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HEADER HYDROLASE 30-SEP-99 1C4X
TITLE 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE (BPHD)
TITLE 2 FROM RHODOCOCCUS SP. STRAIN RHA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: BPHD;
COMPND 6 EC: 3.7.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 BIOLOGICAL_UNIT: OCTAMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 STRAIN: RHA1;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS HYDROLASE, PCB DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NANDHAGOPAL,T.SENDA,Y.MITSUI
REVDAT 1 01-OCT-99 1C4X 0
JRNL AUTH N.NANDHAGOPAL,T.SENDA,T.HATTA,A.YAMADA,E.MASAI,
JRNL AUTH 2 M.FUKUDA,Y.MITSUI
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF MICROBIAL
JRNL TITL 2 2-HYDROXYL-6-OXO-6-PHENYLHEXA-2,4- DIENOIC ACID
JRNL TITL 3 (HPDA) HYDROLASE (BPHD ENZYME) FROM RHODOCOCCUS
JRNL TITL 4 SP. STRAIN RHA1, IN THE PCB DEGRADATION PATHWAY
JRNL REF PROC.JPN.ACAD.,SER.B V. 73 154 1997
JRNL REFN ASTM PJABDW JA ISSN 0386-2208 0535
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.4
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 15274
REMARK 3
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 SET) : 0.178
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1508
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1290
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2200
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 32
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C4X COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-1999.
REMARK 100 THE RCSB ID CODE IS RCSB001310.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : RAXIS II
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : PROCESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.06300
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: MIR
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1/2-X,1/2-Y,1/2+Z
REMARK 290 11555 1/2-Y,1/2+X,1/2+Z
REMARK 290 12555 1/2+Y,1/2-X,1/2+Z
REMARK 290 13555 1/2-X,1/2+Y,1/2-Z
REMARK 290 14555 1/2+X,1/2-Y,1/2-Z
REMARK 290 15555 1/2+Y,1/2+X,1/2-Z
REMARK 290 16555 1/2-Y,1/2-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 55.40000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 68.20000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 55.40000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 68.20000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 55.40000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 68.20000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 55.40000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 68.20000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 55.40000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 68.20000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 55.40000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 68.20000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 55.40000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 68.20000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 55.40000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 55.40000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 68.20000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 110.80000
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 110.80000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 110.80000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 110.80000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 110.80000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 136.40000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 110.80000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 136.40000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 136.40000
REMARK 350
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 7 0.000000 -1.000000 0.000000 110.80000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 110.80000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 136.40000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 LYS A 2
REMARK 465 ALA A 284
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 4*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 LEU A 16 N - CA - C ANGL. DEV. = -5.1 DEGREES
REMARK 500 HIS A 19 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 LEU A 21 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 LEU A 33 CA - CB - CG ANGL. DEV. = 5.1 DEGREES
REMARK 500 ALA A 44 N - CA - C ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP A 47 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 48 N - CA - C ANGL. DEV. = 4.8 DEGREES
REMARK 500 PRO A 49 N - CA - C ANGL. DEV. = 5.5 DEGREES
REMARK 500 PHE A 59 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 ASP A 64 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 GLY A 69 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 HIS A 105 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLU A 125 N - CA - C ANGL. DEV. = 5.0 DEGREES
REMARK 500 VAL A 136 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 156 N - CA - C ANGL. DEV. = -6.1 DEGREES
REMARK 500 PRO A 157 N - CA - C ANGL. DEV. = 4.9 DEGREES
REMARK 500 LYS A 207 N - CA - C ANGL. DEV. = -5.1 DEGREES
REMARK 500 HIS A 225 N - CA - C ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 226 N - CA - C ANGL. DEV. = -5.2 DEGREES
REMARK 500 LEU A 228 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 HIS A 249 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLU A 254 N - CA - C ANGL. DEV. = -5.9 DEGREES
REMARK 500 VAL A 256 N - CA - C ANGL. DEV. = -5.7 DEGREES
REMARK 500 GLU A 268 N - CA - C ANGL. DEV. = 5.5 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 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
REMARK 500 SER A 110 60.37 -113.15
DBREF 1C4X A 1 285 GB D78322 D78322 1 285
SEQRES 1 A 285 MET ALA LYS THR VAL GLU ILE ILE GLU LYS ARG PHE PRO
SEQRES 2 A 285 SER GLY THR LEU ALA SER HIS ALA LEU VAL ALA GLY ASP
SEQRES 3 A 285 PRO GLN SER PRO ALA VAL VAL LEU LEU HIS GLY ALA GLY
SEQRES 4 A 285 PRO GLY ALA HIS ALA ALA SER ASN TRP ARG PRO ILE ILE
SEQRES 5 A 285 PRO ASP LEU ALA GLU ASN PHE PHE VAL VAL ALA PRO ASP
SEQRES 6 A 285 LEU ILE GLY PHE GLY GLN SER GLU TYR PRO GLU THR TYR
SEQRES 7 A 285 PRO GLY HIS ILE MET SER TRP VAL GLY MET ARG VAL GLU
SEQRES 8 A 285 GLN ILE LEU GLY LEU MET ASN HIS PHE GLY ILE GLU LYS
SEQRES 9 A 285 SER HIS ILE VAL GLY ASN SER MET GLY GLY ALA VAL THR
SEQRES 10 A 285 LEU GLN LEU VAL VAL GLU ALA PRO GLU ARG PHE ASP LYS
SEQRES 11 A 285 VAL ALA LEU MET GLY SER VAL GLY ALA PRO MET ASN ALA
SEQRES 12 A 285 ARG PRO PRO GLU LEU ALA ARG LEU LEU ALA PHE TYR ALA
SEQRES 13 A 285 ASP PRO ARG LEU THR PRO TYR ARG GLU LEU ILE HIS SER
SEQRES 14 A 285 PHE VAL TYR ASP PRO GLU ASN PHE PRO GLY MET GLU GLU
SEQRES 15 A 285 ILE VAL LYS SER ARG PHE GLU VAL ALA ASN ASP PRO GLU
SEQRES 16 A 285 VAL ARG ARG ILE GLN GLU VAL MET PHE GLU SER MET LYS
SEQRES 17 A 285 ALA GLY MET GLU SER LEU VAL ILE PRO PRO ALA THR LEU
SEQRES 18 A 285 GLY ARG LEU PRO HIS ASP VAL LEU VAL PHE HIS GLY ARG
SEQRES 19 A 285 GLN ASP ARG ILE VAL PRO LEU ASP THR SER LEU TYR LEU
SEQRES 20 A 285 THR LYS HIS LEU LYS HIS ALA GLU LEU VAL VAL LEU ASP
SEQRES 21 A 285 ARG CYS GLY HIS TRP ALA GLN LEU GLU ARG TRP ASP ALA
SEQRES 22 A 285 MET GLY PRO MET LEU MET GLU HIS PHE ARG ALA ALA
FORMUL 2 HOH *32(H2 O1)
HELIX 1 1 HIS A 42 ARG A 48 1 7
HELIX 2 2 ILE A 50 GLU A 56 1 7
HELIX 3 3 HIS A 80 GLY A 100 1 21
HELIX 4 4 SER A 110 ALA A 123 1 14
HELIX 5 5 PRO A 144 ALA A 152 1 9
HELIX 6 6 PHE A 153 ASP A 156 5 4
HELIX 7 7 ARG A 158 SER A 168 1 11
HELIX 8 8 GLY A 178 ASP A 192 1 15
HELIX 9 9 ASP A 192 LYS A 207 1 16
HELIX 10 10 MET A 210 VAL A 214 5 5
HELIX 11 11 PRO A 216 GLY A 221 1 6
HELIX 12 12 LEU A 240 LEU A 250 1 11
HELIX 13 13 TRP A 264 ARG A 269 1 6
HELIX 14 14 ARG A 269 ALA A 283 1 15
SHEET 1 A 8 ILE A 7 PHE A 11 0
SHEET 2 A 8 SER A 18 ALA A 23 -1 N SER A 18 O PHE A 11
SHEET 3 A 8 PHE A 59 PRO A 63 -1 N VAL A 60 O ALA A 23
SHEET 4 A 8 ALA A 30 LEU A 34 1 O VAL A 31 N VAL A 61
SHEET 5 A 8 SER A 104 ASN A 109 1 N HIS A 105 O ALA A 30
SHEET 6 A 8 PHE A 127 MET A 133 1 N ASP A 128 O SER A 104
SHEET 7 A 8 VAL A 227 GLY A 232 1 O LEU A 228 N LEU A 132
SHEET 8 A 8 ALA A 253 LEU A 258 1 O GLU A 254 N VAL A 229
CRYST1 110.800 110.800 136.400 90.00 90.00 90.00 I 4 2 2 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 0.009025 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009025 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007331 0.00000
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