longtext: 4L0C-pdb

content
HEADER    HYDROLASE                               31-MAY-13   4L0C
TITLE     CRYTAL STRUCTURE OF THE N-FOPMYLMALEAMIC ACID DEFORMYLASE NFO(S94A)
TITLE    2 FROM PSEUDOMONAS PUTIDA S16
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DEFORMYLASE;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;
COMPND   4 SYNONYM: N-FORMYLMALEAMATE DEFORMYLASE, NFO;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE   3 ORGANISM_TAXID: 1042876;
SOURCE   4 STRAIN: S16;
SOURCE   5 GENE: PPS_4059;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    DEFORMYLASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.CHEN,Y.LU,Z.ZHANG,G.WU,P.XU
REVDAT   1   04-JUN-14 4L0C    0
JRNL        AUTH   D.CHEN,Y.LU,Z.ZHANG,G.WU,P.XU
JRNL        TITL   CRYTAL STRUCTURE OF THE N-FOPMYLMALEAMIC ACID DEFORMYLASE
JRNL        TITL 2 NFO FROM PSEUDOMONAS PUTIDA S16
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
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) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.57
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 226522
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) : 0.186
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 11941
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) : 1.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 16459
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.53
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320
REMARK   3   BIN FREE R VALUE SET COUNT          : 821
REMARK   3   BIN FREE R VALUE                    : 0.2540
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 15728
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 47
REMARK   3   SOLVENT ATOMS            : 2104
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.22
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.34000
REMARK   3    B22 (A**2) : 0.99000
REMARK   3    B33 (A**2) : 0.32000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.20000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16325 ; 0.009 ; 0.020
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22305 ; 1.284 ; 1.959
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2077 ; 5.389 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   715 ;29.087 ;23.063
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2382 ;12.409 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   128 ;14.988 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2518 ; 0.084 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12548 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
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  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK   3  THE INPUT
REMARK   4
REMARK   4 4L0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB080020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRF
REMARK 200  BEAMLINE                       : BL17U
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 239055
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.570
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) : 1.65
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: SAD
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   (%): 44.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG8000, 0.3M NABR, 0.1M TRIS PH
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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       43.63400
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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     ASN C   254
REMARK 465     ARG C   255
REMARK 465     ASN D   254
REMARK 465     ARG D   255
REMARK 465     MSE F     1
REMARK 465     GLU F   235
REMARK 465     ARG F   255
REMARK 465     MSE G     1
REMARK 465     ASN G   254
REMARK 465     ARG G   255
REMARK 465     MSE H     1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     MSE A  85    CG  SE    CE
REMARK 470     GLU A  86    CG   CD   OE1  OE2
REMARK 470     GLU C 235    CG   CD   OE1  OE2
REMARK 470     GLU D 235    CG   CD   OE1  OE2
REMARK 470     GLU F 234    CG   CD   OE1  OE2
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   O    HOH G   453     O    HOH H   696              2.17
REMARK 500   O    HOH B   402     O    HOH B   652              2.18
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    ARG G 105   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    MSE H  74   CA  -  CB  -  CG  ANGL. DEV. = -10.3 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    SER A  64     -158.46   -131.67
REMARK 500    ALA A  94     -112.66     64.66
REMARK 500    GLU A 235       -3.64     71.40
REMARK 500    ASN A 244       82.81   -152.22
REMARK 500    SER B  64     -158.75   -131.43
REMARK 500    ALA B  94     -111.46     62.43
REMARK 500    GLU B 235       -4.32     68.78
REMARK 500    ASN B 244       81.95   -151.72
REMARK 500    SER C  64     -159.92   -127.99
REMARK 500    ALA C  94     -115.62     62.51
REMARK 500    GLU C 235      -18.16     65.16
REMARK 500    ASN C 244       79.62   -154.71
REMARK 500    SER D  64     -162.81   -129.59
REMARK 500    ALA D  94     -113.59     59.66
REMARK 500    ASN D 244       82.02   -150.29
REMARK 500    SER E  64     -158.03   -128.84
REMARK 500    ALA E  94     -114.71     61.05
REMARK 500    ASP E 107       75.10   -157.31
REMARK 500    GLU E 235       -7.40     73.43
REMARK 500    ASN E 244       82.77   -150.11
REMARK 500    ASN E 254       17.37     59.06
REMARK 500    SER F  64     -155.49   -130.66
REMARK 500    ALA F  94     -116.47     63.05
REMARK 500    ASP F 107       87.78   -156.68
REMARK 500    ALA G  94     -113.23     63.42
REMARK 500    GLU G 235      -11.33     70.85
REMARK 500    ASN G 244       82.42   -153.66
REMARK 500    SER H  64     -159.18   -131.97
REMARK 500    ALA H  94     -114.31     59.17
REMARK 500    ASP H 107       73.98   -156.73
REMARK 500    GLU H 235       -6.65     72.22
REMARK 500    ASN H 254       19.37     53.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    MSE B  85        -26.81
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 A 612        DISTANCE =  9.17 ANGSTROMS
REMARK 525    HOH B 455        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH D 406        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH H 408        DISTANCE = 12.05 ANGSTROMS
REMARK 525    HOH H 490        DISTANCE =  8.09 ANGSTROMS
REMARK 525    HOH H 684        DISTANCE = 10.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 302
DBREF  4L0C A    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C B    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C C    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C D    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C E    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C F    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C G    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
DBREF  4L0C H    1   255  UNP    F8G0M2   F8G0M2_PSEPU     1    255
SEQADV 4L0C ALA A   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA B   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA C   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA D   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA E   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA F   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA G   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQADV 4L0C ALA H   94  UNP  F8G0M2    SER    94 ENGINEERED MUTATION
SEQRES   1 A  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 A  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 A  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 A  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 A  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 A  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 A  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 A  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 A  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 A  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 A  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 A  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 A  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 A  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 A  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 A  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 A  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 A  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 A  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 A  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 B  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 B  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 B  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 B  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 B  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 B  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 B  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 B  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 B  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 B  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 B  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 B  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 B  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 B  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 B  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 B  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 B  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 B  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 B  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 B  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 C  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 C  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 C  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 C  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 C  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 C  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 C  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 C  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 C  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 C  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 C  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 C  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 C  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 C  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 C  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 C  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 C  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 C  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 C  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 C  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 D  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 D  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 D  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 D  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 D  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 D  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 D  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 D  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 D  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 D  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 D  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 D  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 D  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 D  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 D  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 D  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 D  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 D  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 D  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 D  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 E  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 E  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 E  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 E  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 E  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 E  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 E  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 E  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 E  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 E  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 E  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 E  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 E  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 E  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 E  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 E  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 E  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 E  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 E  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 E  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 F  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 F  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 F  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 F  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 F  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 F  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 F  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 F  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 F  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 F  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 F  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 F  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 F  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 F  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 F  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 F  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 F  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 F  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 F  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 F  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 G  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 G  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 G  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 G  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 G  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 G  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 G  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 G  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 G  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 G  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 G  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 G  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 G  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 G  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 G  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 G  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 G  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 G  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 G  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 G  255  PHE ILE THR ALA VAL SER ASN ARG
SEQRES   1 H  255  MSE LYS GLY TYR ASN VAL TYR ALA ASN GLY ILE ARG GLN
SEQRES   2 H  255  HIS ILE ILE HIS PHE PRO GLY THR GLY SER PRO LEU LEU
SEQRES   3 H  255  LEU ILE PRO GLY ILE THR SER PRO ALA VAL THR TRP GLY
SEQRES   4 H  255  PHE VAL ALA GLU ARG LEU ALA LYS TYR PHE ASP VAL HIS
SEQRES   5 H  255  VAL VAL ASP VAL ARG GLY ARG GLY LEU SER GLU SER GLY
SEQRES   6 H  255  ASP LEU ASP TYR SER LEU ASP ALA MSE ALA ASP ASP LEU
SEQRES   7 H  255  VAL ALA LEU ALA GLN ARG MSE GLU GLY VAL VAL VAL LEU
SEQRES   8 H  255  GLY HIS ALA MSE GLY ALA ARG ILE ALA ILE ARG ALA ALA
SEQRES   9 H  255  ARG LYS ASP SER GLN VAL PHE SER ARG LEU ILE LEU VAL
SEQRES  10 H  255  ASP PRO PRO VAL SER GLY PRO GLY ARG ARG PRO TYR PRO
SEQRES  11 H  255  ALA LYS TRP SER TRP TYR ALA GLU SER ILE ARG LEU ALA
SEQRES  12 H  255  GLN ARG GLY CYS THR ALA MSE GLU MSE ARG SER TYR CYS
SEQRES  13 H  255  PRO THR TRP THR ASP GLU GLN ILE GLU LEU ARG ALA GLU
SEQRES  14 H  255  TRP LEU HIS THR CYS GLN TYR THR ALA VAL LYS THR ALA
SEQRES  15 H  255  PHE ASP GLY PHE HIS THR ASP ASP ILE HIS THR ASP LEU
SEQRES  16 H  255  ALA GLN LEU THR LEU PRO ILE GLN LEU VAL VAL ALA GLY
SEQRES  17 H  255  GLY ALA GLU VAL ILE GLN PRO ASP ASP ILE ALA GLU ILE
SEQRES  18 H  255  ILE SER LEU ALA PRO GLN THR THR THR TYR VAL VAL GLU
SEQRES  19 H  255  GLU ALA GLY HIS MSE ILE PRO TRP ASP ASN LEU GLU GLY
SEQRES  20 H  255  PHE ILE THR ALA VAL SER ASN ARG
MODRES 4L0C MSE A    1  MET  SELENOMETHIONINE
MODRES 4L0C MSE A   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE A   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE A   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE A  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE A  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE A  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE B    1  MET  SELENOMETHIONINE
MODRES 4L0C MSE B   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE B   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE B   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE B  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE B  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE B  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE C    1  MET  SELENOMETHIONINE
MODRES 4L0C MSE C   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE C   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE C   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE C  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE C  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE C  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE D    1  MET  SELENOMETHIONINE
MODRES 4L0C MSE D   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE D   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE D   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE D  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE D  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE D  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE E    1  MET  SELENOMETHIONINE
MODRES 4L0C MSE E   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE E   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE E   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE E  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE E  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE E  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE F   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE F   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE F   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE F  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE F  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE F  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE G   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE G   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE G   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE G  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE G  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE G  239  MET  SELENOMETHIONINE
MODRES 4L0C MSE H   74  MET  SELENOMETHIONINE
MODRES 4L0C MSE H   85  MET  SELENOMETHIONINE
MODRES 4L0C MSE H   95  MET  SELENOMETHIONINE
MODRES 4L0C MSE H  150  MET  SELENOMETHIONINE
MODRES 4L0C MSE H  152  MET  SELENOMETHIONINE
MODRES 4L0C MSE H  239  MET  SELENOMETHIONINE
HET    MSE  A   1       8
HET    MSE  A  74       8
HET    MSE  A  85       5
HET    MSE  A  95       8
HET    MSE  A 150       8
HET    MSE  A 152       8
HET    MSE  A 239       8
HET    MSE  B   1      13
HET    MSE  B  74       8
HET    MSE  B  85       8
HET    MSE  B  95       8
HET    MSE  B 150       8
HET    MSE  B 152       8
HET    MSE  B 239       8
HET    MSE  C   1       8
HET    MSE  C  74       8
HET    MSE  C  85      13
HET    MSE  C  95       8
HET    MSE  C 150       8
HET    MSE  C 152       8
HET    MSE  C 239       8
HET    MSE  D   1       8
HET    MSE  D  74       8
HET    MSE  D  85       8
HET    MSE  D  95       8
HET    MSE  D 150       8
HET    MSE  D 152       8
HET    MSE  D 239       8
HET    MSE  E   1       8
HET    MSE  E  74       8
HET    MSE  E  85       8
HET    MSE  E  95       8
HET    MSE  E 150       8
HET    MSE  E 152       8
HET    MSE  E 239       8
HET    MSE  F  74       8
HET    MSE  F  85       8
HET    MSE  F  95       8
HET    MSE  F 150       8
HET    MSE  F 152       8
HET    MSE  F 239       8
HET    MSE  G  74       8
HET    MSE  G  85       8
HET    MSE  G  95       8
HET    MSE  G 150       8
HET    MSE  G 152       8
HET    MSE  G 239       8
HET    MSE  H  74       8
HET    MSE  H  85       8
HET    MSE  H  95       8
HET    MSE  H 150       8
HET    MSE  H 152       8
HET    MSE  H 239       8
HET    ACY  A 301       4
HET    ACY  A 302       4
HET    ACY  B 301       4
HET    ACY  C 301       4
HET    ACY  D 301       4
HET    ACY  E 301       4
HET    ACY  F 301       4
HET    ACY  G 301       4
HET    ACY  G 302       4
HET    ACY  H 301       4
HET    PEG  H 302       7
HETNAM     MSE SELENOMETHIONINE
HETNAM     ACY ACETIC ACID
HETNAM     PEG DI(HYDROXYETHYL)ETHER
FORMUL   1  MSE    53(C5 H11 N O2 SE)
FORMUL   9  ACY    10(C2 H4 O2)
FORMUL  19  PEG    C4 H10 O3
FORMUL  20  HOH   *2104(H2 O)
HELIX    1   1 PRO A   34  THR A   37  5                                   4
HELIX    2   2 TRP A   38  ALA A   46  1                                   9
HELIX    3   3 SER A   70  ARG A   84  1                                  15
HELIX    4   4 ALA A   94  ASP A  107  1                                  14
HELIX    5   5 LYS A  132  GLY A  146  1                                  15
HELIX    6   6 THR A  148  SER A  154  1                                   7
HELIX    7   7 THR A  160  LEU A  171  1                                  12
HELIX    8   8 HIS A  172  CYS A  174  5                                   3
HELIX    9   9 GLN A  175  ASP A  189  1                                  15
HELIX   10  10 ILE A  191  ALA A  196  1                                   6
HELIX   11  11 GLN A  214  ALA A  225  1                                  12
HELIX   12  12 MSE A  239  ASN A  244  1                                   6
HELIX   13  13 ASN A  244  SER A  253  1                                  10
HELIX   14  14 PRO B   34  THR B   37  5                                   4
HELIX   15  15 TRP B   38  ALA B   46  1                                   9
HELIX   16  16 SER B   70  GLN B   83  1                                  14
HELIX   17  17 ALA B   94  ASP B  107  1                                  14
HELIX   18  18 LYS B  132  GLY B  146  1                                  15
HELIX   19  19 THR B  148  SER B  154  1                                   7
HELIX   20  20 THR B  160  LEU B  171  1                                  12
HELIX   21  21 HIS B  172  CYS B  174  5                                   3
HELIX   22  22 GLN B  175  ASP B  189  1                                  15
HELIX   23  23 ILE B  191  ALA B  196  1                                   6
HELIX   24  24 GLN B  214  ALA B  225  1                                  12
HELIX   25  25 MSE B  239  ASN B  244  1                                   6
HELIX   26  26 ASN B  244  VAL B  252  1                                   9
HELIX   27  27 PRO C   34  THR C   37  5                                   4
HELIX   28  28 TRP C   38  ALA C   46  1                                   9
HELIX   29  29 SER C   70  GLN C   83  1                                  14
HELIX   30  30 ALA C   94  ASP C  107  1                                  14
HELIX   31  31 LYS C  132  GLY C  146  1                                  15
HELIX   32  32 THR C  148  SER C  154  1                                   7
HELIX   33  33 THR C  160  LEU C  171  1                                  12
HELIX   34  34 HIS C  172  CYS C  174  5                                   3
HELIX   35  35 GLN C  175  ASP C  189  1                                  15
HELIX   36  36 ILE C  191  ALA C  196  1                                   6
HELIX   37  37 GLN C  214  ALA C  225  1                                  12
HELIX   38  38 MSE C  239  ASN C  244  1                                   6
HELIX   39  39 ASN C  244  SER C  253  1                                  10
HELIX   40  40 PRO D   34  THR D   37  5                                   4
HELIX   41  41 TRP D   38  ALA D   46  1                                   9
HELIX   42  42 SER D   70  GLN D   83  1                                  14
HELIX   43  43 ALA D   94  ASP D  107  1                                  14
HELIX   44  44 LYS D  132  GLY D  146  1                                  15
HELIX   45  45 THR D  148  SER D  154  1                                   7
HELIX   46  46 THR D  160  LEU D  171  1                                  12
HELIX   47  47 HIS D  172  CYS D  174  5                                   3
HELIX   48  48 GLN D  175  ASP D  189  1                                  15
HELIX   49  49 ILE D  191  ALA D  196  1                                   6
HELIX   50  50 GLN D  214  ALA D  225  1                                  12
HELIX   51  51 MSE D  239  ASN D  244  1                                   6
HELIX   52  52 ASN D  244  SER D  253  1                                  10
HELIX   53  53 PRO E   34  THR E   37  5                                   4
HELIX   54  54 TRP E   38  ALA E   46  1                                   9
HELIX   55  55 SER E   70  GLN E   83  1                                  14
HELIX   56  56 ALA E   94  ASP E  107  1                                  14
HELIX   57  57 LYS E  132  GLY E  146  1                                  15
HELIX   58  58 THR E  148  SER E  154  1                                   7
HELIX   59  59 THR E  160  LEU E  171  1                                  12
HELIX   60  60 HIS E  172  CYS E  174  5                                   3
HELIX   61  61 GLN E  175  ASP E  189  1                                  15
HELIX   62  62 ILE E  191  ALA E  196  1                                   6
HELIX   63  63 GLN E  214  ALA E  225  1                                  12
HELIX   64  64 MSE E  239  ASN E  244  1                                   6
HELIX   65  65 ASN E  244  ASN E  254  1                                  11
HELIX   66  66 PRO F   34  THR F   37  5                                   4
HELIX   67  67 TRP F   38  ALA F   46  1                                   9
HELIX   68  68 SER F   70  GLN F   83  1                                  14
HELIX   69  69 ALA F   94  ASP F  107  1                                  14
HELIX   70  70 LYS F  132  GLY F  146  1                                  15
HELIX   71  71 THR F  148  SER F  154  1                                   7
HELIX   72  72 THR F  160  LEU F  171  1                                  12
HELIX   73  73 HIS F  172  CYS F  174  5                                   3
HELIX   74  74 GLN F  175  ASP F  189  1                                  15
HELIX   75  75 ILE F  191  ALA F  196  1                                   6
HELIX   76  76 GLN F  214  ALA F  225  1                                  12
HELIX   77  77 MSE F  239  ASN F  244  1                                   6
HELIX   78  78 ASN F  244  SER F  253  1                                  10
HELIX   79  79 PRO G   34  THR G   37  5                                   4
HELIX   80  80 TRP G   38  ALA G   46  1                                   9
HELIX   81  81 SER G   70  GLN G   83  1                                  14
HELIX   82  82 ALA G   94  ASP G  107  1                                  14
HELIX   83  83 LYS G  132  GLY G  146  1                                  15
HELIX   84  84 THR G  148  SER G  154  1                                   7
HELIX   85  85 THR G  160  LEU G  171  1                                  12
HELIX   86  86 HIS G  172  CYS G  174  5                                   3
HELIX   87  87 GLN G  175  ASP G  189  1                                  15
HELIX   88  88 ILE G  191  ALA G  196  1                                   6
HELIX   89  89 GLN G  214  ALA G  225  1                                  12
HELIX   90  90 MSE G  239  ASN G  244  1                                   6
HELIX   91  91 ASN G  244  SER G  253  1                                  10
HELIX   92  92 PRO H   34  THR H   37  5                                   4
HELIX   93  93 TRP H   38  ALA H   46  1                                   9
HELIX   94  94 SER H   70  GLN H   83  1                                  14
HELIX   95  95 ALA H   94  ASP H  107  1                                  14
HELIX   96  96 LYS H  132  GLY H  146  1                                  15
HELIX   97  97 THR H  148  SER H  154  1                                   7
HELIX   98  98 THR H  160  LEU H  171  1                                  12
HELIX   99  99 HIS H  172  CYS H  174  5                                   3
HELIX  100 100 GLN H  175  ASP H  189  1                                  15
HELIX  101 101 ILE H  191  ALA H  196  1                                   6
HELIX  102 102 GLN H  214  ALA H  225  1                                  12
HELIX  103 103 MSE H  239  ASN H  244  1                                   6
HELIX  104 104 ASN H  244  ASN H  254  1                                  11
SHEET    1   A 8 LYS A   2  ALA A   8  0
SHEET    2   A 8 ILE A  11  PHE A  18 -1  O  HIS A  17   N  LYS A   2
SHEET    3   A 8 ASP A  50  VAL A  54 -1  O  VAL A  51   N  PHE A  18
SHEET    4   A 8 PRO A  24  ILE A  28  1  N  LEU A  27   O  VAL A  54
SHEET    5   A 8 VAL A  88  HIS A  93  1  O  HIS A  93   N  ILE A  28
SHEET    6   A 8 PHE A 111  VAL A 117  1  O  VAL A 117   N  GLY A  92
SHEET    7   A 8 ILE A 202  ALA A 207  1  O  GLN A 203   N  LEU A 116
SHEET    8   A 8 THR A 229  VAL A 233  1  O  THR A 229   N  LEU A 204
SHEET    1   B 8 LYS B   2  ALA B   8  0
SHEET    2   B 8 ILE B  11  PHE B  18 -1  O  GLN B  13   N  VAL B   6
SHEET    3   B 8 PHE B  49  VAL B  54 -1  O  VAL B  51   N  PHE B  18
SHEET    4   B 8 SER B  23  ILE B  28  1  N  LEU B  27   O  VAL B  54
SHEET    5   B 8 VAL B  88  HIS B  93  1  O  HIS B  93   N  ILE B  28
SHEET    6   B 8 PHE B 111  VAL B 117  1  O  VAL B 117   N  GLY B  92
SHEET    7   B 8 ILE B 202  ALA B 207  1  O  VAL B 205   N  LEU B 116
SHEET    8   B 8 THR B 229  VAL B 233  1  O  THR B 229   N  LEU B 204
SHEET    1   C 8 LYS C   2  ALA C   8  0
SHEET    2   C 8 ILE C  11  PHE C  18 -1  O  GLN C  13   N  VAL C   6
SHEET    3   C 8 ASP C  50  VAL C  54 -1  O  VAL C  51   N  PHE C  18
SHEET    4   C 8 PRO C  24  ILE C  28  1  N  LEU C  25   O  HIS C  52
SHEET    5   C 8 VAL C  88  HIS C  93  1  O  HIS C  93   N  ILE C  28
SHEET    6   C 8 PHE C 111  VAL C 117  1  O  VAL C 117   N  GLY C  92
SHEET    7   C 8 ILE C 202  ALA C 207  1  O  GLN C 203   N  LEU C 116
SHEET    8   C 8 THR C 229  VAL C 233  1  O  THR C 229   N  LEU C 204
SHEET    1   D 8 LYS D   2  ALA D   8  0
SHEET    2   D 8 ILE D  11  PHE D  18 -1  O  ILE D  15   N  TYR D   4
SHEET    3   D 8 PHE D  49  VAL D  54 -1  O  VAL D  51   N  PHE D  18
SHEET    4   D 8 SER D  23  ILE D  28  1  N  LEU D  25   O  ASP D  50
SHEET    5   D 8 VAL D  88  HIS D  93  1  O  HIS D  93   N  ILE D  28
SHEET    6   D 8 PHE D 111  VAL D 117  1  O  VAL D 117   N  GLY D  92
SHEET    7   D 8 ILE D 202  ALA D 207  1  O  VAL D 205   N  LEU D 116
SHEET    8   D 8 THR D 229  VAL D 233  1  O  THR D 229   N  LEU D 204
SHEET    1   E 8 LYS E   2  ALA E   8  0
SHEET    2   E 8 ILE E  11  PHE E  18 -1  O  ILE E  15   N  TYR E   4
SHEET    3   E 8 ASP E  50  VAL E  54 -1  O  VAL E  51   N  PHE E  18
SHEET    4   E 8 PRO E  24  ILE E  28  1  N  LEU E  25   O  HIS E  52
SHEET    5   E 8 VAL E  88  HIS E  93  1  O  HIS E  93   N  ILE E  28
SHEET    6   E 8 PHE E 111  VAL E 117  1  O  VAL E 117   N  GLY E  92
SHEET    7   E 8 ILE E 202  ALA E 207  1  O  VAL E 205   N  LEU E 116
SHEET    8   E 8 THR E 229  VAL E 233  1  O  THR E 229   N  LEU E 204
SHEET    1   F 8 GLY F   3  ALA F   8  0
SHEET    2   F 8 ILE F  11  PHE F  18 -1  O  GLN F  13   N  VAL F   6
SHEET    3   F 8 ASP F  50  VAL F  54 -1  O  VAL F  51   N  PHE F  18
SHEET    4   F 8 PRO F  24  ILE F  28  1  N  LEU F  25   O  HIS F  52
SHEET    5   F 8 VAL F  88  HIS F  93  1  O  VAL F  89   N  LEU F  26
SHEET    6   F 8 PHE F 111  VAL F 117  1  O  VAL F 117   N  GLY F  92
SHEET    7   F 8 ILE F 202  ALA F 207  1  O  GLN F 203   N  LEU F 116
SHEET    8   F 8 THR F 229  VAL F 233  1  O  VAL F 233   N  VAL F 206
SHEET    1   G 8 GLY G   3  ALA G   8  0
SHEET    2   G 8 ILE G  11  PHE G  18 -1  O  ILE G  15   N  TYR G   4
SHEET    3   G 8 ASP G  50  VAL G  54 -1  O  VAL G  51   N  PHE G  18
SHEET    4   G 8 PRO G  24  ILE G  28  1  N  LEU G  25   O  HIS G  52
SHEET    5   G 8 VAL G  88  HIS G  93  1  O  LEU G  91   N  ILE G  28
SHEET    6   G 8 PHE G 111  VAL G 117  1  O  VAL G 117   N  GLY G  92
SHEET    7   G 8 ILE G 202  ALA G 207  1  O  GLN G 203   N  LEU G 116
SHEET    8   G 8 THR G 229  VAL G 233  1  O  THR G 229   N  LEU G 204
SHEET    1   H 8 GLY H   3  ALA H   8  0
SHEET    2   H 8 ILE H  11  PHE H  18 -1  O  GLN H  13   N  VAL H   6
SHEET    3   H 8 ASP H  50  VAL H  54 -1  O  VAL H  51   N  PHE H  18
SHEET    4   H 8 PRO H  24  ILE H  28  1  N  LEU H  25   O  HIS H  52
SHEET    5   H 8 VAL H  88  HIS H  93  1  O  HIS H  93   N  ILE H  28
SHEET    6   H 8 PHE H 111  VAL H 117  1  O  ILE H 115   N  VAL H  90
SHEET    7   H 8 ILE H 202  ALA H 207  1  O  VAL H 205   N  LEU H 116
SHEET    8   H 8 THR H 229  VAL H 233  1  O  THR H 229   N  LEU H 204
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.33
LINK         C   ALA A  73                 N   MSE A  74     1555   1555  1.33
LINK         C   MSE A  74                 N   ALA A  75     1555   1555  1.33
LINK         C   ARG A  84                 N   MSE A  85     1555   1555  1.31
LINK         C   MSE A  85                 N   GLU A  86     1555   1555  1.32
LINK         C   ALA A  94                 N   MSE A  95     1555   1555  1.34
LINK         C   MSE A  95                 N   GLY A  96     1555   1555  1.34
LINK         C   ALA A 149                 N   MSE A 150     1555   1555  1.33
LINK         C   MSE A 150                 N   GLU A 151     1555   1555  1.34
LINK         C   GLU A 151                 N   MSE A 152     1555   1555  1.33
LINK         C   MSE A 152                 N   ARG A 153     1555   1555  1.33
LINK         C   HIS A 238                 N   MSE A 239     1555   1555  1.33
LINK         C   MSE A 239                 N   ILE A 240     1555   1555  1.34
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.34
LINK         C   ALA B  73                 N   MSE B  74     1555   1555  1.33
LINK         C   MSE B  74                 N   ALA B  75     1555   1555  1.33
LINK         C   ARG B  84                 N   MSE B  85     1555   1555  1.22
LINK         C   MSE B  85                 N   GLU B  86     1555   1555  1.29
LINK         C   ALA B  94                 N   MSE B  95     1555   1555  1.34
LINK         C   MSE B  95                 N   GLY B  96     1555   1555  1.34
LINK         C   ALA B 149                 N   MSE B 150     1555   1555  1.34
LINK         C   MSE B 150                 N   GLU B 151     1555   1555  1.34
LINK         C   GLU B 151                 N   MSE B 152     1555   1555  1.33
LINK         C   MSE B 152                 N   ARG B 153     1555   1555  1.33
LINK         C   HIS B 238                 N   MSE B 239     1555   1555  1.34
LINK         C   MSE B 239                 N   ILE B 240     1555   1555  1.34
LINK         C   MSE C   1                 N   LYS C   2     1555   1555  1.33
LINK         C   ALA C  73                 N   MSE C  74     1555   1555  1.34
LINK         C   MSE C  74                 N   ALA C  75     1555   1555  1.34
LINK         C   ARG C  84                 N   MSE C  85     1555   1555  1.33
LINK         C   MSE C  85                 N   GLU C  86     1555   1555  1.32
LINK         C   ALA C  94                 N   MSE C  95     1555   1555  1.34
LINK         C   MSE C  95                 N   GLY C  96     1555   1555  1.34
LINK         C   ALA C 149                 N   MSE C 150     1555   1555  1.34
LINK         C   MSE C 150                 N   GLU C 151     1555   1555  1.33
LINK         C   GLU C 151                 N   MSE C 152     1555   1555  1.33
LINK         C   MSE C 152                 N   ARG C 153     1555   1555  1.33
LINK         C   HIS C 238                 N   MSE C 239     1555   1555  1.33
LINK         C   MSE C 239                 N   ILE C 240     1555   1555  1.33
LINK         C   MSE D   1                 N   LYS D   2     1555   1555  1.33
LINK         C   ALA D  73                 N   MSE D  74     1555   1555  1.34
LINK         C   MSE D  74                 N   ALA D  75     1555   1555  1.33
LINK         C   ARG D  84                 N   MSE D  85     1555   1555  1.33
LINK         C   MSE D  85                 N   GLU D  86     1555   1555  1.33
LINK         C   ALA D  94                 N   MSE D  95     1555   1555  1.33
LINK         C   MSE D  95                 N   GLY D  96     1555   1555  1.34
LINK         C   ALA D 149                 N   MSE D 150     1555   1555  1.33
LINK         C   MSE D 150                 N   GLU D 151     1555   1555  1.34
LINK         C   GLU D 151                 N   MSE D 152     1555   1555  1.33
LINK         C   MSE D 152                 N   ARG D 153     1555   1555  1.33
LINK         C   HIS D 238                 N   MSE D 239     1555   1555  1.33
LINK         C   MSE D 239                 N   ILE D 240     1555   1555  1.34
LINK         C   MSE E   1                 N   LYS E   2     1555   1555  1.33
LINK         C   ALA E  73                 N   MSE E  74     1555   1555  1.33
LINK         C   MSE E  74                 N   ALA E  75     1555   1555  1.21
LINK         C   ARG E  84                 N   MSE E  85     1555   1555  1.33
LINK         C   MSE E  85                 N   GLU E  86     1555   1555  1.33
LINK         C   ALA E  94                 N   MSE E  95     1555   1555  1.34
LINK         C   MSE E  95                 N   GLY E  96     1555   1555  1.34
LINK         C   ALA E 149                 N   MSE E 150     1555   1555  1.33
LINK         C   MSE E 150                 N   GLU E 151     1555   1555  1.33
LINK         C   GLU E 151                 N   MSE E 152     1555   1555  1.34
LINK         C   MSE E 152                 N   ARG E 153     1555   1555  1.33
LINK         C   HIS E 238                 N   MSE E 239     1555   1555  1.27
LINK         C   MSE E 239                 N   ILE E 240     1555   1555  1.34
LINK         C   ALA F  73                 N   MSE F  74     1555   1555  1.34
LINK         C   MSE F  74                 N   ALA F  75     1555   1555  1.33
LINK         C   ARG F  84                 N   MSE F  85     1555   1555  1.34
LINK         C   MSE F  85                 N   GLU F  86     1555   1555  1.33
LINK         C   ALA F  94                 N   MSE F  95     1555   1555  1.34
LINK         C   MSE F  95                 N   GLY F  96     1555   1555  1.33
LINK         C   ALA F 149                 N   MSE F 150     1555   1555  1.33
LINK         C   MSE F 150                 N   GLU F 151     1555   1555  1.34
LINK         C   GLU F 151                 N   MSE F 152     1555   1555  1.33
LINK         C   MSE F 152                 N   ARG F 153     1555   1555  1.33
LINK         C   HIS F 238                 N   MSE F 239     1555   1555  1.33
LINK         C   MSE F 239                 N   ILE F 240     1555   1555  1.33
LINK         C   ALA G  73                 N   MSE G  74     1555   1555  1.34
LINK         C   MSE G  74                 N   ALA G  75     1555   1555  1.35
LINK         C   ARG G  84                 N   MSE G  85     1555   1555  1.34
LINK         C   MSE G  85                 N   GLU G  86     1555   1555  1.33
LINK         C   ALA G  94                 N   MSE G  95     1555   1555  1.33
LINK         C   MSE G  95                 N   GLY G  96     1555   1555  1.33
LINK         C   ALA G 149                 N   MSE G 150     1555   1555  1.33
LINK         C   MSE G 150                 N   GLU G 151     1555   1555  1.33
LINK         C   GLU G 151                 N   MSE G 152     1555   1555  1.33
LINK         C   MSE G 152                 N   ARG G 153     1555   1555  1.33
LINK         C   HIS G 238                 N   MSE G 239     1555   1555  1.33
LINK         C   MSE G 239                 N   ILE G 240     1555   1555  1.33
LINK         C   ALA H  73                 N   MSE H  74     1555   1555  1.34
LINK         C   MSE H  74                 N   ALA H  75     1555   1555  1.33
LINK         C   ARG H  84                 N   MSE H  85     1555   1555  1.33
LINK         C   MSE H  85                 N   GLU H  86     1555   1555  1.33
LINK         C   ALA H  94                 N   MSE H  95     1555   1555  1.34
LINK         C   MSE H  95                 N   GLY H  96     1555   1555  1.33
LINK         C   ALA H 149                 N   MSE H 150     1555   1555  1.34
LINK         C   MSE H 150                 N   GLU H 151     1555   1555  1.33
LINK         C   GLU H 151                 N   MSE H 152     1555   1555  1.34
LINK         C   MSE H 152                 N   ARG H 153     1555   1555  1.33
LINK         C   HIS H 238                 N   MSE H 239     1555   1555  1.33
LINK         C   MSE H 239                 N   ILE H 240     1555   1555  1.34
SITE     1 AC1  5 GLY A  30  THR A  32  SER A  33  MSE A 239
SITE     2 AC1  5 HOH A 682
SITE     1 AC2  4 ARG A  12  GLU A  63  SER A  64  HOH A 575
SITE     1 AC3  5 GLY B  30  THR B  32  SER B  33  MSE B 239
SITE     2 AC3  5 HOH B 651
SITE     1 AC4  5 GLY C  30  THR C  32  SER C  33  MSE C 239
SITE     2 AC4  5 HOH C 409
SITE     1 AC5  4 THR D  32  SER D  33  MSE D 239  HOH D 465
SITE     1 AC6  5 GLY E  30  THR E  32  SER E  33  MSE E 239
SITE     2 AC6  5 HOH E 436
SITE     1 AC7  5 GLY F  30  THR F  32  SER F  33  MSE F 239
SITE     2 AC7  5 HOH F 599
SITE     1 AC8  5 GLY G  30  THR G  32  SER G  33  MSE G 239
SITE     2 AC8  5 HOH G 465
SITE     1 AC9  5 ARG D 153  HOH D 544  SER G  23  VAL G  89
SITE     2 AC9  5 ARG G 113
SITE     1 BC1  5 GLY H  30  THR H  32  SER H  33  MSE H 239
SITE     2 BC1  5 HOH H 688
SITE     1 BC2  2 ALA H 131  LYS H 132
CRYST1   89.412   87.268  130.879  90.00  94.42  90.00 P 1 21 1     16
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      0.011184  0.000000  0.000865        0.00000
SCALE2      0.000000  0.011459  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007663        0.00000
TER    1997      ARG A 255
TER    4021      ARG B 255
TER    5992      SER C 253
TER    7976      SER D 253
TER    9968      ARG E 255
TER   11929      ASN F 254
TER   13884      SER G 253
TER   15881      ARG H 255
MASTER      460    0   64  104   64    0   19    617879    8  579  160
END