HEADER TRANSFERASE, LYASE 04-APR-07 2PFD
TITLE ANISOTROPICALLY REFINED STRUCTURE OF FTCD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORMIMIDOYLTRANSFERASE-CYCLODEAMINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: FORMIMINOTRANSFERASE- CYCLODEAMINASE, FTCD, 58 KDA
COMPND 5 MICROTUBULE-BINDING PROTEIN;
COMPND 6 EC: 2.1.2.5, 4.3.1.4;
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 STRAIN: RAT;
SOURCE 6 GENE: FTCD;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-21(B)
KEYWDS PROTEIN ASSEMBLY, TRANSFERASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.K.POON,X.CHEN,M.LU,F.A.QUIOCHO,Q.WANG,J.MA
REVDAT 7 10-AUG-11 2PFD 1 REMARK
REVDAT 6 13-JUL-11 2PFD 1 VERSN
REVDAT 5 09-JUN-09 2PFD 1 REVDAT
REVDAT 4 24-FEB-09 2PFD 1 VERSN
REVDAT 3 16-DEC-08 2PFD 1 EXPDTA
REVDAT 2 13-MAY-08 2PFD 1 REMARK JRNL
REVDAT 1 24-APR-07 2PFD 0
JRNL AUTH B.K.POON,X.CHEN,M.LU,N.K.VYAS,F.A.QUIOCHO,Q.WANG,J.MA
JRNL TITL ANISOTROPICALLY REFINED STRUCTURE OF FTCD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.MAO,N.K.VYAS,M.N.VYAS,D.H.CHEN,S.J.LUDTKE,W.CHIU,
REMARK 1 AUTH 2 F.A.QUIOCHO
REMARK 1 TITL STRUCTURE OF THE BIFUNCTIONAL AND GOLGI-ASSOCIATED
REMARK 1 TITL 2 FORMIMINOTRANSFERASE CYCLODEAMINASE OCTAMER.
REMARK 1 REF EMBO J. V. 23 2963 2004
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 15272307
REMARK 1 DOI 10.1038/SJ.EMBOJ.7600327
REMARK 2
REMARK 2 RESOLUTION. 3.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 3.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 34749
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) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1712
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) : 3.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1856
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16524
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : 0.74000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.615
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.460
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 65.518
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.867
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.855
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16812 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22800 ; 1.551 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2156 ; 6.411 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 740 ;41.682 ;24.108
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2876 ;22.879 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 136 ;21.895 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2616 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12732 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9467 ; 0.302 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 11485 ; 0.326 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 750 ; 0.194 ; 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): 158 ; 0.272 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.121 ; 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): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 541 1
REMARK 3 1 B 2 B 541 1
REMARK 3 1 C 2 C 541 1
REMARK 3 1 D 2 D 541 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4121 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 4121 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 4121 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 4121 ; 0.040 ; 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 : 1.20
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 2PFD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-07.
REMARK 100 THE RCSB ID CODE IS RCSB042315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 1TT9.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 BIOLOGICAL ASSEMBLY IS AN OCTAMER.
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 BIOMT1 2 -1.000000 0.000000 0.000000 134.84800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 134.84800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 134.84800
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 134.84800
REMARK 350 BIOMT3 4 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 MSE A 1
REMARK 465 MSE B 1
REMARK 465 MSE C 1
REMARK 465 MSE D 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 CD2 LEU D 153 O SER D 165 2.17
REMARK 500 O GLU B 13 N ASN B 15 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 153 CG LEU A 153 CD2 -0.276
REMARK 500 LEU B 153 CG LEU B 153 CD2 -0.295
REMARK 500 LEU C 153 CG LEU C 153 CD2 -0.273
REMARK 500 GLU D 13 CD GLU D 13 OE1 0.161
REMARK 500 LEU D 153 CG LEU D 153 CD2 -0.332
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 PRO A 55 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU A 153 CB - CG - CD1 ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU A 153 CB - CG - CD2 ANGL. DEV. = -15.6 DEGREES
REMARK 500 MSE A 377 CB - CG - SE ANGL. DEV. = 20.0 DEGREES
REMARK 500 MSE A 377 CG - SE - CE ANGL. DEV. = 14.2 DEGREES
REMARK 500 GLU B 13 CA - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 PRO B 55 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU B 153 CD1 - CG - CD2 ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU B 153 CB - CG - CD1 ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU B 153 CB - CG - CD2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG B 435 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 435 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG B 435 NE - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 PRO C 55 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU C 153 CB - CG - CD1 ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU C 153 CB - CG - CD2 ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO D 55 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU D 153 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU D 153 CD1 - CG - CD2 ANGL. DEV. = -19.6 DEGREES
REMARK 500 LEU D 153 CB - CG - CD1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 LEU D 153 CB - CG - CD2 ANGL. DEV. = -12.0 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 GLN A 3 51.96 79.55
REMARK 500 VAL A 8 76.77 -117.89
REMARK 500 GLU A 13 -48.54 -22.57
REMARK 500 ASN A 15 88.28 83.70
REMARK 500 ASN A 16 111.23 162.25
REMARK 500 GLN A 17 -64.63 -19.03
REMARK 500 ASP A 37 141.23 177.48
REMARK 500 PRO A 55 -62.80 -23.88
REMARK 500 GLN A 71 40.93 -94.07
REMARK 500 LEU A 72 -6.53 -153.82
REMARK 500 LYS A 79 91.37 -163.16
REMARK 500 GLU A 81 39.42 -82.96
REMARK 500 PRO A 83 64.43 -46.09
REMARK 500 ARG A 84 -165.28 -67.51
REMARK 500 MSE A 85 -63.45 -163.41
REMARK 500 ASP A 89 -133.06 -63.73
REMARK 500 VAL A 96 -53.51 -128.10
REMARK 500 GLN A 113 -71.53 -68.63
REMARK 500 ASN A 120 78.81 79.62
REMARK 500 GLU A 128 3.22 -55.29
REMARK 500 ALA A 129 -86.06 -99.26
REMARK 500 ALA A 130 130.49 -15.77
REMARK 500 PRO A 133 42.73 -71.99
REMARK 500 ARG A 142 53.60 -54.56
REMARK 500 ALA A 143 56.62 -59.53
REMARK 500 GLU A 145 -149.77 46.57
REMARK 500 ALA A 148 -56.82 -147.45
REMARK 500 PRO A 150 5.30 -63.82
REMARK 500 GLU A 151 -28.46 -154.00
REMARK 500 PRO A 164 -107.41 -31.32
REMARK 500 SER A 165 10.24 -170.43
REMARK 500 ALA A 173 162.51 70.79
REMARK 500 LEU A 190 26.81 -78.29
REMARK 500 SER A 191 -138.49 -97.88
REMARK 500 LYS A 210 -117.25 -75.79
REMARK 500 ASP A 211 119.44 -34.19
REMARK 500 GLN A 212 75.23 93.12
REMARK 500 ASP A 240 98.07 -160.21
REMARK 500 VAL A 249 -70.91 -67.00
REMARK 500 VAL A 265 65.18 -115.78
REMARK 500 VAL A 304 -83.25 -72.94
REMARK 500 ASN A 305 -39.65 -33.51
REMARK 500 SER A 311 -25.84 -142.51
REMARK 500 ALA A 313 162.88 178.18
REMARK 500 GLU A 319 -6.02 -144.84
REMARK 500 ASP A 328 71.34 -105.33
REMARK 500 GLU A 332 159.59 60.09
REMARK 500 SER A 339 153.28 -38.45
REMARK 500 ARG A 345 47.83 -85.06
REMARK 500 GLU A 346 -64.64 -149.71
REMARK 500
REMARK 500 THIS ENTRY HAS 311 RAMACHANDRAN OUTLIERS.
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 LYS A 427 ASN A 428 143.54
REMARK 500 LYS B 427 ASN B 428 143.81
REMARK 500 LYS C 427 ASN C 428 143.98
REMARK 500 LYS D 427 ASN D 428 143.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TT9 RELATED DB: PDB
REMARK 900 THIS IS A FURTHER REFINED ALL-ATOM STRUCTURE OF THE ID CODE
REMARK 900 1TT9 THAT ONLY CONTAINS ALPHA-CARBON ATOMS.
DBREF 2PFD A 1 541 UNP O88618 FTCD_RAT 1 541
DBREF 2PFD B 1 541 UNP O88618 FTCD_RAT 1 541
DBREF 2PFD C 1 541 UNP O88618 FTCD_RAT 1 541
DBREF 2PFD D 1 541 UNP O88618 FTCD_RAT 1 541
SEQRES 1 A 541 MSE SER GLN LEU VAL GLU CYS VAL PRO ASN PHE SER GLU
SEQRES 2 A 541 GLY ASN ASN GLN GLU VAL ILE ASP ALA ILE SER GLN ALA
SEQRES 3 A 541 ILE SER GLN THR PRO GLY CYS VAL LEU LEU ASP VAL ASP
SEQRES 4 A 541 ALA GLY PRO SER THR ASN ARG THR VAL TYR THR PHE VAL
SEQRES 5 A 541 GLY GLN PRO GLU CYS VAL VAL GLU GLY ALA LEU SER ALA
SEQRES 6 A 541 ALA ARG THR ALA SER GLN LEU ILE ASP MSE ARG LYS HIS
SEQRES 7 A 541 LYS GLY GLU HIS PRO ARG MSE GLY ALA LEU ASP VAL CYS
SEQRES 8 A 541 PRO PHE ILE PRO VAL ARG GLY VAL SER MSE ASP GLU CYS
SEQRES 9 A 541 VAL LEU CYS ALA LYS ALA PHE GLY GLN ARG LEU ALA GLU
SEQRES 10 A 541 GLU LEU ASN VAL PRO VAL TYR LEU TYR GLY GLU ALA ALA
SEQRES 11 A 541 GLN MSE PRO SER ARG GLN THR LEU PRO ALA ILE ARG ALA
SEQRES 12 A 541 GLY GLU TYR GLU ALA LEU PRO GLU LYS LEU LYS GLN ALA
SEQRES 13 A 541 GLU TRP VAL PRO ASP PHE GLY PRO SER SER PHE VAL PRO
SEQRES 14 A 541 SER TRP GLY ALA THR VAL THR GLY ALA ARG LYS PHE LEU
SEQRES 15 A 541 ILE ALA PHE ASN ILE ASN LEU LEU SER THR LYS GLU GLN
SEQRES 16 A 541 ALA HIS ARG ILE ALA LEU ASN LEU ARG GLU GLN GLY ARG
SEQRES 17 A 541 GLY LYS ASP GLN PRO GLY ARG LEU LYS LYS VAL GLN GLY
SEQRES 18 A 541 ILE GLY TRP TYR LEU GLU GLU LYS ASN LEU ALA GLN VAL
SEQRES 19 A 541 SER THR ASN LEU LEU ASP PHE GLU VAL THR ALA LEU HIS
SEQRES 20 A 541 THR VAL TYR GLU GLU ALA ARG ARG GLU ALA GLN GLU LEU
SEQRES 21 A 541 ASN LEU PRO VAL VAL GLY SER GLN LEU VAL GLY LEU VAL
SEQRES 22 A 541 PRO LEU LYS ALA LEU LEU ASP ALA ALA ALA PHE TYR CYS
SEQRES 23 A 541 ASP LYS GLU LYS LEU PHE VAL LEU GLU GLU GLU HIS ARG
SEQRES 24 A 541 ILE ARG LEU VAL VAL ASN ARG LEU GLY LEU ASP SER LEU
SEQRES 25 A 541 ALA PRO PHE ASP PRO LYS GLU ARG ILE ILE GLU TYR LEU
SEQRES 26 A 541 VAL PRO ASP SER GLY PRO GLU GLN SER LEU LEU ASP ALA
SEQRES 27 A 541 SER LEU ARG ALA PHE VAL ARG GLU VAL GLY ALA ARG SER
SEQRES 28 A 541 ALA ALA PRO GLY GLY GLY SER VAL ALA ALA ALA VAL ALA
SEQRES 29 A 541 ALA LEU GLY ALA ALA LEU ALA SER MSE VAL GLY GLN MSE
SEQRES 30 A 541 THR TYR GLY ARG ARG GLN PHE ASP HIS LEU ASP SER THR
SEQRES 31 A 541 MSE ARG ARG LEU ILE PRO PRO PHE HIS ALA ALA SER ALA
SEQRES 32 A 541 GLN LEU THR SER LEU VAL ASP ALA ASP ALA ARG ALA PHE
SEQRES 33 A 541 ALA ALA CYS LEU GLY ALA ILE LYS LEU PRO LYS ASN THR
SEQRES 34 A 541 PRO GLU GLU ARG ASP ARG ARG THR CYS ALA LEU GLN GLU
SEQRES 35 A 541 GLY LEU ARG GLN ALA VAL ALA VAL PRO LEU LYS LEU ALA
SEQRES 36 A 541 GLU THR VAL SER GLN LEU TRP PRO ALA LEU GLN GLU LEU
SEQRES 37 A 541 ALA GLN CYS GLY ASN LEU SER CYS LEU SER ASP LEU GLN
SEQRES 38 A 541 VAL ALA ALA LYS ALA LEU GLU THR GLY VAL PHE GLY ALA
SEQRES 39 A 541 TYR PHE ASN VAL LEU ILE ASN LEU LYS ASP MSE THR ASP
SEQRES 40 A 541 ASP VAL PHE LYS GLU LYS THR ARG HIS ARG ILE SER SER
SEQRES 41 A 541 LEU LEU GLN GLU ALA LYS THR GLN ALA ALA LEU VAL LEU
SEQRES 42 A 541 GLY SER LEU GLU ALA ARG LYS GLU
SEQRES 1 B 541 MSE SER GLN LEU VAL GLU CYS VAL PRO ASN PHE SER GLU
SEQRES 2 B 541 GLY ASN ASN GLN GLU VAL ILE ASP ALA ILE SER GLN ALA
SEQRES 3 B 541 ILE SER GLN THR PRO GLY CYS VAL LEU LEU ASP VAL ASP
SEQRES 4 B 541 ALA GLY PRO SER THR ASN ARG THR VAL TYR THR PHE VAL
SEQRES 5 B 541 GLY GLN PRO GLU CYS VAL VAL GLU GLY ALA LEU SER ALA
SEQRES 6 B 541 ALA ARG THR ALA SER GLN LEU ILE ASP MSE ARG LYS HIS
SEQRES 7 B 541 LYS GLY GLU HIS PRO ARG MSE GLY ALA LEU ASP VAL CYS
SEQRES 8 B 541 PRO PHE ILE PRO VAL ARG GLY VAL SER MSE ASP GLU CYS
SEQRES 9 B 541 VAL LEU CYS ALA LYS ALA PHE GLY GLN ARG LEU ALA GLU
SEQRES 10 B 541 GLU LEU ASN VAL PRO VAL TYR LEU TYR GLY GLU ALA ALA
SEQRES 11 B 541 GLN MSE PRO SER ARG GLN THR LEU PRO ALA ILE ARG ALA
SEQRES 12 B 541 GLY GLU TYR GLU ALA LEU PRO GLU LYS LEU LYS GLN ALA
SEQRES 13 B 541 GLU TRP VAL PRO ASP PHE GLY PRO SER SER PHE VAL PRO
SEQRES 14 B 541 SER TRP GLY ALA THR VAL THR GLY ALA ARG LYS PHE LEU
SEQRES 15 B 541 ILE ALA PHE ASN ILE ASN LEU LEU SER THR LYS GLU GLN
SEQRES 16 B 541 ALA HIS ARG ILE ALA LEU ASN LEU ARG GLU GLN GLY ARG
SEQRES 17 B 541 GLY LYS ASP GLN PRO GLY ARG LEU LYS LYS VAL GLN GLY
SEQRES 18 B 541 ILE GLY TRP TYR LEU GLU GLU LYS ASN LEU ALA GLN VAL
SEQRES 19 B 541 SER THR ASN LEU LEU ASP PHE GLU VAL THR ALA LEU HIS
SEQRES 20 B 541 THR VAL TYR GLU GLU ALA ARG ARG GLU ALA GLN GLU LEU
SEQRES 21 B 541 ASN LEU PRO VAL VAL GLY SER GLN LEU VAL GLY LEU VAL
SEQRES 22 B 541 PRO LEU LYS ALA LEU LEU ASP ALA ALA ALA PHE TYR CYS
SEQRES 23 B 541 ASP LYS GLU LYS LEU PHE VAL LEU GLU GLU GLU HIS ARG
SEQRES 24 B 541 ILE ARG LEU VAL VAL ASN ARG LEU GLY LEU ASP SER LEU
SEQRES 25 B 541 ALA PRO PHE ASP PRO LYS GLU ARG ILE ILE GLU TYR LEU
SEQRES 26 B 541 VAL PRO ASP SER GLY PRO GLU GLN SER LEU LEU ASP ALA
SEQRES 27 B 541 SER LEU ARG ALA PHE VAL ARG GLU VAL GLY ALA ARG SER
SEQRES 28 B 541 ALA ALA PRO GLY GLY GLY SER VAL ALA ALA ALA VAL ALA
SEQRES 29 B 541 ALA LEU GLY ALA ALA LEU ALA SER MSE VAL GLY GLN MSE
SEQRES 30 B 541 THR TYR GLY ARG ARG GLN PHE ASP HIS LEU ASP SER THR
SEQRES 31 B 541 MSE ARG ARG LEU ILE PRO PRO PHE HIS ALA ALA SER ALA
SEQRES 32 B 541 GLN LEU THR SER LEU VAL ASP ALA ASP ALA ARG ALA PHE
SEQRES 33 B 541 ALA ALA CYS LEU GLY ALA ILE LYS LEU PRO LYS ASN THR
SEQRES 34 B 541 PRO GLU GLU ARG ASP ARG ARG THR CYS ALA LEU GLN GLU
SEQRES 35 B 541 GLY LEU ARG GLN ALA VAL ALA VAL PRO LEU LYS LEU ALA
SEQRES 36 B 541 GLU THR VAL SER GLN LEU TRP PRO ALA LEU GLN GLU LEU
SEQRES 37 B 541 ALA GLN CYS GLY ASN LEU SER CYS LEU SER ASP LEU GLN
SEQRES 38 B 541 VAL ALA ALA LYS ALA LEU GLU THR GLY VAL PHE GLY ALA
SEQRES 39 B 541 TYR PHE ASN VAL LEU ILE ASN LEU LYS ASP MSE THR ASP
SEQRES 40 B 541 ASP VAL PHE LYS GLU LYS THR ARG HIS ARG ILE SER SER
SEQRES 41 B 541 LEU LEU GLN GLU ALA LYS THR GLN ALA ALA LEU VAL LEU
SEQRES 42 B 541 GLY SER LEU GLU ALA ARG LYS GLU
SEQRES 1 C 541 MSE SER GLN LEU VAL GLU CYS VAL PRO ASN PHE SER GLU
SEQRES 2 C 541 GLY ASN ASN GLN GLU VAL ILE ASP ALA ILE SER GLN ALA
SEQRES 3 C 541 ILE SER GLN THR PRO GLY CYS VAL LEU LEU ASP VAL ASP
SEQRES 4 C 541 ALA GLY PRO SER THR ASN ARG THR VAL TYR THR PHE VAL
SEQRES 5 C 541 GLY GLN PRO GLU CYS VAL VAL GLU GLY ALA LEU SER ALA
SEQRES 6 C 541 ALA ARG THR ALA SER GLN LEU ILE ASP MSE ARG LYS HIS
SEQRES 7 C 541 LYS GLY GLU HIS PRO ARG MSE GLY ALA LEU ASP VAL CYS
SEQRES 8 C 541 PRO PHE ILE PRO VAL ARG GLY VAL SER MSE ASP GLU CYS
SEQRES 9 C 541 VAL LEU CYS ALA LYS ALA PHE GLY GLN ARG LEU ALA GLU
SEQRES 10 C 541 GLU LEU ASN VAL PRO VAL TYR LEU TYR GLY GLU ALA ALA
SEQRES 11 C 541 GLN MSE PRO SER ARG GLN THR LEU PRO ALA ILE ARG ALA
SEQRES 12 C 541 GLY GLU TYR GLU ALA LEU PRO GLU LYS LEU LYS GLN ALA
SEQRES 13 C 541 GLU TRP VAL PRO ASP PHE GLY PRO SER SER PHE VAL PRO
SEQRES 14 C 541 SER TRP GLY ALA THR VAL THR GLY ALA ARG LYS PHE LEU
SEQRES 15 C 541 ILE ALA PHE ASN ILE ASN LEU LEU SER THR LYS GLU GLN
SEQRES 16 C 541 ALA HIS ARG ILE ALA LEU ASN LEU ARG GLU GLN GLY ARG
SEQRES 17 C 541 GLY LYS ASP GLN PRO GLY ARG LEU LYS LYS VAL GLN GLY
SEQRES 18 C 541 ILE GLY TRP TYR LEU GLU GLU LYS ASN LEU ALA GLN VAL
SEQRES 19 C 541 SER THR ASN LEU LEU ASP PHE GLU VAL THR ALA LEU HIS
SEQRES 20 C 541 THR VAL TYR GLU GLU ALA ARG ARG GLU ALA GLN GLU LEU
SEQRES 21 C 541 ASN LEU PRO VAL VAL GLY SER GLN LEU VAL GLY LEU VAL
SEQRES 22 C 541 PRO LEU LYS ALA LEU LEU ASP ALA ALA ALA PHE TYR CYS
SEQRES 23 C 541 ASP LYS GLU LYS LEU PHE VAL LEU GLU GLU GLU HIS ARG
SEQRES 24 C 541 ILE ARG LEU VAL VAL ASN ARG LEU GLY LEU ASP SER LEU
SEQRES 25 C 541 ALA PRO PHE ASP PRO LYS GLU ARG ILE ILE GLU TYR LEU
SEQRES 26 C 541 VAL PRO ASP SER GLY PRO GLU GLN SER LEU LEU ASP ALA
SEQRES 27 C 541 SER LEU ARG ALA PHE VAL ARG GLU VAL GLY ALA ARG SER
SEQRES 28 C 541 ALA ALA PRO GLY GLY GLY SER VAL ALA ALA ALA VAL ALA
SEQRES 29 C 541 ALA LEU GLY ALA ALA LEU ALA SER MSE VAL GLY GLN MSE
SEQRES 30 C 541 THR TYR GLY ARG ARG GLN PHE ASP HIS LEU ASP SER THR
SEQRES 31 C 541 MSE ARG ARG LEU ILE PRO PRO PHE HIS ALA ALA SER ALA
SEQRES 32 C 541 GLN LEU THR SER LEU VAL ASP ALA ASP ALA ARG ALA PHE
SEQRES 33 C 541 ALA ALA CYS LEU GLY ALA ILE LYS LEU PRO LYS ASN THR
SEQRES 34 C 541 PRO GLU GLU ARG ASP ARG ARG THR CYS ALA LEU GLN GLU
SEQRES 35 C 541 GLY LEU ARG GLN ALA VAL ALA VAL PRO LEU LYS LEU ALA
SEQRES 36 C 541 GLU THR VAL SER GLN LEU TRP PRO ALA LEU GLN GLU LEU
SEQRES 37 C 541 ALA GLN CYS GLY ASN LEU SER CYS LEU SER ASP LEU GLN
SEQRES 38 C 541 VAL ALA ALA LYS ALA LEU GLU THR GLY VAL PHE GLY ALA
SEQRES 39 C 541 TYR PHE ASN VAL LEU ILE ASN LEU LYS ASP MSE THR ASP
SEQRES 40 C 541 ASP VAL PHE LYS GLU LYS THR ARG HIS ARG ILE SER SER
SEQRES 41 C 541 LEU LEU GLN GLU ALA LYS THR GLN ALA ALA LEU VAL LEU
SEQRES 42 C 541 GLY SER LEU GLU ALA ARG LYS GLU
SEQRES 1 D 541 MSE SER GLN LEU VAL GLU CYS VAL PRO ASN PHE SER GLU
SEQRES 2 D 541 GLY ASN ASN GLN GLU VAL ILE ASP ALA ILE SER GLN ALA
SEQRES 3 D 541 ILE SER GLN THR PRO GLY CYS VAL LEU LEU ASP VAL ASP
SEQRES 4 D 541 ALA GLY PRO SER THR ASN ARG THR VAL TYR THR PHE VAL
SEQRES 5 D 541 GLY GLN PRO GLU CYS VAL VAL GLU GLY ALA LEU SER ALA
SEQRES 6 D 541 ALA ARG THR ALA SER GLN LEU ILE ASP MSE ARG LYS HIS
SEQRES 7 D 541 LYS GLY GLU HIS PRO ARG MSE GLY ALA LEU ASP VAL CYS
SEQRES 8 D 541 PRO PHE ILE PRO VAL ARG GLY VAL SER MSE ASP GLU CYS
SEQRES 9 D 541 VAL LEU CYS ALA LYS ALA PHE GLY GLN ARG LEU ALA GLU
SEQRES 10 D 541 GLU LEU ASN VAL PRO VAL TYR LEU TYR GLY GLU ALA ALA
SEQRES 11 D 541 GLN MSE PRO SER ARG GLN THR LEU PRO ALA ILE ARG ALA
SEQRES 12 D 541 GLY GLU TYR GLU ALA LEU PRO GLU LYS LEU LYS GLN ALA
SEQRES 13 D 541 GLU TRP VAL PRO ASP PHE GLY PRO SER SER PHE VAL PRO
SEQRES 14 D 541 SER TRP GLY ALA THR VAL THR GLY ALA ARG LYS PHE LEU
SEQRES 15 D 541 ILE ALA PHE ASN ILE ASN LEU LEU SER THR LYS GLU GLN
SEQRES 16 D 541 ALA HIS ARG ILE ALA LEU ASN LEU ARG GLU GLN GLY ARG
SEQRES 17 D 541 GLY LYS ASP GLN PRO GLY ARG LEU LYS LYS VAL GLN GLY
SEQRES 18 D 541 ILE GLY TRP TYR LEU GLU GLU LYS ASN LEU ALA GLN VAL
SEQRES 19 D 541 SER THR ASN LEU LEU ASP PHE GLU VAL THR ALA LEU HIS
SEQRES 20 D 541 THR VAL TYR GLU GLU ALA ARG ARG GLU ALA GLN GLU LEU
SEQRES 21 D 541 ASN LEU PRO VAL VAL GLY SER GLN LEU VAL GLY LEU VAL
SEQRES 22 D 541 PRO LEU LYS ALA LEU LEU ASP ALA ALA ALA PHE TYR CYS
SEQRES 23 D 541 ASP LYS GLU LYS LEU PHE VAL LEU GLU GLU GLU HIS ARG
SEQRES 24 D 541 ILE ARG LEU VAL VAL ASN ARG LEU GLY LEU ASP SER LEU
SEQRES 25 D 541 ALA PRO PHE ASP PRO LYS GLU ARG ILE ILE GLU TYR LEU
SEQRES 26 D 541 VAL PRO ASP SER GLY PRO GLU GLN SER LEU LEU ASP ALA
SEQRES 27 D 541 SER LEU ARG ALA PHE VAL ARG GLU VAL GLY ALA ARG SER
SEQRES 28 D 541 ALA ALA PRO GLY GLY GLY SER VAL ALA ALA ALA VAL ALA
SEQRES 29 D 541 ALA LEU GLY ALA ALA LEU ALA SER MSE VAL GLY GLN MSE
SEQRES 30 D 541 THR TYR GLY ARG ARG GLN PHE ASP HIS LEU ASP SER THR
SEQRES 31 D 541 MSE ARG ARG LEU ILE PRO PRO PHE HIS ALA ALA SER ALA
SEQRES 32 D 541 GLN LEU THR SER LEU VAL ASP ALA ASP ALA ARG ALA PHE
SEQRES 33 D 541 ALA ALA CYS LEU GLY ALA ILE LYS LEU PRO LYS ASN THR
SEQRES 34 D 541 PRO GLU GLU ARG ASP ARG ARG THR CYS ALA LEU GLN GLU
SEQRES 35 D 541 GLY LEU ARG GLN ALA VAL ALA VAL PRO LEU LYS LEU ALA
SEQRES 36 D 541 GLU THR VAL SER GLN LEU TRP PRO ALA LEU GLN GLU LEU
SEQRES 37 D 541 ALA GLN CYS GLY ASN LEU SER CYS LEU SER ASP LEU GLN
SEQRES 38 D 541 VAL ALA ALA LYS ALA LEU GLU THR GLY VAL PHE GLY ALA
SEQRES 39 D 541 TYR PHE ASN VAL LEU ILE ASN LEU LYS ASP MSE THR ASP
SEQRES 40 D 541 ASP VAL PHE LYS GLU LYS THR ARG HIS ARG ILE SER SER
SEQRES 41 D 541 LEU LEU GLN GLU ALA LYS THR GLN ALA ALA LEU VAL LEU
SEQRES 42 D 541 GLY SER LEU GLU ALA ARG LYS GLU
MODRES 2PFD MSE A 75 MET SELENOMETHIONINE
MODRES 2PFD MSE A 85 MET SELENOMETHIONINE
MODRES 2PFD MSE A 101 MET SELENOMETHIONINE
MODRES 2PFD MSE A 132 MET SELENOMETHIONINE
MODRES 2PFD MSE A 373 MET SELENOMETHIONINE
MODRES 2PFD MSE A 377 MET SELENOMETHIONINE
MODRES 2PFD MSE A 391 MET SELENOMETHIONINE
MODRES 2PFD MSE A 505 MET SELENOMETHIONINE
MODRES 2PFD MSE B 75 MET SELENOMETHIONINE
MODRES 2PFD MSE B 85 MET SELENOMETHIONINE
MODRES 2PFD MSE B 101 MET SELENOMETHIONINE
MODRES 2PFD MSE B 132 MET SELENOMETHIONINE
MODRES 2PFD MSE B 373 MET SELENOMETHIONINE
MODRES 2PFD MSE B 377 MET SELENOMETHIONINE
MODRES 2PFD MSE B 391 MET SELENOMETHIONINE
MODRES 2PFD MSE B 505 MET SELENOMETHIONINE
MODRES 2PFD MSE C 75 MET SELENOMETHIONINE
MODRES 2PFD MSE C 85 MET SELENOMETHIONINE
MODRES 2PFD MSE C 101 MET SELENOMETHIONINE
MODRES 2PFD MSE C 132 MET SELENOMETHIONINE
MODRES 2PFD MSE C 373 MET SELENOMETHIONINE
MODRES 2PFD MSE C 377 MET SELENOMETHIONINE
MODRES 2PFD MSE C 391 MET SELENOMETHIONINE
MODRES 2PFD MSE C 505 MET SELENOMETHIONINE
MODRES 2PFD MSE D 75 MET SELENOMETHIONINE
MODRES 2PFD MSE D 85 MET SELENOMETHIONINE
MODRES 2PFD MSE D 101 MET SELENOMETHIONINE
MODRES 2PFD MSE D 132 MET SELENOMETHIONINE
MODRES 2PFD MSE D 373 MET SELENOMETHIONINE
MODRES 2PFD MSE D 377 MET SELENOMETHIONINE
MODRES 2PFD MSE D 391 MET SELENOMETHIONINE
MODRES 2PFD MSE D 505 MET SELENOMETHIONINE
HET MSE A 75 8
HET MSE A 85 8
HET MSE A 101 8
HET MSE A 132 8
HET MSE A 373 8
HET MSE A 377 8
HET MSE A 391 8
HET MSE A 505 8
HET MSE B 75 8
HET MSE B 85 8
HET MSE B 101 8
HET MSE B 132 8
HET MSE B 373 8
HET MSE B 377 8
HET MSE B 391 8
HET MSE B 505 8
HET MSE C 75 8
HET MSE C 85 8
HET MSE C 101 8
HET MSE C 132 8
HET MSE C 373 8
HET MSE C 377 8
HET MSE C 391 8
HET MSE C 505 8
HET MSE D 75 8
HET MSE D 85 8
HET MSE D 101 8
HET MSE D 132 8
HET MSE D 373 8
HET MSE D 377 8
HET MSE D 391 8
HET MSE D 505 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 32(C5 H11 N O2 SE)
HELIX 1 1 ASN A 16 ILE A 27 1 12
HELIX 2 2 GLN A 54 GLN A 71 1 18
HELIX 3 3 LEU A 72 ILE A 73 5 2
HELIX 4 4 ASP A 74 HIS A 78 5 5
HELIX 5 5 SER A 100 ASN A 120 1 21
HELIX 6 6 THR A 137 ARG A 142 1 6
HELIX 7 7 ALA A 148 LEU A 153 1 6
HELIX 8 8 THR A 192 ARG A 204 1 13
HELIX 9 9 ALA A 245 GLU A 259 1 15
HELIX 10 10 PRO A 274 LYS A 290 1 17
HELIX 11 11 GLU A 295 ARG A 306 1 12
HELIX 12 12 ASP A 316 ILE A 321 1 6
HELIX 13 13 ILE A 321 VAL A 326 1 6
HELIX 14 14 SER A 334 ALA A 338 5 5
HELIX 15 15 SER A 339 GLY A 348 1 10
HELIX 16 16 GLY A 356 THR A 378 1 23
HELIX 17 17 PHE A 384 HIS A 386 5 3
HELIX 18 18 LEU A 387 SER A 407 1 21
HELIX 19 19 SER A 407 LYS A 424 1 18
HELIX 20 20 THR A 429 ARG A 433 5 5
HELIX 21 21 ARG A 435 ALA A 469 1 35
HELIX 22 22 CYS A 476 LYS A 503 1 28
HELIX 23 23 ASP A 507 LYS A 540 1 34
HELIX 24 24 ASN B 16 ILE B 27 1 12
HELIX 25 25 GLN B 54 GLN B 71 1 18
HELIX 26 26 LEU B 72 ILE B 73 5 2
HELIX 27 27 ASP B 74 HIS B 78 5 5
HELIX 28 28 SER B 100 ASN B 120 1 21
HELIX 29 29 THR B 137 ARG B 142 1 6
HELIX 30 30 ALA B 148 LEU B 153 1 6
HELIX 31 31 THR B 192 ARG B 204 1 13
HELIX 32 32 ALA B 245 GLU B 259 1 15
HELIX 33 33 PRO B 274 LYS B 290 1 17
HELIX 34 34 GLU B 295 ARG B 306 1 12
HELIX 35 35 ASP B 316 ILE B 321 1 6
HELIX 36 36 ILE B 321 VAL B 326 1 6
HELIX 37 37 SER B 334 ALA B 338 5 5
HELIX 38 38 SER B 339 GLY B 348 1 10
HELIX 39 39 GLY B 356 THR B 378 1 23
HELIX 40 40 PHE B 384 HIS B 386 5 3
HELIX 41 41 LEU B 387 SER B 407 1 21
HELIX 42 42 SER B 407 LYS B 424 1 18
HELIX 43 43 THR B 429 ARG B 433 5 5
HELIX 44 44 ARG B 435 ALA B 469 1 35
HELIX 45 45 CYS B 476 LYS B 503 1 28
HELIX 46 46 ASP B 507 LYS B 540 1 34
HELIX 47 47 ASN C 16 ILE C 27 1 12
HELIX 48 48 GLN C 54 GLN C 71 1 18
HELIX 49 49 LEU C 72 ILE C 73 5 2
HELIX 50 50 ASP C 74 HIS C 78 5 5
HELIX 51 51 SER C 100 ASN C 120 1 21
HELIX 52 52 THR C 137 ARG C 142 1 6
HELIX 53 53 ALA C 148 LEU C 153 1 6
HELIX 54 54 THR C 192 ARG C 204 1 13
HELIX 55 55 ALA C 245 GLU C 259 1 15
HELIX 56 56 PRO C 274 LYS C 290 1 17
HELIX 57 57 GLU C 295 ARG C 306 1 12
HELIX 58 58 ASP C 316 ILE C 321 1 6
HELIX 59 59 ILE C 321 VAL C 326 1 6
HELIX 60 60 SER C 334 ALA C 338 5 5
HELIX 61 61 SER C 339 GLY C 348 1 10
HELIX 62 62 GLY C 356 THR C 378 1 23
HELIX 63 63 PHE C 384 HIS C 386 5 3
HELIX 64 64 LEU C 387 SER C 407 1 21
HELIX 65 65 SER C 407 LYS C 424 1 18
HELIX 66 66 THR C 429 ARG C 433 5 5
HELIX 67 67 ARG C 435 ALA C 469 1 35
HELIX 68 68 CYS C 476 LYS C 503 1 28
HELIX 69 69 ASP C 507 LYS C 540 1 34
HELIX 70 70 ASN D 16 ILE D 27 1 12
HELIX 71 71 GLN D 54 GLN D 71 1 18
HELIX 72 72 LEU D 72 ILE D 73 5 2
HELIX 73 73 ASP D 74 HIS D 78 5 5
HELIX 74 74 SER D 100 ASN D 120 1 21
HELIX 75 75 THR D 137 ARG D 142 1 6
HELIX 76 76 ALA D 148 LEU D 153 1 6
HELIX 77 77 THR D 192 ARG D 204 1 13
HELIX 78 78 ALA D 245 GLU D 259 1 15
HELIX 79 79 PRO D 274 LYS D 290 1 17
HELIX 80 80 GLU D 295 ARG D 306 1 12
HELIX 81 81 ASP D 316 ILE D 321 1 6
HELIX 82 82 ILE D 321 VAL D 326 1 6
HELIX 83 83 SER D 334 ALA D 338 5 5
HELIX 84 84 SER D 339 GLY D 348 1 10
HELIX 85 85 GLY D 356 THR D 378 1 23
HELIX 86 86 PHE D 384 HIS D 386 5 3
HELIX 87 87 LEU D 387 SER D 407 1 21
HELIX 88 88 SER D 407 LYS D 424 1 18
HELIX 89 89 THR D 429 ARG D 433 5 5
HELIX 90 90 ARG D 435 ALA D 469 1 35
HELIX 91 91 CYS D 476 LYS D 503 1 28
HELIX 92 92 ASP D 507 LYS D 540 1 34
SHEET 1 A 4 LEU A 4 CYS A 7 0
SHEET 2 A 4 VAL A 90 ARG A 97 -1 O ILE A 94 N GLU A 6
SHEET 3 A 4 THR A 174 ALA A 178 1 O VAL A 175 N CYS A 91
SHEET 4 A 4 VAL A 123 GLY A 127 1 N TYR A 126 O THR A 176
SHEET 1 B 3 ASN A 10 PHE A 11 0
SHEET 2 B 3 ARG A 46 GLY A 53 -1 O THR A 47 N PHE A 11
SHEET 3 B 3 CYS A 33 GLY A 41 -1 N ASP A 39 O VAL A 48
SHEET 1 C 4 VAL A 219 LEU A 226 0
SHEET 2 C 4 LEU A 231 LEU A 238 -1 O ASN A 237 N GLN A 220
SHEET 3 C 4 ILE A 183 LEU A 189 -1 N PHE A 185 O THR A 236
SHEET 4 C 4 VAL A 264 VAL A 270 -1 O VAL A 265 N ASN A 188
SHEET 1 D 4 LEU B 4 CYS B 7 0
SHEET 2 D 4 VAL B 90 ARG B 97 -1 O ILE B 94 N GLU B 6
SHEET 3 D 4 VAL B 175 ALA B 178 1 O VAL B 175 N CYS B 91
SHEET 4 D 4 TYR B 126 GLY B 127 1 N TYR B 126 O THR B 176
SHEET 1 E 3 ASN B 10 PHE B 11 0
SHEET 2 E 3 ARG B 46 GLY B 53 -1 O THR B 47 N PHE B 11
SHEET 3 E 3 CYS B 33 GLY B 41 -1 N ASP B 39 O VAL B 48
SHEET 1 F 4 VAL B 219 LEU B 226 0
SHEET 2 F 4 LEU B 231 LEU B 238 -1 O ASN B 237 N GLN B 220
SHEET 3 F 4 ILE B 183 LEU B 189 -1 N PHE B 185 O THR B 236
SHEET 4 F 4 VAL B 264 VAL B 270 -1 O VAL B 265 N ASN B 188
SHEET 1 G 4 LEU C 4 CYS C 7 0
SHEET 2 G 4 VAL C 90 ARG C 97 -1 O ILE C 94 N GLU C 6
SHEET 3 G 4 VAL C 175 ALA C 178 1 O VAL C 175 N CYS C 91
SHEET 4 G 4 TYR C 126 GLY C 127 1 N TYR C 126 O THR C 176
SHEET 1 H 3 ASN C 10 PHE C 11 0
SHEET 2 H 3 ARG C 46 GLY C 53 -1 O THR C 47 N PHE C 11
SHEET 3 H 3 CYS C 33 GLY C 41 -1 N ASP C 39 O VAL C 48
SHEET 1 I 4 VAL C 219 LEU C 226 0
SHEET 2 I 4 LEU C 231 LEU C 238 -1 O ASN C 237 N GLN C 220
SHEET 3 I 4 ILE C 183 LEU C 189 -1 N PHE C 185 O THR C 236
SHEET 4 I 4 VAL C 264 VAL C 270 -1 O VAL C 265 N ASN C 188
SHEET 1 J 4 LEU D 4 CYS D 7 0
SHEET 2 J 4 VAL D 90 ARG D 97 -1 O ILE D 94 N GLU D 6
SHEET 3 J 4 THR D 174 ALA D 178 1 O VAL D 175 N CYS D 91
SHEET 4 J 4 VAL D 123 GLY D 127 1 N TYR D 126 O THR D 176
SHEET 1 K 3 ASN D 10 PHE D 11 0
SHEET 2 K 3 ARG D 46 GLY D 53 -1 O THR D 47 N PHE D 11
SHEET 3 K 3 CYS D 33 GLY D 41 -1 N ASP D 39 O VAL D 48
SHEET 1 L 4 VAL D 219 LEU D 226 0
SHEET 2 L 4 LEU D 231 LEU D 238 -1 O ASN D 237 N GLN D 220
SHEET 3 L 4 ILE D 183 LEU D 189 -1 N PHE D 185 O THR D 236
SHEET 4 L 4 VAL D 264 VAL D 270 -1 O VAL D 265 N ASN D 188
LINK C ASP A 74 N MSE A 75 1555 1555 1.33
LINK C MSE A 75 N ARG A 76 1555 1555 1.33
LINK C ARG A 84 N MSE A 85 1555 1555 1.33
LINK C MSE A 85 N GLY A 86 1555 1555 1.33
LINK C SER A 100 N MSE A 101 1555 1555 1.33
LINK C MSE A 101 N ASP A 102 1555 1555 1.33
LINK C GLN A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N PRO A 133 1555 1555 1.35
LINK C SER A 372 N MSE A 373 1555 1555 1.32
LINK C MSE A 373 N VAL A 374 1555 1555 1.32
LINK C GLN A 376 N MSE A 377 1555 1555 1.32
LINK C MSE A 377 N THR A 378 1555 1555 1.33
LINK C THR A 390 N MSE A 391 1555 1555 1.33
LINK C MSE A 391 N ARG A 392 1555 1555 1.33
LINK C ASP A 504 N MSE A 505 1555 1555 1.33
LINK C MSE A 505 N THR A 506 1555 1555 1.33
LINK C ASP B 74 N MSE B 75 1555 1555 1.33
LINK C MSE B 75 N ARG B 76 1555 1555 1.33
LINK C ARG B 84 N MSE B 85 1555 1555 1.33
LINK C MSE B 85 N GLY B 86 1555 1555 1.33
LINK C SER B 100 N MSE B 101 1555 1555 1.33
LINK C MSE B 101 N ASP B 102 1555 1555 1.33
LINK C GLN B 131 N MSE B 132 1555 1555 1.33
LINK C MSE B 132 N PRO B 133 1555 1555 1.35
LINK C SER B 372 N MSE B 373 1555 1555 1.33
LINK C MSE B 373 N VAL B 374 1555 1555 1.32
LINK C GLN B 376 N MSE B 377 1555 1555 1.32
LINK C MSE B 377 N THR B 378 1555 1555 1.33
LINK C THR B 390 N MSE B 391 1555 1555 1.34
LINK C MSE B 391 N ARG B 392 1555 1555 1.33
LINK C ASP B 504 N MSE B 505 1555 1555 1.33
LINK C MSE B 505 N THR B 506 1555 1555 1.33
LINK C ASP C 74 N MSE C 75 1555 1555 1.33
LINK C MSE C 75 N ARG C 76 1555 1555 1.33
LINK C ARG C 84 N MSE C 85 1555 1555 1.33
LINK C MSE C 85 N GLY C 86 1555 1555 1.33
LINK C SER C 100 N MSE C 101 1555 1555 1.33
LINK C MSE C 101 N ASP C 102 1555 1555 1.33
LINK C GLN C 131 N MSE C 132 1555 1555 1.33
LINK C MSE C 132 N PRO C 133 1555 1555 1.35
LINK C SER C 372 N MSE C 373 1555 1555 1.33
LINK C MSE C 373 N VAL C 374 1555 1555 1.33
LINK C GLN C 376 N MSE C 377 1555 1555 1.32
LINK C MSE C 377 N THR C 378 1555 1555 1.32
LINK C THR C 390 N MSE C 391 1555 1555 1.34
LINK C MSE C 391 N ARG C 392 1555 1555 1.34
LINK C ASP C 504 N MSE C 505 1555 1555 1.33
LINK C MSE C 505 N THR C 506 1555 1555 1.33
LINK C ASP D 74 N MSE D 75 1555 1555 1.33
LINK C MSE D 75 N ARG D 76 1555 1555 1.33
LINK C ARG D 84 N MSE D 85 1555 1555 1.33
LINK C MSE D 85 N GLY D 86 1555 1555 1.33
LINK C SER D 100 N MSE D 101 1555 1555 1.33
LINK C MSE D 101 N ASP D 102 1555 1555 1.33
LINK C GLN D 131 N MSE D 132 1555 1555 1.33
LINK C MSE D 132 N PRO D 133 1555 1555 1.35
LINK C SER D 372 N MSE D 373 1555 1555 1.33
LINK C MSE D 373 N VAL D 374 1555 1555 1.32
LINK C GLN D 376 N MSE D 377 1555 1555 1.32
LINK C MSE D 377 N THR D 378 1555 1555 1.33
LINK C THR D 390 N MSE D 391 1555 1555 1.34
LINK C MSE D 391 N ARG D 392 1555 1555 1.33
LINK C ASP D 504 N MSE D 505 1555 1555 1.33
LINK C MSE D 505 N THR D 506 1555 1555 1.33
CRYST1 134.848 134.848 156.365 90.00 90.00 90.00 P 4 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 0.007416 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007416 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006395 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
