HEADER TRANSFERASE 13-JAN-15 4XL2
TITLE CRYSTAL STRUCTURE OF OXIDIZED FORM OF THIOLASE FROM CLOSTRIDIUM
TITLE 2 ACETOBUTYLICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACETOACETYL-COA THIOLASE;
COMPND 5 EC: 2.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM (STRAIN ATCC 824 /
SOURCE 3 DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787);
SOURCE 4 ORGANISM_TAXID: 272562;
SOURCE 5 STRAIN: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
SOURCE 6 GENE: THLA, THL, CA_C2873;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KIM,S.C.HA,J.W.AHN,E.J.KIM,J.H.LIM,K.J.KIM
REVDAT 3 08-NOV-23 4XL2 1 REMARK
REVDAT 2 17-OCT-18 4XL2 1 REMARK
REVDAT 1 07-OCT-15 4XL2 0
JRNL AUTH S.KIM,Y.S.JANG,S.C.HA,J.W.AHN,E.J.KIM,J.HONG LIM,C.CHO,
JRNL AUTH 2 Y.SHIN RYU,S.KUK LEE,S.Y.LEE,K.J.KIM
JRNL TITL REDOX-SWITCH REGULATORY MECHANISM OF THIOLASE FROM
JRNL TITL 2 CLOSTRIDIUM ACETOBUTYLICUM
JRNL REF NAT COMMUN V. 6 8410 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26391388
JRNL DOI 10.1038/NCOMMS9410
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 73992
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3911
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4975
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 234
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 488
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.69000
REMARK 3 B22 (A**2) : 3.20000
REMARK 3 B33 (A**2) : -1.51000
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): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5889 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5901 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7921 ; 1.811 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13602 ; 0.893 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 778 ; 6.538 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;36.594 ;25.495
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1047 ;15.176 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;13.394 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 905 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6674 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1196 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3105 ; 2.719 ; 2.839
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3102 ; 2.714 ; 2.837
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3884 ; 3.816 ; 4.234
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3885 ; 3.815 ; 4.236
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2784 ; 3.931 ; 3.395
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2784 ; 3.919 ; 3.395
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4038 ; 5.910 ; 4.838
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6968 ; 7.697 ;24.120
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6756 ; 7.577 ;23.748
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.23985
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79061
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1DLV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, K-CITRATE, NACL, PH 4.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 -1.000000 0.000000 0.000000 101.61350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.99350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 101.61350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.99350
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: TETRAMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 GLY A 282
REMARK 465 VAL A 283
REMARK 465 ASP A 284
REMARK 465 PRO A 285
REMARK 465 ALA A 286
REMARK 465 ILE A 287
REMARK 465 MET A 288
REMARK 465 GLY A 289
REMARK 465 TYR A 290
REMARK 465 GLU A 394
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 GLY B 282
REMARK 465 VAL B 283
REMARK 465 ASP B 284
REMARK 465 PRO B 285
REMARK 465 ALA B 286
REMARK 465 ILE B 287
REMARK 465 MET B 288
REMARK 465 GLY B 289
REMARK 465 TYR B 290
REMARK 465 GLU B 394
REMARK 465 HIS B 395
REMARK 465 HIS B 396
REMARK 465 HIS B 397
REMARK 465 HIS B 398
REMARK 465 HIS B 399
REMARK 465 HIS B 400
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 B 167 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 167 NE - CZ - NH2 ANGL. DEV. = -3.6 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 LYS A 19 -117.29 -117.32
REMARK 500 ASN A 64 70.57 48.71
REMARK 500 VAL A 87 -121.68 50.06
REMARK 500 ARG A 133 -63.30 70.01
REMARK 500 ARG A 133 -53.42 64.25
REMARK 500 GLU A 317 66.81 -118.70
REMARK 500 CYS A 378 157.61 73.53
REMARK 500 LYS B 19 -115.76 -114.73
REMARK 500 ASN B 64 70.51 50.32
REMARK 500 VAL B 87 -122.67 51.36
REMARK 500 ARG B 133 -62.09 67.64
REMARK 500 ARG B 133 -56.86 74.32
REMARK 500 CYS B 378 154.51 73.29
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 PRO A 349 ILE A 350 -149.31
REMARK 500 PRO B 349 ILE B 350 -148.81
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 ACT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XL3 RELATED DB: PDB
REMARK 900 RELATED ID: 4XL4 RELATED DB: PDB
DBREF 4XL2 A 1 392 UNP P45359 THLA_CLOAB 1 392
DBREF 4XL2 B 1 392 UNP P45359 THLA_CLOAB 1 392
SEQADV 4XL2 LEU A 393 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 GLU A 394 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 395 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 396 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 397 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 398 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 399 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS A 400 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 LEU B 393 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 GLU B 394 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 395 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 396 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 397 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 398 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 399 UNP P45359 EXPRESSION TAG
SEQADV 4XL2 HIS B 400 UNP P45359 EXPRESSION TAG
SEQRES 1 A 400 MET LYS GLU VAL VAL ILE ALA SER ALA VAL ARG THR ALA
SEQRES 2 A 400 ILE GLY SER TYR GLY LYS SER LEU LYS ASP VAL PRO ALA
SEQRES 3 A 400 VAL ASP LEU GLY ALA THR ALA ILE LYS GLU ALA VAL LYS
SEQRES 4 A 400 LYS ALA GLY ILE LYS PRO GLU ASP VAL ASN GLU VAL ILE
SEQRES 5 A 400 LEU GLY ASN VAL LEU GLN ALA GLY LEU GLY GLN ASN PRO
SEQRES 6 A 400 ALA ARG GLN ALA SER PHE LYS ALA GLY LEU PRO VAL GLU
SEQRES 7 A 400 ILE PRO ALA MET THR ILE ASN LYS VAL CYS GLY SER GLY
SEQRES 8 A 400 LEU ARG THR VAL SER LEU ALA ALA GLN ILE ILE LYS ALA
SEQRES 9 A 400 GLY ASP ALA ASP VAL ILE ILE ALA GLY GLY MET GLU ASN
SEQRES 10 A 400 MET SER ARG ALA PRO TYR LEU ALA ASN ASN ALA ARG TRP
SEQRES 11 A 400 GLY TYR ARG MET GLY ASN ALA LYS PHE VAL ASP GLU MET
SEQRES 12 A 400 ILE THR ASP GLY LEU TRP ASP ALA PHE ASN ASP TYR HIS
SEQRES 13 A 400 MET GLY ILE THR ALA GLU ASN ILE ALA GLU ARG TRP ASN
SEQRES 14 A 400 ILE SER ARG GLU GLU GLN ASP GLU PHE ALA LEU ALA SER
SEQRES 15 A 400 GLN LYS LYS ALA GLU GLU ALA ILE LYS SER GLY GLN PHE
SEQRES 16 A 400 LYS ASP GLU ILE VAL PRO VAL VAL ILE LYS GLY ARG LYS
SEQRES 17 A 400 GLY GLU THR VAL VAL ASP THR ASP GLU HIS PRO ARG PHE
SEQRES 18 A 400 GLY SER THR ILE GLU GLY LEU ALA LYS LEU LYS PRO ALA
SEQRES 19 A 400 PHE LYS LYS ASP GLY THR VAL THR ALA GLY ASN ALA SER
SEQRES 20 A 400 GLY LEU ASN ASP CYS ALA ALA VAL LEU VAL ILE MET SER
SEQRES 21 A 400 ALA GLU LYS ALA LYS GLU LEU GLY VAL LYS PRO LEU ALA
SEQRES 22 A 400 LYS ILE VAL SER TYR GLY SER ALA GLY VAL ASP PRO ALA
SEQRES 23 A 400 ILE MET GLY TYR GLY PRO PHE TYR ALA THR LYS ALA ALA
SEQRES 24 A 400 ILE GLU LYS ALA GLY TRP THR VAL ASP GLU LEU ASP LEU
SEQRES 25 A 400 ILE GLU SER ASN GLU ALA PHE ALA ALA GLN SER LEU ALA
SEQRES 26 A 400 VAL ALA LYS ASP LEU LYS PHE ASP MET ASN LYS VAL ASN
SEQRES 27 A 400 VAL ASN GLY GLY ALA ILE ALA LEU GLY HIS PRO ILE GLY
SEQRES 28 A 400 ALA SER GLY ALA ARG ILE LEU VAL THR LEU VAL HIS ALA
SEQRES 29 A 400 MET GLN LYS ARG ASP ALA LYS LYS GLY LEU ALA THR LEU
SEQRES 30 A 400 CYS ILE GLY GLY GLY GLN GLY THR ALA ILE LEU LEU GLU
SEQRES 31 A 400 LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 400 MET LYS GLU VAL VAL ILE ALA SER ALA VAL ARG THR ALA
SEQRES 2 B 400 ILE GLY SER TYR GLY LYS SER LEU LYS ASP VAL PRO ALA
SEQRES 3 B 400 VAL ASP LEU GLY ALA THR ALA ILE LYS GLU ALA VAL LYS
SEQRES 4 B 400 LYS ALA GLY ILE LYS PRO GLU ASP VAL ASN GLU VAL ILE
SEQRES 5 B 400 LEU GLY ASN VAL LEU GLN ALA GLY LEU GLY GLN ASN PRO
SEQRES 6 B 400 ALA ARG GLN ALA SER PHE LYS ALA GLY LEU PRO VAL GLU
SEQRES 7 B 400 ILE PRO ALA MET THR ILE ASN LYS VAL CYS GLY SER GLY
SEQRES 8 B 400 LEU ARG THR VAL SER LEU ALA ALA GLN ILE ILE LYS ALA
SEQRES 9 B 400 GLY ASP ALA ASP VAL ILE ILE ALA GLY GLY MET GLU ASN
SEQRES 10 B 400 MET SER ARG ALA PRO TYR LEU ALA ASN ASN ALA ARG TRP
SEQRES 11 B 400 GLY TYR ARG MET GLY ASN ALA LYS PHE VAL ASP GLU MET
SEQRES 12 B 400 ILE THR ASP GLY LEU TRP ASP ALA PHE ASN ASP TYR HIS
SEQRES 13 B 400 MET GLY ILE THR ALA GLU ASN ILE ALA GLU ARG TRP ASN
SEQRES 14 B 400 ILE SER ARG GLU GLU GLN ASP GLU PHE ALA LEU ALA SER
SEQRES 15 B 400 GLN LYS LYS ALA GLU GLU ALA ILE LYS SER GLY GLN PHE
SEQRES 16 B 400 LYS ASP GLU ILE VAL PRO VAL VAL ILE LYS GLY ARG LYS
SEQRES 17 B 400 GLY GLU THR VAL VAL ASP THR ASP GLU HIS PRO ARG PHE
SEQRES 18 B 400 GLY SER THR ILE GLU GLY LEU ALA LYS LEU LYS PRO ALA
SEQRES 19 B 400 PHE LYS LYS ASP GLY THR VAL THR ALA GLY ASN ALA SER
SEQRES 20 B 400 GLY LEU ASN ASP CYS ALA ALA VAL LEU VAL ILE MET SER
SEQRES 21 B 400 ALA GLU LYS ALA LYS GLU LEU GLY VAL LYS PRO LEU ALA
SEQRES 22 B 400 LYS ILE VAL SER TYR GLY SER ALA GLY VAL ASP PRO ALA
SEQRES 23 B 400 ILE MET GLY TYR GLY PRO PHE TYR ALA THR LYS ALA ALA
SEQRES 24 B 400 ILE GLU LYS ALA GLY TRP THR VAL ASP GLU LEU ASP LEU
SEQRES 25 B 400 ILE GLU SER ASN GLU ALA PHE ALA ALA GLN SER LEU ALA
SEQRES 26 B 400 VAL ALA LYS ASP LEU LYS PHE ASP MET ASN LYS VAL ASN
SEQRES 27 B 400 VAL ASN GLY GLY ALA ILE ALA LEU GLY HIS PRO ILE GLY
SEQRES 28 B 400 ALA SER GLY ALA ARG ILE LEU VAL THR LEU VAL HIS ALA
SEQRES 29 B 400 MET GLN LYS ARG ASP ALA LYS LYS GLY LEU ALA THR LEU
SEQRES 30 B 400 CYS ILE GLY GLY GLY GLN GLY THR ALA ILE LEU LEU GLU
SEQRES 31 B 400 LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
HET ACT A 501 4
HET PEG A 502 7
HET PEG A 503 7
HET PEG A 504 7
HET PEG A 505 7
HET GOL A 506 6
HET ACT B 501 4
HET PEG B 502 7
HET PEG B 503 7
HET PEG B 504 7
HET PEG B 505 7
HET GOL B 506 6
HETNAM ACT ACETATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 PEG 8(C4 H10 O3)
FORMUL 8 GOL 2(C3 H8 O3)
FORMUL 15 HOH *488(H2 O)
HELIX 1 AA1 PRO A 25 GLY A 42 1 18
HELIX 2 AA2 LYS A 44 VAL A 48 5 5
HELIX 3 AA3 ASN A 64 ALA A 73 1 10
HELIX 4 AA4 LYS A 86 CYS A 88 5 3
HELIX 5 AA5 GLY A 89 ALA A 104 1 16
HELIX 6 AA6 GLU A 142 LEU A 148 1 7
HELIX 7 AA7 MET A 157 ASN A 169 1 13
HELIX 8 AA8 SER A 171 SER A 192 1 22
HELIX 9 AA9 THR A 224 LYS A 230 1 7
HELIX 10 AB1 ALA A 261 LEU A 267 1 7
HELIX 11 AB2 PHE A 293 ALA A 303 1 11
HELIX 12 AB3 THR A 306 LEU A 310 5 5
HELIX 13 AB4 PHE A 319 LYS A 331 1 13
HELIX 14 AB5 ASP A 333 VAL A 337 5 5
HELIX 15 AB6 GLY A 342 GLY A 347 1 6
HELIX 16 AB7 PRO A 349 ASP A 369 1 21
HELIX 17 AB8 PRO B 25 GLY B 42 1 18
HELIX 18 AB9 LYS B 44 VAL B 48 5 5
HELIX 19 AC1 ASN B 64 ALA B 73 1 10
HELIX 20 AC2 LYS B 86 CYS B 88 5 3
HELIX 21 AC3 GLY B 89 ALA B 104 1 16
HELIX 22 AC4 SER B 119 ALA B 121 5 3
HELIX 23 AC5 GLU B 142 LEU B 148 1 7
HELIX 24 AC6 MET B 157 ASN B 169 1 13
HELIX 25 AC7 SER B 171 SER B 192 1 22
HELIX 26 AC8 THR B 224 LYS B 230 1 7
HELIX 27 AC9 ALA B 261 LEU B 267 1 7
HELIX 28 AD1 PHE B 293 ALA B 303 1 11
HELIX 29 AD2 PHE B 319 LYS B 331 1 13
HELIX 30 AD3 ASP B 333 VAL B 337 5 5
HELIX 31 AD4 GLY B 342 GLY B 347 1 6
HELIX 32 AD5 PRO B 349 ASP B 369 1 21
SHEET 1 AA110 GLY A 15 SER A 16 0
SHEET 2 AA110 ASN A 250 SER A 260 -1 O ASP A 251 N GLY A 15
SHEET 3 AA110 VAL A 109 ASN A 117 -1 N ILE A 110 O ILE A 258
SHEET 4 AA110 GLU A 50 GLY A 54 1 N GLY A 54 O GLY A 113
SHEET 5 AA110 ALA A 81 ASN A 85 1 O ILE A 84 N LEU A 53
SHEET 6 AA110 ALA B 81 ASN B 85 -1 O ASN B 85 N THR A 83
SHEET 7 AA110 GLU B 50 GLY B 54 1 N LEU B 53 O ILE B 84
SHEET 8 AA110 VAL B 109 ASN B 117 1 O ILE B 111 N ILE B 52
SHEET 9 AA110 ASN B 250 SER B 260 -1 O ILE B 258 N ILE B 110
SHEET 10 AA110 GLY B 15 SER B 16 -1 N GLY B 15 O ASP B 251
SHEET 1 AA218 LEU A 312 SER A 315 0
SHEET 2 AA218 LYS A 372 LEU A 377 1 O LEU A 374 N GLU A 314
SHEET 3 AA218 THR A 385 LYS A 391 -1 O LEU A 389 N GLY A 373
SHEET 4 AA218 ALA A 273 TYR A 278 -1 N LYS A 274 O GLU A 390
SHEET 5 AA218 VAL A 4 ARG A 11 -1 N VAL A 4 O ILE A 275
SHEET 6 AA218 ASN A 250 SER A 260 -1 O VAL A 257 N ALA A 7
SHEET 7 AA218 VAL A 109 ASN A 117 -1 N ILE A 110 O ILE A 258
SHEET 8 AA218 GLU A 50 GLY A 54 1 N GLY A 54 O GLY A 113
SHEET 9 AA218 ALA A 81 ASN A 85 1 O ILE A 84 N LEU A 53
SHEET 10 AA218 ALA B 81 ASN B 85 -1 O ASN B 85 N THR A 83
SHEET 11 AA218 GLU B 50 GLY B 54 1 N LEU B 53 O ILE B 84
SHEET 12 AA218 VAL B 109 ASN B 117 1 O ILE B 111 N ILE B 52
SHEET 13 AA218 ASN B 250 SER B 260 -1 O ILE B 258 N ILE B 110
SHEET 14 AA218 VAL B 4 ARG B 11 -1 N ALA B 7 O VAL B 257
SHEET 15 AA218 ALA B 273 TYR B 278 -1 O ILE B 275 N VAL B 4
SHEET 16 AA218 THR B 385 LYS B 391 -1 O GLU B 390 N LYS B 274
SHEET 17 AA218 LYS B 372 LEU B 377 -1 N GLY B 373 O LEU B 389
SHEET 18 AA218 LEU B 312 SER B 315 1 N GLU B 314 O LEU B 374
SHEET 1 AA3 4 VAL A 140 ASP A 141 0
SHEET 2 AA3 4 TYR A 123 ALA A 125 -1 N LEU A 124 O VAL A 140
SHEET 3 AA3 4 TYR B 123 ALA B 125 -1 O ALA B 125 N TYR A 123
SHEET 4 AA3 4 VAL B 140 ASP B 141 -1 O VAL B 140 N LEU B 124
SHEET 1 AA4 2 TRP A 149 ASP A 150 0
SHEET 2 AA4 2 TYR A 155 HIS A 156 -1 O TYR A 155 N ASP A 150
SHEET 1 AA5 2 VAL A 202 LYS A 205 0
SHEET 2 AA5 2 GLU A 210 VAL A 213 -1 O THR A 211 N ILE A 204
SHEET 1 AA6 2 TRP B 149 ASP B 150 0
SHEET 2 AA6 2 TYR B 155 HIS B 156 -1 O TYR B 155 N ASP B 150
SHEET 1 AA7 2 VAL B 202 LYS B 205 0
SHEET 2 AA7 2 GLU B 210 VAL B 213 -1 O THR B 211 N ILE B 204
SSBOND 1 CYS A 88 CYS A 378 1555 1555 2.18
SSBOND 2 CYS B 88 CYS B 378 1555 1555 2.20
SITE 1 AC1 7 SER A 96 GLY A 279 SER A 280 THR A 385
SITE 2 AC1 7 ALA A 386 ILE A 387 HOH A 746
SITE 1 AC2 5 LYS A 265 GLU A 266 GLY A 268 LYS A 270
SITE 2 AC2 5 LYS A 302
SITE 1 AC3 5 TRP A 130 ARG A 133 HOH A 679 HOH A 696
SITE 2 AC3 5 LYS B 22
SITE 1 AC4 4 ASP A 28 THR A 32 LYS A 35 HOH A 720
SITE 1 AC5 5 LEU A 324 ALA A 327 PHE A 332 MET A 334
SITE 2 AC5 5 HOH A 753
SITE 1 AC6 7 LEU A 148 SER A 247 GLY A 248 ALA A 318
SITE 2 AC6 7 HIS A 348 HOH A 651 HOH A 817
SITE 1 AC7 7 SER B 96 GLY B 279 SER B 280 THR B 385
SITE 2 AC7 7 ALA B 386 ILE B 387 HOH B 709
SITE 1 AC8 3 TRP B 130 HOH B 657 HOH B 738
SITE 1 AC9 4 LYS A 138 ALA B 137 LYS B 138 HOH B 623
SITE 1 AD1 4 ASP B 28 THR B 32 LYS B 35 HOH B 688
SITE 1 AD2 2 TYR A 17 ARG B 133
SITE 1 AD3 6 LEU B 148 SER B 247 ALA B 318 HIS B 348
SITE 2 AD3 6 HOH B 652 HOH B 813
CRYST1 203.227 53.987 72.968 90.00 90.00 90.00 P 21 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 0.004921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
