HEADER TRANSFERASE 25-AUG-04 1XA3
TITLE CRYSTAL STRUCTURE OF CAIB, A TYPE III COA TRANSFERASE IN
TITLE 2 CARNITINE METABOLISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CROTONOBETAINYL-COA:CARNITINE COA-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.8.3.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: CAIB;
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: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT73.3
KEYWDS CAIB, CARNITINE, COA TRANSFERASE, COA, COENZYME A,
KEYWDS 2 INTERLOCKED, DIMER, BIS-TRIS, STRUCTURAL PROTEOMICS IN
KEYWDS 3 EUROPE, SPINE, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.STENMARK,D.GURMU,P.NORDLUND,STRUCTURAL PROTEOMICS IN
AUTHOR 2 EUROPE (SPINE)
REVDAT 2 24-FEB-09 1XA3 1 VERSN
REVDAT 1 16-NOV-04 1XA3 0
JRNL AUTH P.STENMARK,D.GURMU,P.NORDLUND
JRNL TITL CRYSTAL STRUCTURE OF CAIB, A TYPE-III COA
JRNL TITL 2 TRANSFERASE IN CARNITINE METABOLISM
JRNL REF BIOCHEMISTRY V. 43 13996 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15518548
JRNL DOI 10.1021/BI048481C
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 72842
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3866
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) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4549
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.69000
REMARK 3 B33 (A**2) : -0.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.181
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6447 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5770 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8743 ; 1.485 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13460 ; 0.857 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 798 ; 5.928 ; 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): 938 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7166 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1278 ; 0.008 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1252 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6851 ; 0.247 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3537 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 437 ; 0.145 ; 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): 5 ; 0.246 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.229 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.108 ; 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): 3981 ; 0.893 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6399 ; 1.594 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2466 ; 2.771 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2344 ; 4.228 ; 4.500
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 : 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 : 1.40
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 1XA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB030129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76742
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.760
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : 0.09200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8200
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) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.42
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM SULPHATE,
REMARK 280 GLYCEROL, SODIUM CHLORIDE, BIS-TRIS, PH 5.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 64.90100
REMARK 290 SMTRY3 2 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 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
REMARK 350 TOTAL BURIED SURFACE AREA: 13830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
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 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 -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 THR A -14
REMARK 465 SER A -13
REMARK 465 LEU A -12
REMARK 465 TYR A -11
REMARK 465 LYS A -10
REMARK 465 LYS A -9
REMARK 465 ALA A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 GLU A -5
REMARK 465 THR A -4
REMARK 465 LEU A -3
REMARK 465 TYR A -2
REMARK 465 ILE A -1
REMARK 465 GLN A 0
REMARK 465 GLY A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 GLU A 404
REMARK 465 ASP A 405
REMARK 465 SER A 406
REMARK 465 THR A 407
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 HIS A 411
REMARK 465 HIS A 412
REMARK 465 HIS A 413
REMARK 465 MSE B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 THR B -14
REMARK 465 SER B -13
REMARK 465 LEU B -12
REMARK 465 TYR B -11
REMARK 465 LYS B -10
REMARK 465 LYS B -9
REMARK 465 ALA B -8
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 GLU B -5
REMARK 465 THR B -4
REMARK 465 LEU B -3
REMARK 465 TYR B -2
REMARK 465 ILE B -1
REMARK 465 GLN B 0
REMARK 465 GLY B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 GLU B 404
REMARK 465 ASP B 405
REMARK 465 SER B 406
REMARK 465 THR B 407
REMARK 465 HIS B 408
REMARK 465 HIS B 409
REMARK 465 HIS B 410
REMARK 465 HIS B 411
REMARK 465 HIS B 412
REMARK 465 HIS B 413
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 CG MSE B 32 O HOH B 1875 2.00
REMARK 500 CG MSE A 32 O HOH A 1892 2.05
REMARK 500 O ARG A 283 O HOH A 1893 2.10
REMARK 500 O HOH B 1739 O HOH B 1822 2.14
REMARK 500 O HOH B 1659 O HOH B 1912 2.17
REMARK 500 O HOH B 1752 O HOH B 1809 2.19
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 CYS A 222 CB CYS A 222 SG -0.097
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 ASP A 347 CB - CG - OD2 ANGL. DEV. = 7.7 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 GLU A 23 -124.27 65.60
REMARK 500 ILE A 24 -62.36 -103.52
REMARK 500 ASN A 57 -44.91 -135.48
REMARK 500 ASP A 76 -124.68 48.65
REMARK 500 LEU A 280 118.44 -160.14
REMARK 500 GLU B 23 -130.33 69.51
REMARK 500 ILE B 24 -62.01 -101.33
REMARK 500 ASN B 57 -44.50 -134.61
REMARK 500 ASP B 76 -117.29 44.51
REMARK 500 PRO B 99 49.78 -80.67
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 SO4 A 1501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1502
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 1601
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 1602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XA4 RELATED DB: PDB
REMARK 900 CAIB COMPLEXED WITH COENZYME A
REMARK 900 RELATED ID: AD59 RELATED DB: TARGETDB
DBREF 1XA3 A 2 405 UNP P31572 CAIB_ECOLI 2 405
DBREF 1XA3 B 2 405 UNP P31572 CAIB_ECOLI 2 405
SEQADV 1XA3 MSE A -23 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -22 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -21 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -20 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -19 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -18 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A -17 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY A -16 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER A -15 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR A -14 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER A -13 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LEU A -12 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 TYR A -11 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LYS A -10 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LYS A -9 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 ALA A -8 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY A -7 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER A -6 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLU A -5 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR A -4 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LEU A -3 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 TYR A -2 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 ILE A -1 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLN A 0 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY A 1 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 MSE A 6 UNP P31572 MET 6 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 32 UNP P31572 MET 32 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 86 UNP P31572 MET 86 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 161 UNP P31572 MET 161 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 200 UNP P31572 MET 200 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 204 UNP P31572 MET 204 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 207 UNP P31572 MET 207 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 212 UNP P31572 MET 212 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 213 UNP P31572 MET 213 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 221 UNP P31572 MET 221 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 225 UNP P31572 MET 225 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 248 UNP P31572 MET 248 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 346 UNP P31572 MET 346 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 357 UNP P31572 MET 357 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 371 UNP P31572 MET 371 MODIFIED RESIDUE
SEQADV 1XA3 MSE A 376 UNP P31572 MET 376 MODIFIED RESIDUE
SEQADV 1XA3 SER A 406 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR A 407 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 408 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 409 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 410 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 411 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 412 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS A 413 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 MSE B -23 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -22 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -21 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -20 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -19 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -18 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B -17 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY B -16 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER B -15 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR B -14 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER B -13 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LEU B -12 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 TYR B -11 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LYS B -10 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LYS B -9 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 ALA B -8 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY B -7 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 SER B -6 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLU B -5 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR B -4 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 LEU B -3 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 TYR B -2 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 ILE B -1 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLN B 0 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 GLY B 1 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 MSE B 6 UNP P31572 MET 6 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 32 UNP P31572 MET 32 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 86 UNP P31572 MET 86 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 161 UNP P31572 MET 161 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 200 UNP P31572 MET 200 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 204 UNP P31572 MET 204 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 207 UNP P31572 MET 207 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 212 UNP P31572 MET 212 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 213 UNP P31572 MET 213 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 221 UNP P31572 MET 221 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 225 UNP P31572 MET 225 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 248 UNP P31572 MET 248 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 346 UNP P31572 MET 346 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 357 UNP P31572 MET 357 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 371 UNP P31572 MET 371 MODIFIED RESIDUE
SEQADV 1XA3 MSE B 376 UNP P31572 MET 376 MODIFIED RESIDUE
SEQADV 1XA3 SER B 406 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 THR B 407 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 408 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 409 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 410 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 411 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 412 UNP P31572 EXPRESSION TAG
SEQADV 1XA3 HIS B 413 UNP P31572 EXPRESSION TAG
SEQRES 1 A 437 MSE HIS HIS HIS HIS HIS HIS GLY SER THR SER LEU TYR
SEQRES 2 A 437 LYS LYS ALA GLY SER GLU THR LEU TYR ILE GLN GLY ASP
SEQRES 3 A 437 HIS LEU PRO MSE PRO LYS PHE GLY PRO LEU ALA GLY LEU
SEQRES 4 A 437 ARG VAL VAL PHE SER GLY ILE GLU ILE ALA GLY PRO PHE
SEQRES 5 A 437 ALA GLY GLN MSE PHE ALA GLU TRP GLY ALA GLU VAL ILE
SEQRES 6 A 437 TRP ILE GLU ASN VAL ALA TRP ALA ASP THR ILE ARG VAL
SEQRES 7 A 437 GLN PRO ASN TYR PRO GLN LEU SER ARG ARG ASN LEU HIS
SEQRES 8 A 437 ALA LEU SER LEU ASN ILE PHE LYS ASP GLU GLY ARG GLU
SEQRES 9 A 437 ALA PHE LEU LYS LEU MSE GLU THR THR ASP ILE PHE ILE
SEQRES 10 A 437 GLU ALA SER LYS GLY PRO ALA PHE ALA ARG ARG GLY ILE
SEQRES 11 A 437 THR ASP GLU VAL LEU TRP GLN HIS ASN PRO LYS LEU VAL
SEQRES 12 A 437 ILE ALA HIS LEU SER GLY PHE GLY GLN TYR GLY THR GLU
SEQRES 13 A 437 GLU TYR THR ASN LEU PRO ALA TYR ASN THR ILE ALA GLN
SEQRES 14 A 437 ALA PHE SER GLY TYR LEU ILE GLN ASN GLY ASP VAL ASP
SEQRES 15 A 437 GLN PRO MSE PRO ALA PHE PRO TYR THR ALA ASP TYR PHE
SEQRES 16 A 437 SER GLY LEU THR ALA THR THR ALA ALA LEU ALA ALA LEU
SEQRES 17 A 437 HIS LYS VAL ARG GLU THR GLY LYS GLY GLU SER ILE ASP
SEQRES 18 A 437 ILE ALA MSE TYR GLU VAL MSE LEU ARG MSE GLY GLN TYR
SEQRES 19 A 437 PHE MSE MSE ASP TYR PHE ASN GLY GLY GLU MSE CYS PRO
SEQRES 20 A 437 ARG MSE SER LYS GLY LYS ASP PRO TYR TYR ALA GLY CYS
SEQRES 21 A 437 GLY LEU TYR LYS CYS ALA ASP GLY TYR ILE VAL MSE GLU
SEQRES 22 A 437 LEU VAL GLY ILE THR GLN ILE GLU GLU CYS PHE LYS ASP
SEQRES 23 A 437 ILE GLY LEU ALA HIS LEU LEU GLY THR PRO GLU ILE PRO
SEQRES 24 A 437 GLU GLY THR GLN LEU ILE HIS ARG ILE GLU CYS PRO TYR
SEQRES 25 A 437 GLY PRO LEU VAL GLU GLU LYS LEU ASP ALA TRP LEU ALA
SEQRES 26 A 437 THR HIS THR ILE ALA GLU VAL LYS GLU ARG PHE ALA GLU
SEQRES 27 A 437 LEU ASN ILE ALA CYS ALA LYS VAL LEU THR VAL PRO GLU
SEQRES 28 A 437 LEU GLU SER ASN PRO GLN TYR VAL ALA ARG GLU SER ILE
SEQRES 29 A 437 THR GLN TRP GLN THR MSE ASP GLY ARG THR CYS LYS GLY
SEQRES 30 A 437 PRO ASN ILE MSE PRO LYS PHE LYS ASN ASN PRO GLY GLN
SEQRES 31 A 437 ILE TRP ARG GLY MSE PRO SER HIS GLY MSE ASP THR ALA
SEQRES 32 A 437 ALA ILE LEU LYS ASN ILE GLY TYR SER GLU ASN ASP ILE
SEQRES 33 A 437 GLN GLU LEU VAL SER LYS GLY LEU ALA LYS VAL GLU ASP
SEQRES 34 A 437 SER THR HIS HIS HIS HIS HIS HIS
SEQRES 1 B 437 MSE HIS HIS HIS HIS HIS HIS GLY SER THR SER LEU TYR
SEQRES 2 B 437 LYS LYS ALA GLY SER GLU THR LEU TYR ILE GLN GLY ASP
SEQRES 3 B 437 HIS LEU PRO MSE PRO LYS PHE GLY PRO LEU ALA GLY LEU
SEQRES 4 B 437 ARG VAL VAL PHE SER GLY ILE GLU ILE ALA GLY PRO PHE
SEQRES 5 B 437 ALA GLY GLN MSE PHE ALA GLU TRP GLY ALA GLU VAL ILE
SEQRES 6 B 437 TRP ILE GLU ASN VAL ALA TRP ALA ASP THR ILE ARG VAL
SEQRES 7 B 437 GLN PRO ASN TYR PRO GLN LEU SER ARG ARG ASN LEU HIS
SEQRES 8 B 437 ALA LEU SER LEU ASN ILE PHE LYS ASP GLU GLY ARG GLU
SEQRES 9 B 437 ALA PHE LEU LYS LEU MSE GLU THR THR ASP ILE PHE ILE
SEQRES 10 B 437 GLU ALA SER LYS GLY PRO ALA PHE ALA ARG ARG GLY ILE
SEQRES 11 B 437 THR ASP GLU VAL LEU TRP GLN HIS ASN PRO LYS LEU VAL
SEQRES 12 B 437 ILE ALA HIS LEU SER GLY PHE GLY GLN TYR GLY THR GLU
SEQRES 13 B 437 GLU TYR THR ASN LEU PRO ALA TYR ASN THR ILE ALA GLN
SEQRES 14 B 437 ALA PHE SER GLY TYR LEU ILE GLN ASN GLY ASP VAL ASP
SEQRES 15 B 437 GLN PRO MSE PRO ALA PHE PRO TYR THR ALA ASP TYR PHE
SEQRES 16 B 437 SER GLY LEU THR ALA THR THR ALA ALA LEU ALA ALA LEU
SEQRES 17 B 437 HIS LYS VAL ARG GLU THR GLY LYS GLY GLU SER ILE ASP
SEQRES 18 B 437 ILE ALA MSE TYR GLU VAL MSE LEU ARG MSE GLY GLN TYR
SEQRES 19 B 437 PHE MSE MSE ASP TYR PHE ASN GLY GLY GLU MSE CYS PRO
SEQRES 20 B 437 ARG MSE SER LYS GLY LYS ASP PRO TYR TYR ALA GLY CYS
SEQRES 21 B 437 GLY LEU TYR LYS CYS ALA ASP GLY TYR ILE VAL MSE GLU
SEQRES 22 B 437 LEU VAL GLY ILE THR GLN ILE GLU GLU CYS PHE LYS ASP
SEQRES 23 B 437 ILE GLY LEU ALA HIS LEU LEU GLY THR PRO GLU ILE PRO
SEQRES 24 B 437 GLU GLY THR GLN LEU ILE HIS ARG ILE GLU CYS PRO TYR
SEQRES 25 B 437 GLY PRO LEU VAL GLU GLU LYS LEU ASP ALA TRP LEU ALA
SEQRES 26 B 437 THR HIS THR ILE ALA GLU VAL LYS GLU ARG PHE ALA GLU
SEQRES 27 B 437 LEU ASN ILE ALA CYS ALA LYS VAL LEU THR VAL PRO GLU
SEQRES 28 B 437 LEU GLU SER ASN PRO GLN TYR VAL ALA ARG GLU SER ILE
SEQRES 29 B 437 THR GLN TRP GLN THR MSE ASP GLY ARG THR CYS LYS GLY
SEQRES 30 B 437 PRO ASN ILE MSE PRO LYS PHE LYS ASN ASN PRO GLY GLN
SEQRES 31 B 437 ILE TRP ARG GLY MSE PRO SER HIS GLY MSE ASP THR ALA
SEQRES 32 B 437 ALA ILE LEU LYS ASN ILE GLY TYR SER GLU ASN ASP ILE
SEQRES 33 B 437 GLN GLU LEU VAL SER LYS GLY LEU ALA LYS VAL GLU ASP
SEQRES 34 B 437 SER THR HIS HIS HIS HIS HIS HIS
MODRES 1XA3 MSE A 6 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 32 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 86 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 161 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 200 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 204 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 207 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 212 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 213 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 221 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 225 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 248 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 346 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 357 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 371 MET SELENOMETHIONINE
MODRES 1XA3 MSE A 376 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 6 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 32 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 86 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 161 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 200 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 204 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 207 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 212 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 213 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 221 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 225 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 248 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 346 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 357 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 371 MET SELENOMETHIONINE
MODRES 1XA3 MSE B 376 MET SELENOMETHIONINE
HET MSE A 6 8
HET MSE A 32 8
HET MSE A 86 8
HET MSE A 161 8
HET MSE A 200 8
HET MSE A 204 8
HET MSE A 207 8
HET MSE A 212 8
HET MSE A 213 8
HET MSE A 221 8
HET MSE A 225 8
HET MSE A 248 8
HET MSE A 346 8
HET MSE A 357 8
HET MSE A 371 8
HET MSE A 376 8
HET MSE B 6 8
HET MSE B 32 8
HET MSE B 86 8
HET MSE B 161 8
HET MSE B 200 8
HET MSE B 204 8
HET MSE B 207 8
HET MSE B 212 8
HET MSE B 213 8
HET MSE B 221 8
HET MSE B 225 8
HET MSE B 248 8
HET MSE B 346 8
HET MSE B 357 8
HET MSE B 371 8
HET MSE B 376 8
HET SO4 A1501 5
HET SO4 B1502 5
HET BTB A1601 14
HET BTB B1602 14
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETSYN BTB BIS-TRIS BUFFER
FORMUL 1 MSE 32(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 BTB 2(C8 H19 N O5)
FORMUL 7 HOH *640(H2 O)
HELIX 1 1 ILE A 24 TRP A 36 1 13
HELIX 2 2 ASP A 50 GLN A 55 5 6
HELIX 3 3 ASN A 57 ARG A 63 1 7
HELIX 4 4 LYS A 75 GLU A 87 1 13
HELIX 5 5 PRO A 99 ARG A 104 1 6
HELIX 6 6 THR A 107 ASN A 115 1 9
HELIX 7 7 TYR A 140 SER A 148 1 9
HELIX 8 8 TYR A 150 GLN A 153 5 4
HELIX 9 9 TYR A 166 GLY A 191 1 26
HELIX 10 10 MSE A 200 GLY A 208 1 9
HELIX 11 11 GLY A 208 ASN A 217 1 10
HELIX 12 12 GLY A 252 GLY A 264 1 13
HELIX 13 13 LEU A 265 LEU A 269 5 5
HELIX 14 14 TYR A 288 THR A 302 1 15
HELIX 15 15 THR A 304 ASN A 316 1 13
HELIX 16 16 THR A 324 LEU A 328 5 5
HELIX 17 17 ASN A 331 GLU A 338 1 8
HELIX 18 18 ASP A 377 ILE A 385 1 9
HELIX 19 19 SER A 388 LYS A 398 1 11
HELIX 20 20 ILE B 24 TRP B 36 1 13
HELIX 21 21 ASP B 50 GLN B 55 5 6
HELIX 22 22 ASN B 57 ARG B 63 1 7
HELIX 23 23 LYS B 75 GLU B 87 1 13
HELIX 24 24 PRO B 99 ARG B 104 1 6
HELIX 25 25 THR B 107 ASN B 115 1 9
HELIX 26 26 TYR B 140 SER B 148 1 9
HELIX 27 27 TYR B 150 GLN B 153 5 4
HELIX 28 28 TYR B 166 GLY B 191 1 26
HELIX 29 29 MSE B 200 GLY B 208 1 9
HELIX 30 30 GLY B 208 ASN B 217 1 10
HELIX 31 31 GLY B 252 GLY B 264 1 13
HELIX 32 32 LEU B 265 LEU B 269 5 5
HELIX 33 33 TYR B 288 THR B 302 1 15
HELIX 34 34 THR B 304 ASN B 316 1 13
HELIX 35 35 THR B 324 LEU B 328 5 5
HELIX 36 36 ASN B 331 GLU B 338 1 8
HELIX 37 37 ASP B 377 ILE B 385 1 9
HELIX 38 38 SER B 388 GLY B 399 1 12
SHEET 1 A 8 ALA A 401 LYS A 402 0
SHEET 2 A 8 HIS A 67 LEU A 71 -1 N SER A 70 O LYS A 402
SHEET 3 A 8 GLU A 39 GLU A 44 1 N TRP A 42 O HIS A 67
SHEET 4 A 8 ARG A 16 SER A 20 1 N VAL A 17 O GLU A 39
SHEET 5 A 8 ILE A 91 ALA A 95 1 O ILE A 93 N SER A 20
SHEET 6 A 8 VAL A 119 SER A 124 1 O VAL A 119 N PHE A 92
SHEET 7 A 8 GLU A 194 ALA A 199 1 O ILE A 196 N HIS A 122
SHEET 8 A 8 LYS B 359 PHE B 360 -1 O LYS B 359 N ASP A 197
SHEET 1 B 2 GLY A 155 ASP A 156 0
SHEET 2 B 2 GLN A 159 PRO A 160 -1 O GLN A 159 N ASP A 156
SHEET 1 C 3 CYS A 236 CYS A 241 0
SHEET 2 C 3 GLY A 244 GLU A 249 -1 O GLY A 244 N CYS A 241
SHEET 3 C 3 ALA A 318 LYS A 321 -1 O ALA A 320 N VAL A 247
SHEET 1 D 2 ILE A 340 GLN A 344 0
SHEET 2 D 2 THR A 350 PRO A 354 -1 O GLY A 353 N THR A 341
SHEET 1 E 8 LYS A 359 PHE A 360 0
SHEET 2 E 8 GLU B 194 ALA B 199 -1 O ASP B 197 N LYS A 359
SHEET 3 E 8 VAL B 119 SER B 124 1 N HIS B 122 O ILE B 196
SHEET 4 E 8 ILE B 91 ALA B 95 1 N PHE B 92 O ALA B 121
SHEET 5 E 8 ARG B 16 SER B 20 1 N VAL B 18 O ILE B 91
SHEET 6 E 8 GLU B 39 GLU B 44 1 O GLU B 39 N VAL B 17
SHEET 7 E 8 HIS B 67 LEU B 71 1 O HIS B 67 N TRP B 42
SHEET 8 E 8 ALA B 401 LYS B 402 -1 O LYS B 402 N SER B 70
SHEET 1 F 2 GLY B 155 ASP B 156 0
SHEET 2 F 2 GLN B 159 PRO B 160 -1 O GLN B 159 N ASP B 156
SHEET 1 G 3 CYS B 236 CYS B 241 0
SHEET 2 G 3 GLY B 244 GLU B 249 -1 O GLY B 244 N CYS B 241
SHEET 3 G 3 ALA B 318 LYS B 321 -1 O ALA B 320 N VAL B 247
SHEET 1 H 2 ILE B 340 GLN B 344 0
SHEET 2 H 2 THR B 350 PRO B 354 -1 O CYS B 351 N TRP B 343
LINK C PRO A 5 N MSE A 6 1555 1555 1.33
LINK C MSE A 6 N PRO A 7 1555 1555 1.32
LINK C GLN A 31 N MSE A 32 1555 1555 1.34
LINK C MSE A 32 N PHE A 33 1555 1555 1.32
LINK C LEU A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N GLU A 87 1555 1555 1.34
LINK C PRO A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N PRO A 162 1555 1555 1.32
LINK C ALA A 199 N MSE A 200 1555 1555 1.32
LINK C MSE A 200 N TYR A 201 1555 1555 1.34
LINK C VAL A 203 N MSE A 204 1555 1555 1.32
LINK C MSE A 204 N LEU A 205 1555 1555 1.35
LINK C ARG A 206 N MSE A 207 1555 1555 1.33
LINK C MSE A 207 N GLY A 208 1555 1555 1.34
LINK C PHE A 211 N MSE A 212 1555 1555 1.34
LINK C MSE A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N ASP A 214 1555 1555 1.33
LINK C GLU A 220 N MSE A 221 1555 1555 1.32
LINK C MSE A 221 N CYS A 222 1555 1555 1.31
LINK C ARG A 224 N MSE A 225 1555 1555 1.33
LINK C MSE A 225 N SER A 226 1555 1555 1.33
LINK C VAL A 247 N MSE A 248 1555 1555 1.33
LINK C MSE A 248 N GLU A 249 1555 1555 1.32
LINK C THR A 345 N MSE A 346 1555 1555 1.32
LINK C MSE A 346 N ASP A 347 1555 1555 1.34
LINK C ILE A 356 N MSE A 357 1555 1555 1.34
LINK C MSE A 357 N PRO A 358 1555 1555 1.33
LINK C GLY A 370 N MSE A 371 1555 1555 1.32
LINK C MSE A 371 N PRO A 372 1555 1555 1.32
LINK C GLY A 375 N MSE A 376 1555 1555 1.33
LINK C MSE A 376 N ASP A 377 1555 1555 1.32
LINK C PRO B 5 N MSE B 6 1555 1555 1.33
LINK C MSE B 6 N PRO B 7 1555 1555 1.32
LINK C GLN B 31 N MSE B 32 1555 1555 1.35
LINK C MSE B 32 N PHE B 33 1555 1555 1.33
LINK C LEU B 85 N MSE B 86 1555 1555 1.34
LINK C MSE B 86 N GLU B 87 1555 1555 1.34
LINK C PRO B 160 N MSE B 161 1555 1555 1.33
LINK C MSE B 161 N PRO B 162 1555 1555 1.32
LINK C ALA B 199 N MSE B 200 1555 1555 1.32
LINK C MSE B 200 N TYR B 201 1555 1555 1.33
LINK C VAL B 203 N MSE B 204 1555 1555 1.34
LINK C MSE B 204 N LEU B 205 1555 1555 1.34
LINK C ARG B 206 N MSE B 207 1555 1555 1.32
LINK C MSE B 207 N GLY B 208 1555 1555 1.34
LINK C PHE B 211 N MSE B 212 1555 1555 1.34
LINK C MSE B 212 N MSE B 213 1555 1555 1.32
LINK C MSE B 213 N ASP B 214 1555 1555 1.33
LINK C GLU B 220 N MSE B 221 1555 1555 1.33
LINK C MSE B 221 N CYS B 222 1555 1555 1.34
LINK C ARG B 224 N MSE B 225 1555 1555 1.33
LINK C MSE B 225 N SER B 226 1555 1555 1.32
LINK C VAL B 247 N MSE B 248 1555 1555 1.32
LINK C MSE B 248 N GLU B 249 1555 1555 1.33
LINK C THR B 345 N MSE B 346 1555 1555 1.32
LINK C MSE B 346 N ASP B 347 1555 1555 1.34
LINK C ILE B 356 N MSE B 357 1555 1555 1.33
LINK C MSE B 357 N PRO B 358 1555 1555 1.32
LINK C GLY B 370 N MSE B 371 1555 1555 1.33
LINK C MSE B 371 N PRO B 372 1555 1555 1.32
LINK C GLY B 375 N MSE B 376 1555 1555 1.33
LINK C MSE B 376 N ASP B 377 1555 1555 1.34
CISPEP 1 PHE A 164 PRO A 165 0 -4.77
CISPEP 2 MSE A 357 PRO A 358 0 -9.56
CISPEP 3 PHE B 164 PRO B 165 0 -4.08
CISPEP 4 MSE B 357 PRO B 358 0 -10.54
SITE 1 AC1 6 SER A 96 LYS A 97 ARG A 104 HOH A1686
SITE 2 AC1 6 HOH A1767 HOH A1771
SITE 1 AC2 4 LYS B 97 ALA B 100 ARG B 103 ARG B 104
SITE 1 AC3 12 TYR A 210 ASP A 230 TYR A 233 GLU A 249
SITE 2 AC3 12 HOH A1657 HOH A1658 HOH A1829 GLU B 23
SITE 3 AC3 12 TYR B 140 TYR B 166 HOH B1621 HOH B1861
SITE 1 AC4 10 GLU A 23 TYR A 140 TYR A 166 TYR B 210
SITE 2 AC4 10 ASP B 230 GLU B 249 VAL B 251 HOH B1606
SITE 3 AC4 10 HOH B1638 HOH B1721
CRYST1 55.580 129.802 69.792 90.00 109.48 90.00 P 1 21 1 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 0.017992 0.000000 0.006365 0.00000
SCALE2 0.000000 0.007704 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
