HEADER LYASE 20-JUN-01 1JF9
TITLE CRYSTAL STRUCTURE OF SELENOCYSTEINE LYASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SELENOCYSTEINE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NIFS/CDSB, SELENOCYSTEINE REDUCTASE, SELENOCYSTEINE BETA-
COMPND 5 LYASE, SCL;
COMPND 6 EC: 4.4.1.16;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: NIFS/CSDB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 PROMOTER;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS NIFS, SELENOCYSTEINE, CYSTEINE, PURSULFIDE, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, NYSGXRC, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.LIMA,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (NYSGXRC)
REVDAT 7 03-FEB-21 1JF9 1 AUTHOR REMARK SEQADV LINK
REVDAT 6 21-JAN-15 1JF9 1 REMARK
REVDAT 5 13-JUL-11 1JF9 1 VERSN
REVDAT 4 24-FEB-09 1JF9 1 VERSN
REVDAT 3 25-JAN-05 1JF9 1 AUTHOR KEYWDS REMARK
REVDAT 2 13-MAR-02 1JF9 1 JRNL
REVDAT 1 04-JUL-01 1JF9 0
JRNL AUTH C.D.LIMA
JRNL TITL ANALYSIS OF THE E. COLI NIFS CSDB PROTEIN AT 2.0A REVEALS
JRNL TITL 2 THE STRUCTURAL BASIS FOR PERSELENIDE AND PERSULFIDE
JRNL TITL 3 INTERMEDIATE FORMATION
JRNL REF J.MOL.BIOL. V. 315 1199 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11827487
JRNL DOI 10.1006/JMBI.2001.5308
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 63941
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 3409
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3119
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 579
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.27
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.26700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4M NACL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 66.78900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.18750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.18750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 100.18350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.18750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.18750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.39450
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.18750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.18750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.18350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.18750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.18750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.39450
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 66.78900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
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 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 -1
REMARK 465 SER A 0
REMARK 465 MET A 1
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 A 845 O HOH A 883 2.09
REMARK 500 O HOH A 628 O HOH A 919 2.10
REMARK 500 OE2 GLU A 250 O HOH A 869 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 869 O HOH A 869 7555 1.33
REMARK 500 O HOH A 512 O HOH A 512 7555 1.45
REMARK 500 O HOH A 655 O HOH A 655 7555 2.09
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 A 17 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP A 41 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TYR A 51 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 GLU A 250 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ALA A 270 CA - C - O ANGL. DEV. = -16.9 DEGREES
REMARK 500 ARG A 273 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 359 NH1 - CZ - NH2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 359 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 359 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG A 379 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 400 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 400 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 403 NE - CZ - NH2 ANGL. DEV. = -4.8 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 HIS A 55 60.51 -102.57
REMARK 500 ILE A 127 -58.14 -131.24
REMARK 500 LEU A 227 40.77 -101.28
REMARK 500 TRP A 249 -78.87 -105.95
REMARK 500 SER A 254 -23.41 76.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 270 PRO A 271 -45.44
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 ALA A 270 -24.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T129 RELATED DB: TARGETDB
DBREF 1JF9 A 1 406 UNP P77444 SUFS_ECOLI 1 406
SEQADV 1JF9 GLY A -1 UNP P77444 EXPRESSION TAG
SEQADV 1JF9 SER A 0 UNP P77444 EXPRESSION TAG
SEQRES 1 A 408 GLY SER MET ILE PHE SER VAL ASP LYS VAL ARG ALA ASP
SEQRES 2 A 408 PHE PRO VAL LEU SER ARG GLU VAL ASN GLY LEU PRO LEU
SEQRES 3 A 408 ALA TYR LEU ASP SER ALA ALA SER ALA GLN LYS PRO SER
SEQRES 4 A 408 GLN VAL ILE ASP ALA GLU ALA GLU PHE TYR ARG HIS GLY
SEQRES 5 A 408 TYR ALA ALA VAL HIS ARG GLY ILE HIS THR LEU SER ALA
SEQRES 6 A 408 GLN ALA THR GLU LYS MET GLU ASN VAL ARG LYS ARG ALA
SEQRES 7 A 408 SER LEU PHE ILE ASN ALA ARG SER ALA GLU GLU LEU VAL
SEQRES 8 A 408 PHE VAL ARG GLY THR THR GLU GLY ILE ASN LEU VAL ALA
SEQRES 9 A 408 ASN SER TRP GLY ASN SER ASN VAL ARG ALA GLY ASP ASN
SEQRES 10 A 408 ILE ILE ILE SER GLN MET GLU HIS HIS ALA ASN ILE VAL
SEQRES 11 A 408 PRO TRP GLN MET LEU CYS ALA ARG VAL GLY ALA GLU LEU
SEQRES 12 A 408 ARG VAL ILE PRO LEU ASN PRO ASP GLY THR LEU GLN LEU
SEQRES 13 A 408 GLU THR LEU PRO THR LEU PHE ASP GLU LYS THR ARG LEU
SEQRES 14 A 408 LEU ALA ILE THR HIS VAL SER ASN VAL LEU GLY THR GLU
SEQRES 15 A 408 ASN PRO LEU ALA GLU MET ILE THR LEU ALA HIS GLN HIS
SEQRES 16 A 408 GLY ALA LYS VAL LEU VAL ASP GLY ALA GLN ALA VAL MET
SEQRES 17 A 408 HIS HIS PRO VAL ASP VAL GLN ALA LEU ASP CYS ASP PHE
SEQRES 18 A 408 TYR VAL PHE SER GLY HIS LYS LEU TYR GLY PRO THR GLY
SEQRES 19 A 408 ILE GLY ILE LEU TYR VAL LYS GLU ALA LEU LEU GLN GLU
SEQRES 20 A 408 MET PRO PRO TRP GLU GLY GLY GLY SER MET ILE ALA THR
SEQRES 21 A 408 VAL SER LEU SER GLU GLY THR THR TRP THR LYS ALA PRO
SEQRES 22 A 408 TRP ARG PHE GLU ALA GLY THR PRO ASN THR GLY GLY ILE
SEQRES 23 A 408 ILE GLY LEU GLY ALA ALA LEU GLU TYR VAL SER ALA LEU
SEQRES 24 A 408 GLY LEU ASN ASN ILE ALA GLU TYR GLU GLN ASN LEU MET
SEQRES 25 A 408 HIS TYR ALA LEU SER GLN LEU GLU SER VAL PRO ASP LEU
SEQRES 26 A 408 THR LEU TYR GLY PRO GLN ASN ARG LEU GLY VAL ILE ALA
SEQRES 27 A 408 PHE ASN LEU GLY LYS HIS HIS ALA TYR ASP VAL GLY SER
SEQRES 28 A 408 PHE LEU ASP ASN TYR GLY ILE ALA VAL ARG THR GLY HIS
SEQRES 29 A 408 HIS CYS ALA MET PRO LEU MET ALA TYR TYR ASN VAL PRO
SEQRES 30 A 408 ALA MET CYS ARG ALA SER LEU ALA MET TYR ASN THR HIS
SEQRES 31 A 408 GLU GLU VAL ASP ARG LEU VAL THR GLY LEU GLN ARG ILE
SEQRES 32 A 408 HIS ARG LEU LEU GLY
HET PLP A 500 15
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 HOH *579(H2 O)
HELIX 1 1 SER A 4 ASP A 11 1 8
HELIX 2 2 PHE A 12 SER A 16 5 5
HELIX 3 3 PRO A 36 GLY A 50 1 15
HELIX 4 4 HIS A 59 ILE A 80 1 22
HELIX 5 5 SER A 84 GLU A 86 5 3
HELIX 6 6 GLY A 93 VAL A 110 1 18
HELIX 7 7 HIS A 123 ASN A 126 5 4
HELIX 8 8 ILE A 127 GLY A 138 1 12
HELIX 9 9 GLN A 153 GLU A 155 5 3
HELIX 10 10 THR A 156 PHE A 161 1 6
HELIX 11 11 PRO A 182 HIS A 193 1 12
HELIX 12 12 ASP A 211 ASP A 216 1 6
HELIX 13 13 HIS A 225 LEU A 227 5 3
HELIX 14 14 LYS A 239 GLN A 244 1 6
HELIX 15 15 PRO A 271 GLU A 275 5 5
HELIX 16 16 ASN A 280 GLY A 298 1 19
HELIX 17 17 GLY A 298 GLU A 318 1 21
HELIX 18 18 HIS A 343 TYR A 354 1 12
HELIX 19 19 ALA A 365 TYR A 372 1 8
HELIX 20 20 THR A 387 GLY A 406 1 20
SHEET 1 A 2 GLU A 18 VAL A 19 0
SHEET 2 A 2 LEU A 22 PRO A 23 -1 O LEU A 22 N VAL A 19
SHEET 1 B 2 ALA A 25 TYR A 26 0
SHEET 2 B 2 ILE A 356 ALA A 357 1 N ALA A 357 O ALA A 25
SHEET 1 C 7 LEU A 88 VAL A 91 0
SHEET 2 C 7 GLY A 234 VAL A 238 -1 N GLY A 234 O VAL A 91
SHEET 3 C 7 PHE A 219 SER A 223 -1 O TYR A 220 N TYR A 237
SHEET 4 C 7 LYS A 196 ASP A 200 1 O VAL A 197 N PHE A 219
SHEET 5 C 7 THR A 165 THR A 171 1 O ARG A 166 N LYS A 196
SHEET 6 C 7 ASN A 115 SER A 119 1 O ASN A 115 N ARG A 166
SHEET 7 C 7 GLU A 140 ILE A 144 1 O GLU A 140 N ILE A 116
SHEET 1 D 2 ILE A 256 THR A 258 0
SHEET 2 D 2 THR A 266 TRP A 267 -1 O THR A 266 N ALA A 257
SHEET 1 E 4 LEU A 323 TYR A 326 0
SHEET 2 E 4 VAL A 334 LEU A 339 -1 O ALA A 336 N TYR A 326
SHEET 3 E 4 MET A 377 SER A 381 -1 N CYS A 378 O PHE A 337
SHEET 4 E 4 ARG A 359 GLY A 361 -1 O ARG A 359 N ARG A 379
LINK NZ LYS A 226 C4A PLP A 500 1555 1555 1.36
SITE 1 AC1 15 THR A 94 THR A 95 HIS A 123 ALA A 125
SITE 2 AC1 15 ASN A 175 ASP A 200 ALA A 202 GLN A 203
SITE 3 AC1 15 SER A 223 HIS A 225 LYS A 226 GLY A 277
SITE 4 AC1 15 THR A 278 HOH A 588 HOH A 596
CRYST1 126.375 126.375 133.578 90.00 90.00 90.00 P 43 21 2 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 0.007913 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007913 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007486 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
