HEADER OXIDOREDUCTASE 12-APR-05 1ZCJ
TITLE CRYSTAL STRUCTURE OF 3-HYDROXYACYL-COA DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEROXISOMAL BIFUNCTIONAL ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 3-HYDROXYACYL-COA DEHYDROGENASE;
COMPND 5 SYNONYM: PBE, PBFE, MFE1 (3S)-HYDROXYACYL-COA DEHYDROGENASE;
COMPND 6 EC: 1.1.1.35;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 1, RAT, L-BIFUNCTIONAL
KEYWDS 2 ENZYME, MFE-1, FATTY ACID BETA OXIDATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.TASKINEN,T.R.KIEMA,J.K.HILTUNEN,R.K.WIERENGA
REVDAT 5 25-OCT-23 1ZCJ 1 REMARK
REVDAT 4 11-OCT-17 1ZCJ 1 REMARK
REVDAT 3 13-JUL-11 1ZCJ 1 VERSN
REVDAT 2 24-FEB-09 1ZCJ 1 VERSN
REVDAT 1 10-JAN-06 1ZCJ 0
JRNL AUTH J.P.TASKINEN,T.R.KIEMA,J.K.HILTUNEN,R.K.WIERENGA
JRNL TITL STRUCTURAL STUDIES OF MFE-1: THE 1.9A CRYSTAL STRUCTURE OF
JRNL TITL 2 THE DEHYDROGENASE PART OF RAT PEROXISOMAL MFE-1
JRNL REF J.MOL.BIOL. V. 355 734 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16330050
JRNL DOI 10.1016/J.JMB.2005.10.085
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34648
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1115
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4977
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1680
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3559
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 582
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 0.73000
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): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.118
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3692 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4995 ; 1.680 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 458 ; 6.181 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 540 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2789 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2939 ; 0.235 ; 0.200
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): 761 ; 0.185 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 156 ; 0.190 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 63 ; 0.155 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2289 ; 0.814 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3692 ; 1.439 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1403 ; 2.325 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1303 ; 3.570 ; 4.500
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 : 3
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 278 A 472
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5240 -24.1340 -4.0880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1942 T22: 0.1896
REMARK 3 T33: 0.1539 T12: -0.0012
REMARK 3 T13: 0.0269 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.7919 L22: 0.9891
REMARK 3 L33: 0.8224 L12: -0.1067
REMARK 3 L13: -0.5419 L23: 0.3081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0848 S12: 0.0132 S13: 0.2783
REMARK 3 S21: 0.0305 S22: 0.0145 S23: 0.0512
REMARK 3 S31: -0.1068 S32: -0.0771 S33: -0.0993
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 478 A 604
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5290 -43.8180 19.1600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1900 T22: 0.1948
REMARK 3 T33: 0.1340 T12: -0.0162
REMARK 3 T13: -0.0012 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.1452 L22: 0.8231
REMARK 3 L33: 1.3060 L12: -0.3094
REMARK 3 L13: -0.5661 L23: 0.2827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0643 S12: -0.0280 S13: 0.0223
REMARK 3 S21: 0.0112 S22: 0.0315 S23: 0.1149
REMARK 3 S31: 0.1079 S32: -0.1506 S33: 0.0328
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 614 A 710
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6050 -47.3820 2.0390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1965 T22: 0.1207
REMARK 3 T33: 0.0933 T12: -0.0039
REMARK 3 T13: 0.0026 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.7810 L22: 0.7596
REMARK 3 L33: 0.6522 L12: -0.0948
REMARK 3 L13: -0.1277 L23: -0.0215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0399 S12: 0.0197 S13: -0.0809
REMARK 3 S21: 0.0421 S22: 0.0374 S23: -0.0695
REMARK 3 S31: 0.1357 S32: 0.0291 S33: 0.0025
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-02
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 : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.134
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37374
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1WDK ALPHA SUBUNIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, TRI-NA CITRATE, AMMONIUM
REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 29.12500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 61.45500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.45500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 14.56250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.45500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 61.45500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.68750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.45500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.45500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 14.56250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 61.45500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.45500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.68750
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 29.12500
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1115 LIES ON A SPECIAL POSITION.
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 ALA A 260
REMARK 465 SER A 720
REMARK 465 LYS A 721
REMARK 465 LEU A 722
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 OE1 GLN A 268 O HOH A 1267 1.22
REMARK 500 CD GLN A 268 O HOH A 1267 2.03
REMARK 500 O HOH A 898 O HOH A 1260 2.13
REMARK 500 O HOH A 961 O HOH A 1299 2.19
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 519 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 SER A 542 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 GLY A 553 N - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A 657 NE - CZ - NH2 ANGL. DEV. = -3.7 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 LEU A 304 50.02 -117.89
REMARK 500 ALA A 380 47.97 -141.75
REMARK 500 PHE A 382 127.12 -38.99
REMARK 500 GLU A 383 89.31 -67.81
REMARK 500 ARG A 423 51.72 -149.26
REMARK 500 PHE A 478 -126.11 50.41
REMARK 500 THR A 539 -23.00 -152.66
REMARK 500 SER A 542 -28.58 120.51
REMARK 500 ALA A 715 -8.30 -140.41
REMARK 500 HIS A 718 -14.22 -147.10
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 ARG A 552 GLY A 553 -34.51
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ZCJ A 260 722 UNP P07896 ECHP_RAT 259 721
SEQRES 1 A 463 ALA SER GLY GLN ALA LYS ALA LEU GLN TYR ALA PHE PHE
SEQRES 2 A 463 ALA GLU LYS SER ALA ASN LYS TRP SER THR PRO SER GLY
SEQRES 3 A 463 ALA SER TRP LYS THR ALA SER ALA GLN PRO VAL SER SER
SEQRES 4 A 463 VAL GLY VAL LEU GLY LEU GLY THR MET GLY ARG GLY ILE
SEQRES 5 A 463 ALA ILE SER PHE ALA ARG VAL GLY ILE SER VAL VAL ALA
SEQRES 6 A 463 VAL GLU SER ASP PRO LYS GLN LEU ASP ALA ALA LYS LYS
SEQRES 7 A 463 ILE ILE THR PHE THR LEU GLU LYS GLU ALA SER ARG ALA
SEQRES 8 A 463 HIS GLN ASN GLY GLN ALA SER ALA LYS PRO LYS LEU ARG
SEQRES 9 A 463 PHE SER SER SER THR LYS GLU LEU SER THR VAL ASP LEU
SEQRES 10 A 463 VAL VAL GLU ALA VAL PHE GLU ASP MET ASN LEU LYS LYS
SEQRES 11 A 463 LYS VAL PHE ALA GLU LEU SER ALA LEU CYS LYS PRO GLY
SEQRES 12 A 463 ALA PHE LEU CYS THR ASN THR SER ALA LEU ASN VAL ASP
SEQRES 13 A 463 ASP ILE ALA SER SER THR ASP ARG PRO GLN LEU VAL ILE
SEQRES 14 A 463 GLY THR HIS PHE PHE SER PRO ALA HIS VAL MET ARG LEU
SEQRES 15 A 463 LEU GLU VAL ILE PRO SER ARG TYR SER SER PRO THR THR
SEQRES 16 A 463 ILE ALA THR VAL MET SER LEU SER LYS LYS ILE GLY LYS
SEQRES 17 A 463 ILE GLY VAL VAL VAL GLY ASN CYS TYR GLY PHE VAL GLY
SEQRES 18 A 463 ASN ARG MET LEU ALA PRO TYR TYR ASN GLN GLY PHE PHE
SEQRES 19 A 463 LEU LEU GLU GLU GLY SER LYS PRO GLU ASP VAL ASP GLY
SEQRES 20 A 463 VAL LEU GLU GLU PHE GLY PHE LYS MET GLY PRO PHE ARG
SEQRES 21 A 463 VAL SER ASP LEU ALA GLY LEU ASP VAL GLY TRP LYS ILE
SEQRES 22 A 463 ARG LYS GLY GLN GLY LEU THR GLY PRO SER LEU PRO PRO
SEQRES 23 A 463 GLY THR PRO VAL ARG LYS ARG GLY ASN SER ARG TYR SER
SEQRES 24 A 463 PRO LEU GLY ASP MET LEU CYS GLU ALA GLY ARG PHE GLY
SEQRES 25 A 463 GLN LYS THR GLY LYS GLY TRP TYR GLN TYR ASP LYS PRO
SEQRES 26 A 463 LEU GLY ARG ILE HIS LYS PRO ASP PRO TRP LEU SER THR
SEQRES 27 A 463 PHE LEU SER GLN TYR ARG GLU VAL HIS HIS ILE GLU GLN
SEQRES 28 A 463 ARG THR ILE SER LYS GLU GLU ILE LEU GLU ARG CYS LEU
SEQRES 29 A 463 TYR SER LEU ILE ASN GLU ALA PHE ARG ILE LEU GLU GLU
SEQRES 30 A 463 GLY MET ALA ALA ARG PRO GLU HIS ILE ASP VAL ILE TYR
SEQRES 31 A 463 LEU HIS GLY TYR GLY TRP PRO ARG HIS LYS GLY GLY PRO
SEQRES 32 A 463 MET PHE TYR ALA ALA SER VAL GLY LEU PRO THR VAL LEU
SEQRES 33 A 463 GLU LYS LEU GLN LYS TYR TYR ARG GLN ASN PRO ASP ILE
SEQRES 34 A 463 PRO GLN LEU GLU PRO SER ASP TYR LEU ARG ARG LEU VAL
SEQRES 35 A 463 ALA GLN GLY SER PRO PRO LEU LYS GLU TRP GLN SER LEU
SEQRES 36 A 463 ALA GLY PRO HIS GLY SER LYS LEU
FORMUL 2 HOH *582(H2 O)
HELIX 1 1 SER A 261 ALA A 273 1 13
HELIX 2 2 GLU A 274 LYS A 279 5 6
HELIX 3 3 GLY A 305 ARG A 317 1 13
HELIX 4 4 ASP A 328 ASN A 353 1 26
HELIX 5 5 SER A 367 SER A 372 5 6
HELIX 6 6 ASP A 384 CYS A 399 1 16
HELIX 7 7 ASN A 413 SER A 419 1 7
HELIX 8 8 ARG A 423 GLN A 425 5 3
HELIX 9 9 SER A 451 ILE A 465 1 15
HELIX 10 10 VAL A 479 GLU A 497 1 19
HELIX 11 11 LYS A 500 GLY A 512 1 13
HELIX 12 12 GLY A 516 GLY A 525 1 10
HELIX 13 13 GLY A 525 GLN A 536 1 12
HELIX 14 14 PRO A 559 ALA A 567 1 9
HELIX 15 15 ASP A 592 HIS A 606 1 15
HELIX 16 16 SER A 614 GLU A 636 1 23
HELIX 17 17 ARG A 641 TYR A 653 1 13
HELIX 18 18 PRO A 656 GLY A 660 5 5
HELIX 19 19 GLY A 661 GLY A 670 1 10
HELIX 20 20 GLY A 670 ASN A 685 1 16
HELIX 21 21 ILE A 688 GLU A 692 5 5
HELIX 22 22 SER A 694 GLN A 703 1 10
HELIX 23 23 PRO A 707 LYS A 709 5 3
HELIX 24 24 GLU A 710 GLY A 716 1 7
SHEET 1 A 8 LEU A 362 SER A 365 0
SHEET 2 A 8 SER A 321 VAL A 325 1 N ALA A 324 O ARG A 363
SHEET 3 A 8 SER A 298 LEU A 302 1 N VAL A 301 O VAL A 325
SHEET 4 A 8 LEU A 376 GLU A 379 1 O VAL A 378 N GLY A 300
SHEET 5 A 8 PHE A 404 THR A 407 1 O CYS A 406 N VAL A 377
SHEET 6 A 8 VAL A 427 PHE A 432 1 O THR A 430 N THR A 407
SHEET 7 A 8 LEU A 441 PRO A 446 -1 O ILE A 445 N GLY A 429
SHEET 8 A 8 ILE A 468 VAL A 471 1 O VAL A 470 N VAL A 444
SHEET 1 B 2 LYS A 551 ARG A 552 0
SHEET 2 B 2 SER A 555 ARG A 556 -1 O SER A 555 N ARG A 552
SHEET 1 C 2 TYR A 579 TYR A 581 0
SHEET 2 C 2 HIS A 589 PRO A 591 -1 O LYS A 590 N GLN A 580
CISPEP 1 SER A 434 PRO A 435 0 -2.85
CISPEP 2 GLY A 540 PRO A 541 0 -23.64
CISPEP 3 PRO A 541 SER A 542 0 -5.93
CISPEP 4 PRO A 717 HIS A 718 0 -27.12
CISPEP 5 HIS A 718 GLY A 719 0 -6.18
CRYST1 122.910 122.910 58.250 90.00 90.00 90.00 P 41 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 0.008136 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
