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HEADER HYDROLASE 17-MAY-13 4KRX
TITLE STRUCTURE OF AES FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL ESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: AES, ECE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: AES, B0476, JW0465, YBAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RD130;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE31
KEYWDS ALPHA/BETA-HYDROLASE, HORMONE-SENSITIVE-LIPASE FAMILY, INHIBITION OF
KEYWDS 2 MALT, ACYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHIEFNER,K.GERBER,A.BROSIG,W.BOOS
REVDAT 1 21-AUG-13 4KRX 0
JRNL AUTH A.SCHIEFNER,K.GERBER,A.BROSIG,W.BOOS
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSES OF AES, AN INHIBITOR OF
JRNL TITL 2 MALT IN ESCHERICHIA COLI.
JRNL REF PROTEINS 2013
JRNL REFN ESSN 1097-0134
JRNL PMID 23934774
JRNL DOI 10.1002/PROT.24383
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 104093
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2084
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6839
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7507
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 658
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.22000
REMARK 3 B22 (A**2) : -1.22000
REMARK 3 B33 (A**2) : 3.95000
REMARK 3 B12 (A**2) : -1.22000
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): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.000
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7858 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7263 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10711 ; 1.858 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16685 ; 0.894 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 974 ; 5.683 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 383 ;33.600 ;23.551
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1242 ;13.509 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;19.494 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1145 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9075 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1900 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 319
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1741 -24.6718 -0.1866
REMARK 3 T TENSOR
REMARK 3 T11: 0.0900 T22: 0.0811
REMARK 3 T33: 0.0221 T12: 0.0005
REMARK 3 T13: -0.0138 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.3231 L22: 0.2383
REMARK 3 L33: 0.1515 L12: 0.0083
REMARK 3 L13: 0.0362 L23: -0.1017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0285 S12: -0.0200 S13: 0.0712
REMARK 3 S21: 0.0147 S22: 0.0099 S23: -0.0347
REMARK 3 S31: 0.0359 S32: -0.0275 S33: 0.0186
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 319
REMARK 3 ORIGIN FOR THE GROUP (A): -73.1877 -46.1927 5.0186
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0755
REMARK 3 T33: 0.0308 T12: 0.0059
REMARK 3 T13: -0.0071 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.3456 L22: 0.3469
REMARK 3 L33: 0.1387 L12: 0.1831
REMARK 3 L13: -0.0733 L23: 0.1248
REMARK 3 S TENSOR
REMARK 3 S11: -0.0271 S12: -0.0227 S13: 0.0386
REMARK 3 S21: -0.0431 S22: -0.0195 S23: 0.1010
REMARK 3 S31: -0.0054 S32: 0.0337 S33: 0.0465
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 319
REMARK 3 ORIGIN FOR THE GROUP (A): -73.1622 -84.5043 -3.0863
REMARK 3 T TENSOR
REMARK 3 T11: 0.0709 T22: 0.0699
REMARK 3 T33: 0.0381 T12: -0.0072
REMARK 3 T13: 0.0127 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.3728 L22: 0.6384
REMARK 3 L33: 0.0789 L12: -0.1420
REMARK 3 L13: 0.0105 L23: -0.0071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.0384 S13: -0.0498
REMARK 3 S21: 0.0465 S22: -0.0045 S23: 0.1543
REMARK 3 S31: -0.0037 S32: 0.0714 S33: -0.0012
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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4KRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
REMARK 200 MONOCHROMATOR : FIXED-EXIT LN2 COOLED DOUBLE
REMARK 200 CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104093
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.80600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3GA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1 M TRIS/HCL,
REMARK 280 30% W/V PEG4000, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.66933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.33467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.33467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 100.66933
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 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: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 550 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 416 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 ARG A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 THR A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 ILE A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 MET B -13
REMARK 465 ARG B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 THR B -3
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 ILE B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 PRO B 3
REMARK 465 MET C -13
REMARK 465 ARG C -12
REMARK 465 GLY C -11
REMARK 465 SER C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 THR C -3
REMARK 465 ASP C -2
REMARK 465 PRO C -1
REMARK 465 ILE C 0
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 PRO C 3
REMARK 465 GLU C 4
REMARK 465 ASN C 5
REMARK 465 LYS C 6
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 GLU C 16 CD GLU C 16 OE2 0.079
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 184 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 184 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 207 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 249 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 105 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 246 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 269 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 269 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 MET C 300 CG - SD - CE ANGL. DEV. = -11.9 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 PRO A 29 173.11 -59.38
REMARK 500 PHE A 95 -5.63 72.24
REMARK 500 SER A 165 -123.71 55.53
REMARK 500 TYR A 195 57.44 37.73
REMARK 500 TYR A 240 -62.03 -120.02
REMARK 500 PHE B 95 -12.26 78.32
REMARK 500 ASN B 99 -171.98 -170.21
REMARK 500 SER B 165 -124.78 58.22
REMARK 500 PRO B 238 0.15 -65.32
REMARK 500 PHE B 261 42.77 -107.04
REMARK 500 HIS B 292 151.62 -46.67
REMARK 500 ASP C 82 60.74 -118.08
REMARK 500 PHE C 95 -12.99 72.37
REMARK 500 SER C 165 -123.56 60.35
REMARK 500 TYR C 195 52.59 36.76
REMARK 500 TYR C 240 -62.44 -120.67
REMARK 500 PHE C 261 53.61 -105.10
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 PG4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KRY RELATED DB: PDB
DBREF 4KRX A 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRX B 1 319 UNP P23872 AES_ECOLI 1 319
DBREF 4KRX C 1 319 UNP P23872 AES_ECOLI 1 319
SEQADV 4KRX MET A -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ARG A -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRX GLY A -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRX SER A -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS A -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRX THR A -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ASP A -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRX PRO A -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ILE A 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRX MET B -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ARG B -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRX GLY B -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRX SER B -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS B -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRX THR B -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ASP B -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRX PRO B -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ILE B 0 UNP P23872 EXPRESSION TAG
SEQADV 4KRX MET C -13 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ARG C -12 UNP P23872 EXPRESSION TAG
SEQADV 4KRX GLY C -11 UNP P23872 EXPRESSION TAG
SEQADV 4KRX SER C -10 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -9 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -8 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -7 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -6 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -5 UNP P23872 EXPRESSION TAG
SEQADV 4KRX HIS C -4 UNP P23872 EXPRESSION TAG
SEQADV 4KRX THR C -3 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ASP C -2 UNP P23872 EXPRESSION TAG
SEQADV 4KRX PRO C -1 UNP P23872 EXPRESSION TAG
SEQADV 4KRX ILE C 0 UNP P23872 EXPRESSION TAG
SEQRES 1 A 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 A 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 A 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 A 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 A 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 A 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 A 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 A 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 A 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 A 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 A 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 A 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 A 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 A 333 MET SER ARG ILE GLY PHE ALA GLY ASP SER ALA GLY ALA
SEQRES 15 A 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 A 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 A 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 A 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 A 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 A 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 A 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 A 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 A 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 A 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 A 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 A 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 B 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 B 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 B 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 B 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 B 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 B 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 B 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 B 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 B 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 B 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 B 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 B 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 B 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 B 333 MET SER ARG ILE GLY PHE ALA GLY ASP SER ALA GLY ALA
SEQRES 15 B 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 B 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 B 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 B 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 B 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 B 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 B 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 B 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 B 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 B 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 B 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 B 333 ALA GLN PHE PHE THR ALA GLN LEU
SEQRES 1 C 333 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 C 333 ILE MET LYS PRO GLU ASN LYS LEU PRO VAL LEU ASP LEU
SEQRES 3 C 333 ILE SER ALA GLU MET LYS THR VAL VAL ASN THR LEU GLN
SEQRES 4 C 333 PRO ASP LEU PRO PRO TRP PRO ALA THR GLY THR ILE ALA
SEQRES 5 C 333 GLU GLN ARG GLN TYR TYR THR LEU GLU ARG ARG PHE TRP
SEQRES 6 C 333 ASN ALA GLY ALA PRO GLU MET ALA THR ARG ALA TYR MET
SEQRES 7 C 333 VAL PRO THR LYS TYR GLY GLN VAL GLU THR ARG LEU PHE
SEQRES 8 C 333 CYS PRO GLN PRO ASP SER PRO ALA THR LEU PHE TYR LEU
SEQRES 9 C 333 HIS GLY GLY GLY PHE ILE LEU GLY ASN LEU ASP THR HIS
SEQRES 10 C 333 ASP ARG ILE MET ARG LEU LEU ALA SER TYR SER GLN CYS
SEQRES 11 C 333 THR VAL ILE GLY ILE ASP TYR THR LEU SER PRO GLU ALA
SEQRES 12 C 333 ARG PHE PRO GLN ALA ILE GLU GLU ILE VAL ALA ALA CYS
SEQRES 13 C 333 CYS TYR PHE HIS GLN GLN ALA GLU ASP TYR GLN ILE ASN
SEQRES 14 C 333 MET SER ARG ILE GLY PHE ALA GLY ASP SER ALA GLY ALA
SEQRES 15 C 333 MET LEU ALA LEU ALA SER ALA LEU TRP LEU ARG ASP LYS
SEQRES 16 C 333 GLN ILE ASP CYS GLY LYS VAL ALA GLY VAL LEU LEU TRP
SEQRES 17 C 333 TYR GLY LEU TYR GLY LEU ARG ASP SER VAL THR ARG ARG
SEQRES 18 C 333 LEU LEU GLY GLY VAL TRP ASP GLY LEU THR GLN GLN ASP
SEQRES 19 C 333 LEU GLN MET TYR GLU GLU ALA TYR LEU SER ASN ASP ALA
SEQRES 20 C 333 ASP ARG GLU SER PRO TYR TYR CYS LEU PHE ASN ASN ASP
SEQRES 21 C 333 LEU THR ARG GLU VAL PRO PRO CYS PHE ILE ALA GLY ALA
SEQRES 22 C 333 GLU PHE ASP PRO LEU LEU ASP ASP SER ARG LEU LEU TYR
SEQRES 23 C 333 GLN THR LEU ALA ALA HIS GLN GLN PRO CYS GLU PHE LYS
SEQRES 24 C 333 LEU TYR PRO GLY THR LEU HIS ALA PHE LEU HIS TYR SER
SEQRES 25 C 333 ARG MET MET LYS THR ALA ASP GLU ALA LEU ARG ASP GLY
SEQRES 26 C 333 ALA GLN PHE PHE THR ALA GLN LEU
HET PG4 A 401 13
HET PG4 B 401 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 4 PG4 2(C8 H18 O5)
FORMUL 6 HOH *658(H2 O)
HELIX 1 1 PRO A 8 ILE A 13 1 6
HELIX 2 2 SER A 14 ASN A 22 1 9
HELIX 3 3 THR A 36 ALA A 53 1 18
HELIX 4 4 HIS A 103 GLN A 115 1 13
HELIX 5 5 PRO A 132 GLN A 148 1 17
HELIX 6 6 GLN A 148 GLN A 153 1 6
HELIX 7 7 SER A 165 LYS A 181 1 17
HELIX 8 8 SER A 203 LEU A 209 1 7
HELIX 9 9 THR A 217 LEU A 229 1 13
HELIX 10 10 ASN A 231 SER A 237 5 7
HELIX 11 11 CYS A 241 ASN A 245 5 5
HELIX 12 12 LEU A 264 HIS A 278 1 15
HELIX 13 13 ALA A 293 SER A 298 5 6
HELIX 14 14 MET A 301 GLN A 318 1 18
HELIX 15 15 PRO B 8 ILE B 13 1 6
HELIX 16 16 SER B 14 THR B 23 1 10
HELIX 17 17 THR B 36 ALA B 53 1 18
HELIX 18 18 HIS B 103 GLN B 115 1 13
HELIX 19 19 PRO B 132 GLN B 148 1 17
HELIX 20 20 GLN B 148 GLN B 153 1 6
HELIX 21 21 SER B 165 LYS B 181 1 17
HELIX 22 22 SER B 203 LEU B 209 1 7
HELIX 23 23 THR B 217 LEU B 229 1 13
HELIX 24 24 ASN B 231 SER B 237 5 7
HELIX 25 25 CYS B 241 ASN B 245 5 5
HELIX 26 26 LEU B 264 HIS B 278 1 15
HELIX 27 27 ALA B 293 SER B 298 5 6
HELIX 28 28 MET B 301 GLN B 318 1 18
HELIX 29 29 PRO C 8 ILE C 13 1 6
HELIX 30 30 SER C 14 ASN C 22 1 9
HELIX 31 31 THR C 36 ALA C 53 1 18
HELIX 32 32 HIS C 103 GLN C 115 1 13
HELIX 33 33 PRO C 132 GLN C 148 1 17
HELIX 34 34 GLN C 148 GLN C 153 1 6
HELIX 35 35 SER C 165 LYS C 181 1 17
HELIX 36 36 SER C 203 LEU C 209 1 7
HELIX 37 37 THR C 217 LEU C 229 1 13
HELIX 38 38 ASN C 231 SER C 237 5 7
HELIX 39 39 CYS C 241 ASN C 245 5 5
HELIX 40 40 LEU C 264 HIS C 278 1 15
HELIX 41 41 ALA C 293 SER C 298 5 6
HELIX 42 42 MET C 301 GLN C 318 1 18
SHEET 1 A 8 ALA A 59 VAL A 65 0
SHEET 2 A 8 VAL A 72 CYS A 78 -1 O LEU A 76 N ARG A 61
SHEET 3 A 8 THR A 117 ILE A 121 -1 O VAL A 118 N PHE A 77
SHEET 4 A 8 THR A 86 LEU A 90 1 N LEU A 87 O ILE A 119
SHEET 5 A 8 ARG A 158 ASP A 164 1 O GLY A 160 N PHE A 88
SHEET 6 A 8 LYS A 187 TRP A 194 1 O ALA A 189 N ILE A 159
SHEET 7 A 8 CYS A 254 ALA A 259 1 O PHE A 255 N LEU A 193
SHEET 8 A 8 CYS A 282 TYR A 287 1 O GLU A 283 N ILE A 256
SHEET 1 B 8 ALA B 59 VAL B 65 0
SHEET 2 B 8 VAL B 72 CYS B 78 -1 O CYS B 78 N ALA B 59
SHEET 3 B 8 THR B 117 ILE B 121 -1 O VAL B 118 N PHE B 77
SHEET 4 B 8 THR B 86 LEU B 90 1 N LEU B 87 O THR B 117
SHEET 5 B 8 ARG B 158 ASP B 164 1 O ALA B 162 N LEU B 90
SHEET 6 B 8 LYS B 187 TRP B 194 1 O ALA B 189 N ILE B 159
SHEET 7 B 8 CYS B 254 ALA B 259 1 O PHE B 255 N LEU B 193
SHEET 8 B 8 CYS B 282 TYR B 287 1 O GLU B 283 N ILE B 256
SHEET 1 C 8 ALA C 59 VAL C 65 0
SHEET 2 C 8 VAL C 72 CYS C 78 -1 O LEU C 76 N ARG C 61
SHEET 3 C 8 THR C 117 ILE C 121 -1 O VAL C 118 N PHE C 77
SHEET 4 C 8 THR C 86 LEU C 90 1 N LEU C 87 O THR C 117
SHEET 5 C 8 ARG C 158 ASP C 164 1 O ALA C 162 N LEU C 90
SHEET 6 C 8 LYS C 187 TRP C 194 1 O ALA C 189 N ILE C 159
SHEET 7 C 8 CYS C 254 ALA C 259 1 O ALA C 257 N LEU C 193
SHEET 8 C 8 CYS C 282 TYR C 287 1 O GLU C 283 N ILE C 256
SSBOND 1 CYS A 143 CYS A 185 1555 1555 2.04
SSBOND 2 CYS B 143 CYS B 185 1555 1555 2.04
SSBOND 3 CYS C 143 CYS C 185 1555 1555 2.06
CISPEP 1 SER A 126 PRO A 127 0 8.00
CISPEP 2 PHE A 131 PRO A 132 0 -2.32
CISPEP 3 SER B 126 PRO B 127 0 2.46
CISPEP 4 PHE B 131 PRO B 132 0 -0.15
CISPEP 5 SER C 126 PRO C 127 0 3.35
CISPEP 6 PHE C 131 PRO C 132 0 3.25
SITE 1 AC1 12 GLY A 93 GLY A 94 SER A 165 ALA A 166
SITE 2 AC1 12 LEU A 197 LEU A 216 TYR A 224 HOH A 553
SITE 3 AC1 12 HOH A 582 HOH A 698 HOH A 702 HOH A 737
SITE 1 AC2 10 GLY B 93 GLY B 94 PHE B 95 SER B 165
SITE 2 AC2 10 LEU B 197 LEU B 216 TYR B 224 HOH B 538
SITE 3 AC2 10 HOH B 637 HOH B 659
CRYST1 113.712 113.712 151.004 90.00 90.00 120.00 P 32 2 1 18
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 0.008794 0.005077 0.000000 0.00000
SCALE2 0.000000 0.010155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006622 0.00000
TER 2547 LEU A 319
TER 5090 LEU B 319
TER 7623 LEU C 319
MASTER 480 0 2 42 24 0 6 6 8191 3 32 78
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