQADV 2PSF ALA B  124  UNP  P27652    CYS   124 ENGINEERED
SEQADV 2PSF ALA B  130  UNP  P27652    SER   130 ENGINEERED
SEQADV 2PSF ARG B  136  UNP  P27652    LYS   136 ENGINEERED
SEQADV 2PSF MET B  143  UNP  P27652    ALA   143 ENGINEERED
SEQADV 2PSF VAL B  185  UNP  P27652    MET   185 ENGINEERED
SEQADV 2PSF LEU B  253  UNP  P27652    MET   253 ENGINEERED
SEQADV 2PSF LEU B  287  UNP  P27652    SER   287 ENGINEERED
SEQRES   1 A  310  GLY SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET
SEQRES   2 A  310  ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET
SEQRES   3 A  310  ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU
SEQRES   4 A  310  LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN
SEQRES   5 A  310  ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS
SEQRES   6 A  310  ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE
SEQRES   7 A  310  GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR
SEQRES   8 A  310  ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE
SEQRES   9 A  310  GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY
SEQRES  10 A  310  HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR
SEQRES  11 A  310  GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU
SEQRES  12 A  310  SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO
SEQRES  13 A  310  ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU
SEQRES  14 A  310  GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU
SEQRES  15 A  310  THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO
SEQRES  16 A  310  GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS
SEQRES  17 A  310  GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU
SEQRES  18 A  310  ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN
SEQRES  19 A  310  ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP
SEQRES  20 A  310  ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE
SEQRES  21 A  310  PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO
SEQRES  22 A  310  ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU
SEQRES  23 A  310  GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS
SEQRES  24 A  310  SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN
SEQRES   1 B  310  GLY SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET
SEQRES   2 B  310  ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET
SEQRES   3 B  310  ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU
SEQRES   4 B  310  LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN
SEQRES   5 B  310  ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS
SEQRES   6 B  310  ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE
SEQRES   7 B  310  GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR
SEQRES   8 B  310  ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE
SEQRES   9 B  310  GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY
SEQRES  10 B  310  HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR
SEQRES  11 B  310  GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU
SEQRES  12 B  310  SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO
SEQRES  13 B  310  ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU
SEQRES  14 B  310  GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU
SEQRES  15 B  310  THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO
SEQRES  16 B  310  GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS
SEQRES  17 B  310  GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU
SEQRES  18 B  310  ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN
SEQRES  19 B  310  ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP
SEQRES  20 B  310  ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE
SEQRES  21 B  310  PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO
SEQRES  22 B  310  ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU
SEQRES  23 B  310  GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS
SEQRES  24 B  310  SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN
FORMUL   3  HOH   *790(H2 O)
HELIX    1   1 PRO A    8  ARG A   13  1                                   6
HELIX    2   2 THR A   16  ARG A   23  1                                   8
HELIX    3   3 SER A   56  ARG A   61  5                                   6
HELIX    4   4 VAL A   63  ILE A   67  5                                   5
HELIX    5   5 ARG A   93  GLU A  106  1                                  14
HELIX    6   6 ASP A  120  HIS A  133  1                                  14
HELIX    7   7 ASP A  158  SER A  168  1                                  11
HELIX    8   8 SER A  168  GLU A  177  1                                  10
HELIX    9   9 ASN A  179  THR A  184  1                                   6
HELIX   10  10 THR A  184  LYS A  189  1                                   6
HELIX   11  11 GLU A  195  GLU A  204  1                                  10
HELIX   12  12 PRO A  205  LYS A  207  5                                   3
HELIX   13  13 GLY A  210  VAL A  212  5                                   3
HELIX   14  14 ARG A  213  GLU A  222  1                                  10
HELIX   15  15 LYS A  230  ALA A  246  1                                  17
HELIX   16  16 PHE A  262  LYS A  271  1                                  10
HELIX   17  17 PHE A  286  ASP A  290  5                                   5
HELIX   18  18 ALA A  291  ASN A  309  1                                  19
HELIX   19  19 THR B   16  ALA B   22  1                                   7
HELIX   20  20 SER B   56  ARG B   61  5                                   6
HELIX   21  21 VAL B   63  ILE B   67  5                                   5
HELIX   22  22 ARG B   93  GLU B  106  1                                  14
HELIX   23  23 ASP B  120  HIS B  133  1                                  14
HELIX   24  24 ILE B  159  SER B  168  1                                  10
HELIX   25  25 GLU B  169  GLU B  177  1                                   9
HELIX   26  26 ASN B  179  THR B  184  1                                   6
HELIX   27  27 THR B  184  LYS B  189  1                                   6
HELIX   28  28 GLU B  195  GLU B  204  1                                  10
HELIX   29  29 PRO B  205  LYS B  207  5                                   3
HELIX   30  30 GLY B  210  VAL B  212  5                                   3
HELIX   31  31 ARG B  213  GLU B  222  1                                  10
HELIX   32  32 LYS B  230  ALA B  246  1                                  17
HELIX   33  33 PHE B  262  LYS B  271  1                                  10
HELIX   34  34 PHE B  286  ASP B  290  5                                   5
HELIX   35  35 ALA B  291  GLU B  310  1                                  20
SHEET    1   A 8 LYS A  25  VAL A  29  0
SHEET    2   A 8 SER A  32  ASP A  38 -1  O  TYR A  36   N  LYS A  25
SHEET    3   A 8 ARG A  72  PRO A  76 -1  O  ILE A  75   N  TYR A  37
SHEET    4   A 8 ALA A  46  LEU A  50  1  N  VAL A  47   O  ARG A  72
SHEET    5   A 8 ILE A 114  HIS A 119  1  O  ILE A 115   N  ILE A  48
SHEET    6   A 8 ILE A 137  MET A 143  1  O  VAL A 141   N  PHE A 116
SHEET    7   A 8 LYS A 252  PRO A 259  1  O  LEU A 253   N  HIS A 142
SHEET    8   A 8 THR A 276  GLY A 283  1  O  GLU A 277   N  PHE A 254
SHEET    1   B 8 LYS B  25  VAL B  29  0
SHEET    2   B 8 SER B  32  ASP B  38 -1  O  TYR B  36   N  LYS B  25
SHEET    3   B 8 ARG B  72  PRO B  76 -1  O  ILE B  75   N  TYR B  37
SHEET    4   B 8 ALA B  46  LEU B  50  1  N  VAL B  47   O  ARG B  72
SHEET    5   B 8 ILE B 114  HIS B 119  1  O  ILE B 115   N  ILE B  48
SHEET    6   B 8 ILE B 137  MET B 143  1  O  VAL B 141   N  PHE B 116
SHEET    7   B 8 LYS B 252  PRO B 259  1  O  LEU B 253   N  HIS B 142
SHEET    8   B 8 THR B 276  GLY B 283  1  O  VAL B 279   N  GLU B 256
CISPEP   1 ASP A  258    PRO A  259          0         5.59
CISPEP   2 ASP B  258    PRO B  259          0         5.02
CRYST1   81.178   82.279   90.379  90.00  90.00  90.00 P 21 21 21    8
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      0.012319  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012154  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011065        0.00000
TER    2517      ASN A 309
TER    4985      GLU B 310
MASTER      373    0    0   35   16    0    0    6 5773    2    0   48
END