HEADER SIGNALING PROTEIN 22-MAY-12 4FB4
TITLE THE STRUCTURE OF AN ABC-TRANSPORTER FAMILY PROTEIN FROM
TITLE 2 RHODOPSEUDOMONAS PALUSTRIS IN COMPLEX WITH CAFFEIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE BRANCHED-CHAIN AMINO ACID TRANSPORT SYSTEM
COMPND 3 SUBSTRATE-BINDING PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;
SOURCE 3 ORGANISM_TAXID: 258594;
SOURCE 4 STRAIN: CGA009;
SOURCE 5 GENE: LIVK, RPA1789;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, ALPHA/BETA, AROMATIC COMPOUND
KEYWDS 2 TRANSPORT, AROMATIC COMPOUNDS, SIGNALING PROTEIN, MIDWEST CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, MCSG
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,J.C.MACK,S.ZERBS,F.COLLART,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 6 15-NOV-17 4FB4 1 REMARK
REVDAT 5 25-SEP-13 4FB4 1 JRNL
REVDAT 4 07-AUG-13 4FB4 1 JRNL
REVDAT 3 24-JUL-13 4FB4 1 JRNL
REVDAT 2 15-MAY-13 4FB4 1 JRNL
REVDAT 1 26-SEP-12 4FB4 0
JRNL AUTH K.TAN,C.CHANG,M.CUFF,J.OSIPIUK,E.LANDORF,J.C.MACK,S.ZERBS,
JRNL AUTH 2 A.JOACHIMIAK,F.R.COLLART
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF SOLUTE BINDING
JRNL TITL 2 PROTEINS FOR AROMATIC COMPOUNDS DERIVED FROM LIGNIN:
JRNL TITL 3 P-COUMARIC ACID AND RELATED AROMATIC ACIDS.
JRNL REF PROTEINS V. 81 1709 2013
JRNL REFN ISSN 0887-3585
JRNL PMID 23606130
JRNL DOI 10.1002/PROT.24305
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 25528
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1290
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1181
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 44
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2699
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.66000
REMARK 3 B33 (A**2) : -0.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.900
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2774 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1872 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3766 ; 1.594 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4596 ; 1.036 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 361 ; 5.537 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;32.801 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;13.594 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.610 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 435 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3091 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 525 ; 0.009 ; 0.020
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 26 A 385
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9476 60.1327 22.4573
REMARK 3 T TENSOR
REMARK 3 T11: 0.0107 T22: 0.0177
REMARK 3 T33: 0.0275 T12: 0.0031
REMARK 3 T13: -0.0044 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.6596 L22: 1.2836
REMARK 3 L33: 0.9563 L12: 0.2270
REMARK 3 L13: 0.1868 L23: 0.5146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: -0.0627 S13: 0.0147
REMARK 3 S21: 0.0617 S22: 0.0519 S23: -0.1527
REMARK 3 S31: -0.0151 S32: 0.0400 S33: -0.0705
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 ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4FB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27597
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.68400
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: SAD
REMARK 200 SOFTWARE USED: MLPHARE, DM 6.1, HKL-3000, SHELXD, SOLVE, RESOLVE,
REMARK 200 CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES:NAOH PH 6.5, 30% PEG 4K,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 24.49300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.50750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.52750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.50750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.49300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.52750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 24
REMARK 465 ASN A 25
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 GLU A 27 CG CD OE1 OE2
REMARK 470 LYS A 385 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 246 CG HIS A 246 CD2 0.056
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 336 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH2 ANGL. DEV. = 4.0 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 99 -158.41 -108.37
REMARK 500 ASP A 273 63.37 -150.12
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 DHC A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TX6 RELATED DB: PDB
REMARK 900 SAME IN COMPLEX WITH 3,4-HYDOXYPHENYL PYRUVATE
REMARK 900 RELATED ID: 4F8J RELATED DB: PDB
REMARK 900 SAME IN COMPLEX WITH P-COUMARATE
REMARK 900 RELATED ID: MCSG-APC102206 RELATED DB: TARGETTRACK
DBREF 4FB4 A 26 385 UNP Q6N8W4 Q6N8W4_RHOPA 26 385
SEQADV 4FB4 SER A 24 UNP Q6N8W4 EXPRESSION TAG
SEQADV 4FB4 ASN A 25 UNP Q6N8W4 EXPRESSION TAG
SEQRES 1 A 362 SER ASN ALA GLU THR ASN GLU ILE THR ILE GLY ILE THR
SEQRES 2 A 362 VAL THR THR THR GLY PRO ALA ALA ALA LEU GLY ILE PRO
SEQRES 3 A 362 GLU ARG ASN ALA LEU GLU PHE VAL ALA LYS GLU ILE GLY
SEQRES 4 A 362 GLY HIS PRO LEU LYS VAL ILE VAL LEU ASP ASP GLY GLY
SEQRES 5 A 362 ASP PRO THR ALA ALA THR THR ASN ALA ARG ARG PHE VAL
SEQRES 6 A 362 THR GLU SER LYS ALA ASP VAL ILE MSE GLY SER SER VAL
SEQRES 7 A 362 THR PRO PRO THR VAL ALA VAL SER ASN VAL ALA ASN GLU
SEQRES 8 A 362 ALA GLN VAL PRO HIS ILE ALA LEU ALA PRO LEU PRO ILE
SEQRES 9 A 362 THR PRO GLU ARG ALA LYS TRP SER VAL ALA MSE PRO GLN
SEQRES 10 A 362 PRO ILE PRO ILE MSE GLY LYS VAL LEU TYR GLU HIS MSE
SEQRES 11 A 362 LYS LYS ASN ASN ILE LYS THR VAL GLY TYR ILE GLY TYR
SEQRES 12 A 362 SER ASP SER TYR GLY ASP LEU TRP PHE ASN ASP LEU LYS
SEQRES 13 A 362 LYS GLN GLY GLU ALA MSE GLY LEU LYS ILE VAL ALA GLU
SEQRES 14 A 362 GLU ARG PHE ALA ARG PRO ASP THR SER VAL ALA GLY GLN
SEQRES 15 A 362 VAL LEU LYS LEU VAL ALA ALA ASN PRO ASP ALA ILE LEU
SEQRES 16 A 362 VAL GLY ALA SER GLY THR ALA ALA ALA LEU PRO GLN THR
SEQRES 17 A 362 SER LEU ARG GLU ARG GLY TYR LYS GLY LEU ILE TYR GLN
SEQRES 18 A 362 THR HIS GLY ALA ALA SER MSE ASP PHE ILE ARG ILE ALA
SEQRES 19 A 362 GLY LYS SER ALA GLU GLY VAL LEU MSE ALA SER GLY PRO
SEQRES 20 A 362 VAL MSE ASP PRO GLU GLY GLN ASP ASP SER ALA LEU THR
SEQRES 21 A 362 LYS LYS PRO GLY LEU GLU LEU ASN THR ALA TYR GLU ALA
SEQRES 22 A 362 LYS TYR GLY PRO ASN SER ARG SER GLN PHE ALA ALA HIS
SEQRES 23 A 362 SER PHE ASP ALA PHE LYS VAL LEU GLU ARG VAL VAL PRO
SEQRES 24 A 362 VAL ALA LEU LYS THR ALA LYS PRO GLY THR GLN GLU PHE
SEQRES 25 A 362 ARG GLU ALA ILE ARG LYS ALA LEU VAL SER GLU LYS ASP
SEQRES 26 A 362 ILE ALA ALA SER GLN GLY VAL TYR SER PHE THR GLU THR
SEQRES 27 A 362 ASP ARG TYR GLY LEU ASP ASP ARG SER ARG ILE LEU LEU
SEQRES 28 A 362 THR VAL LYS ASP GLY LYS TYR VAL MSE VAL LYS
MODRES 4FB4 MSE A 97 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 138 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 145 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 153 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 185 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 251 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 266 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 272 MET SELENOMETHIONINE
MODRES 4FB4 MSE A 383 MET SELENOMETHIONINE
HET MSE A 97 8
HET MSE A 138 8
HET MSE A 145 8
HET MSE A 153 8
HET MSE A 185 8
HET MSE A 251 8
HET MSE A 266 8
HET MSE A 272 8
HET MSE A 383 8
HET DHC A 401 13
HET GOL A 402 6
HETNAM MSE SELENOMETHIONINE
HETNAM DHC CAFFEIC ACID
HETNAM GOL GLYCEROL
HETSYN DHC 3,4-DIHYDROXYCINNAMIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 2 DHC C9 H8 O4
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *127(H2 O)
HELIX 1 1 ALA A 43 LEU A 54 1 12
HELIX 2 2 GLU A 55 VAL A 57 5 3
HELIX 3 3 ASP A 76 GLU A 90 1 15
HELIX 4 4 VAL A 101 GLN A 116 1 16
HELIX 5 5 THR A 128 LYS A 133 1 6
HELIX 6 6 PRO A 141 ASN A 156 1 16
HELIX 7 7 ASP A 168 MSE A 185 1 18
HELIX 8 8 VAL A 202 ASN A 213 1 12
HELIX 9 9 SER A 222 ARG A 236 1 15
HELIX 10 10 HIS A 246 ALA A 249 5 4
HELIX 11 11 SER A 250 GLY A 258 1 9
HELIX 12 12 LYS A 259 GLU A 262 5 4
HELIX 13 13 GLY A 269 GLN A 277 5 9
HELIX 14 14 THR A 283 GLY A 299 1 17
HELIX 15 15 SER A 304 LYS A 326 1 23
HELIX 16 16 THR A 332 GLU A 346 1 15
HELIX 17 17 ASP A 367 ARG A 371 5 5
SHEET 1 A 6 GLU A 60 ILE A 61 0
SHEET 2 A 6 HIS A 64 ASP A 72 -1 O HIS A 64 N ILE A 61
SHEET 3 A 6 ILE A 31 VAL A 37 1 N ILE A 35 O ILE A 69
SHEET 4 A 6 VAL A 95 GLY A 98 1 O MSE A 97 N GLY A 34
SHEET 5 A 6 HIS A 119 ALA A 121 1 O ILE A 120 N ILE A 96
SHEET 6 A 6 SER A 135 ALA A 137 1 O VAL A 136 N ALA A 121
SHEET 1 B 7 LYS A 188 PHE A 195 0
SHEET 2 B 7 THR A 160 TYR A 166 1 N VAL A 161 O LYS A 188
SHEET 3 B 7 ALA A 216 GLY A 220 1 O GLY A 220 N ILE A 164
SHEET 4 B 7 LEU A 241 GLN A 244 1 O TYR A 243 N ILE A 217
SHEET 5 B 7 LEU A 265 SER A 268 1 O LEU A 265 N GLN A 244
SHEET 6 B 7 ILE A 372 LYS A 377 -1 O LEU A 374 N MSE A 266
SHEET 7 B 7 LYS A 380 MSE A 383 -1 O VAL A 382 N THR A 375
SHEET 1 C 2 ILE A 349 ALA A 350 0
SHEET 2 C 2 VAL A 355 TYR A 356 -1 O TYR A 356 N ILE A 349
LINK C ILE A 96 N MSE A 97 1555 1555 1.31
LINK C MSE A 97 N GLY A 98 1555 1555 1.32
LINK C ALA A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N PRO A 139 1555 1555 1.37
LINK C ILE A 144 N MSE A 145 1555 1555 1.32
LINK C MSE A 145 N GLY A 146 1555 1555 1.33
LINK C HIS A 152 N MSE A 153 1555 1555 1.32
LINK C MSE A 153 N LYS A 154 1555 1555 1.33
LINK C ALA A 184 N MSE A 185 1555 1555 1.34
LINK C MSE A 185 N GLY A 186 1555 1555 1.33
LINK C SER A 250 N MSE A 251 1555 1555 1.33
LINK C MSE A 251 N ASP A 252 1555 1555 1.33
LINK C LEU A 265 N MSE A 266 1555 1555 1.33
LINK C MSE A 266 N ALA A 267 1555 1555 1.32
LINK C VAL A 271 N MSE A 272 1555 1555 1.32
LINK C MSE A 272 N ASP A 273 1555 1555 1.34
LINK C VAL A 382 N MSE A 383 1555 1555 1.33
LINK C MSE A 383 N VAL A 384 1555 1555 1.33
CISPEP 1 GLY A 98 SER A 99 0 -0.40
SITE 1 AC1 15 LEU A 46 VAL A 101 THR A 102 LEU A 122
SITE 2 AC1 15 PRO A 124 PRO A 139 TYR A 170 ARG A 197
SITE 3 AC1 15 SER A 222 HIS A 246 GLY A 247 GLN A 305
SITE 4 AC1 15 PHE A 306 HIS A 309 HOH A 501
SITE 1 AC2 8 PRO A 42 TYR A 166 ARG A 197 SER A 222
SITE 2 AC2 8 GLY A 223 THR A 224 ALA A 225 HOH A 507
CRYST1 48.986 71.055 91.015 90.00 90.00 90.00 P 21 21 21 4
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 0.020414 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014074 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
