| content |
HEADER HYDROLASE 02-MAR-10 3AFI
TITLE CRYSTAL STRUCTURE OF DBJA (HIS-DBJA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: E, A, B, F;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM JAPONICUM;
SOURCE 3 ORGANISM_TAXID: 224911;
SOURCE 4 STRAIN: USDA 110;
SOURCE 5 GENE: DBJA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PYBJA2
KEYWDS A/B-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SATO,T.SENDA
REVDAT 1 19-JAN-11 3AFI 0
JRNL AUTH Z.PROKOP,Y.SATO,J.BREZOVSKY,T.MOZGA,R.CHALOUPKOVA,
JRNL AUTH 2 T.KOUDELAKOVA,P.JERABEK,V.STEPANKOVA,R.NATSUME,
JRNL AUTH 3 J.G.VAN LEEUWEN,D.B.JANSSEN,J.FLORIAN,Y.NAGATA,T.SENDA,
JRNL AUTH 4 J.DAMBORSKY
JRNL TITL ENANTIOSELECTIVITY OF HALOALKANE DEHALOGENASES AND ITS
JRNL TITL 2 MODULATION BY SURFACE LOOP ENGINEERING
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 49 6111 2010
JRNL REFN ISSN 1433-7851
JRNL PMID 20645368
JRNL DOI 10.1002/ANIE.201001753
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 127902
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
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 : 6770
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8607
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 450
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9401
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 1120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : 0.07000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.819
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9701 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13209 ; 1.275 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1196 ; 5.184 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 464 ;31.605 ;21.875
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1424 ;12.553 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;19.028 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1405 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7690 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4700 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6684 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 963 ; 0.113 ; 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): 35 ; 0.272 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.087 ; 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): 6028 ; 0.654 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9656 ; 1.233 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3673 ; 2.000 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3553 ; 3.366 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3AFI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB029188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SI
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 95.2
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.17500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1BN6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.9, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 106.42750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.92150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 106.42750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.92150
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 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: 1870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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 MET E 1
REMARK 465 SER E 2
REMARK 465 LYS E 3
REMARK 465 PRO E 4
REMARK 465 ILE E 5
REMARK 465 GLU E 6
REMARK 465 ILE E 7
REMARK 465 GLU E 8
REMARK 465 ILE E 9
REMARK 465 LEU E 308
REMARK 465 ALA E 309
REMARK 465 ALA E 310
REMARK 465 HIS E 311
REMARK 465 HIS E 312
REMARK 465 HIS E 313
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 ILE A 5
REMARK 465 GLU A 6
REMARK 465 ILE A 7
REMARK 465 GLU A 8
REMARK 465 GLN A 307
REMARK 465 LEU A 308
REMARK 465 ALA A 309
REMARK 465 ALA A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 ILE B 5
REMARK 465 ARG B 305
REMARK 465 PRO B 306
REMARK 465 GLN B 307
REMARK 465 LEU B 308
REMARK 465 ALA B 309
REMARK 465 ALA B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 LYS F 3
REMARK 465 PRO F 4
REMARK 465 ILE F 5
REMARK 465 GLU F 6
REMARK 465 ILE F 7
REMARK 465 GLU F 8
REMARK 465 ILE F 9
REMARK 465 GLN F 307
REMARK 465 LEU F 308
REMARK 465 ALA F 309
REMARK 465 ALA F 310
REMARK 465 HIS F 311
REMARK 465 HIS F 312
REMARK 465 HIS F 313
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 E 83 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 83 NE - CZ - NH2 ANGL. DEV. = -3.9 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 SER E 17 -152.69 -124.55
REMARK 500 PRO E 39 52.81 -102.62
REMARK 500 THR E 40 -159.22 -101.77
REMARK 500 ASP E 103 -137.07 57.82
REMARK 500 ARG E 179 -56.18 -127.02
REMARK 500 ALA E 253 -67.45 -147.54
REMARK 500 LEU E 279 -135.44 -120.26
REMARK 500 SER A 17 -147.88 -119.36
REMARK 500 PRO A 39 51.58 -102.04
REMARK 500 THR A 40 -158.02 -103.76
REMARK 500 ASP A 103 -140.27 58.22
REMARK 500 ARG A 179 -53.04 -123.64
REMARK 500 ALA A 253 -72.12 -146.54
REMARK 500 LEU A 279 -135.66 -123.84
REMARK 500 SER B 17 -155.96 -122.30
REMARK 500 PRO B 39 56.09 -102.89
REMARK 500 THR B 40 -161.89 -105.11
REMARK 500 ASP B 103 -133.71 57.33
REMARK 500 ARG B 179 -54.89 -123.63
REMARK 500 ALA B 253 -65.49 -147.92
REMARK 500 LEU B 279 -134.67 -125.31
REMARK 500 SER F 17 -149.46 -122.07
REMARK 500 GLN F 27 -23.97 101.63
REMARK 500 PRO F 39 54.46 -105.01
REMARK 500 THR F 40 -160.44 -106.13
REMARK 500 ASP F 103 -137.54 58.24
REMARK 500 ARG F 179 -54.18 -127.36
REMARK 500 ALA F 253 -72.20 -147.86
REMARK 500 LEU F 279 -136.64 -122.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E1444 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH A1337 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH A1466 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH B1525 DISTANCE = 5.73 ANGSTROMS
REMARK 525 HOH A1557 DISTANCE = 6.16 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A2M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DBJA (WILD TYPE TYPE I)
REMARK 900 RELATED ID: 3A2N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DBJA (WILD TYPE TYPE II)
REMARK 900 RELATED ID: 3A2L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DBJA (MUTANT DBJA DELTA)
DBREF 3AFI E 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3AFI A 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3AFI B 1 310 UNP P59337 DHAA_BRAJA 1 310
DBREF 3AFI F 1 310 UNP P59337 DHAA_BRAJA 1 310
SEQADV 3AFI HIS E 311 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS E 312 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS E 313 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS E 314 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS E 315 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS E 316 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 311 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 312 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 313 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 314 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 315 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS A 316 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 311 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 312 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 313 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 314 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 315 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS B 316 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 311 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 312 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 313 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 314 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 315 UNP P59337 EXPRESSION TAG
SEQADV 3AFI HIS F 316 UNP P59337 EXPRESSION TAG
SEQRES 1 E 316 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 E 316 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 E 316 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 E 316 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 E 316 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 E 316 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 E 316 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 E 316 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 E 316 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 E 316 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 E 316 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 E 316 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 E 316 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 E 316 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 E 316 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 E 316 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 E 316 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 E 316 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 E 316 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 E 316 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 E 316 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 E 316 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 E 316 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 E 316 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS
SEQRES 25 E 316 HIS HIS HIS HIS
SEQRES 1 A 316 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 A 316 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 A 316 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 316 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 A 316 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 A 316 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 A 316 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 A 316 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 A 316 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 A 316 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 A 316 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 A 316 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 A 316 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 A 316 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 A 316 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 A 316 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 A 316 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 A 316 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 A 316 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 A 316 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 A 316 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 A 316 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 A 316 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 A 316 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS
SEQRES 25 A 316 HIS HIS HIS HIS
SEQRES 1 B 316 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 B 316 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 B 316 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 316 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 B 316 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 B 316 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 B 316 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 B 316 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 B 316 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 B 316 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 B 316 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 B 316 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 B 316 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 B 316 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 B 316 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 B 316 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 B 316 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 B 316 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 B 316 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 B 316 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 B 316 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 B 316 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 B 316 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 B 316 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS
SEQRES 25 B 316 HIS HIS HIS HIS
SEQRES 1 F 316 MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO
SEQRES 2 F 316 VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA
SEQRES 3 F 316 GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 F 316 THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL
SEQRES 5 F 316 SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 6 F 316 PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE
SEQRES 7 F 316 PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN
SEQRES 8 F 316 ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP
SEQRES 9 F 316 GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO
SEQRES 10 F 316 ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG
SEQRES 11 F 316 PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL
SEQRES 12 F 316 ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL
SEQRES 13 F 316 PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET
SEQRES 14 F 316 ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO
SEQRES 15 F 316 GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA
SEQRES 16 F 316 PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG
SEQRES 17 F 316 PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY
SEQRES 18 F 316 GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS
SEQRES 19 F 316 ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE
SEQRES 20 F 316 THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA
SEQRES 21 F 316 GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE
SEQRES 22 F 316 ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS
SEQRES 23 F 316 ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA
SEQRES 24 F 316 GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS
SEQRES 25 F 316 HIS HIS HIS HIS
HET CL E 401 1
HET CL A 402 1
HET CL B 403 1
HET CL F 404 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 4(CL 1-)
FORMUL 9 HOH *1120(H2 O)
HELIX 1 1 SER E 41 ARG E 46 5 6
HELIX 2 2 ILE E 48 SER E 53 1 6
HELIX 3 3 ARG E 77 ARG E 92 1 16
HELIX 4 4 ASP E 103 ARG E 116 1 14
HELIX 5 5 THR E 134 PHE E 138 5 5
HELIX 6 6 VAL E 143 GLU E 145 5 3
HELIX 7 7 GLU E 146 ARG E 161 1 16
HELIX 8 8 GLY E 164 LEU E 171 1 8
HELIX 9 9 ASN E 174 ARG E 179 1 6
HELIX 10 10 LEU E 181 ILE E 185 5 5
HELIX 11 11 GLY E 190 THR E 199 1 10
HELIX 12 12 PRO E 204 SER E 206 5 3
HELIX 13 13 ARG E 207 PHE E 213 1 7
HELIX 14 14 PRO E 214 LEU E 217 5 4
HELIX 15 15 PRO E 223 SER E 240 1 18
HELIX 16 16 SER E 256 LEU E 267 1 12
HELIX 17 17 TYR E 281 VAL E 304 1 24
HELIX 18 18 SER A 41 ARG A 46 5 6
HELIX 19 19 ILE A 48 SER A 53 1 6
HELIX 20 20 ARG A 77 ARG A 92 1 16
HELIX 21 21 ASP A 103 ARG A 116 1 14
HELIX 22 22 THR A 134 PHE A 138 5 5
HELIX 23 23 VAL A 143 GLU A 145 5 3
HELIX 24 24 GLU A 146 ARG A 161 1 16
HELIX 25 25 GLY A 164 LEU A 171 1 8
HELIX 26 26 ASN A 174 ARG A 179 1 6
HELIX 27 27 LEU A 181 ILE A 185 5 5
HELIX 28 28 GLY A 190 THR A 199 1 10
HELIX 29 29 PRO A 204 SER A 206 5 3
HELIX 30 30 ARG A 207 LEU A 217 1 11
HELIX 31 31 PRO A 223 SER A 240 1 18
HELIX 32 32 SER A 256 LEU A 267 1 12
HELIX 33 33 TYR A 281 HIS A 286 1 6
HELIX 34 34 HIS A 286 ARG A 305 1 20
HELIX 35 35 SER B 41 ARG B 46 5 6
HELIX 36 36 ILE B 48 SER B 53 1 6
HELIX 37 37 ARG B 77 ARG B 92 1 16
HELIX 38 38 ASP B 103 ARG B 116 1 14
HELIX 39 39 THR B 134 PHE B 138 5 5
HELIX 40 40 VAL B 143 GLU B 145 5 3
HELIX 41 41 GLU B 146 ARG B 161 1 16
HELIX 42 42 GLU B 165 LEU B 171 1 7
HELIX 43 43 ASN B 174 ARG B 179 1 6
HELIX 44 44 LEU B 181 ILE B 185 5 5
HELIX 45 45 GLY B 190 THR B 199 1 10
HELIX 46 46 PRO B 204 SER B 206 5 3
HELIX 47 47 ARG B 207 PHE B 213 1 7
HELIX 48 48 PRO B 214 LEU B 217 5 4
HELIX 49 49 PRO B 223 SER B 240 1 18
HELIX 50 50 SER B 256 LEU B 267 1 12
HELIX 51 51 TYR B 281 VAL B 304 1 24
HELIX 52 52 SER F 41 ARG F 46 5 6
HELIX 53 53 ILE F 48 SER F 53 1 6
HELIX 54 54 ARG F 77 ARG F 92 1 16
HELIX 55 55 ASP F 103 ARG F 116 1 14
HELIX 56 56 THR F 134 PHE F 138 5 5
HELIX 57 57 VAL F 143 GLU F 145 5 3
HELIX 58 58 GLU F 146 ARG F 161 1 16
HELIX 59 59 GLY F 164 LEU F 171 1 8
HELIX 60 60 ASN F 174 ARG F 179 1 6
HELIX 61 61 ARG F 179 GLY F 184 1 6
HELIX 62 62 GLY F 190 THR F 199 1 10
HELIX 63 63 PRO F 204 SER F 206 5 3
HELIX 64 64 ARG F 207 LEU F 217 1 11
HELIX 65 65 PRO F 223 SER F 240 1 18
HELIX 66 66 SER F 256 SER F 266 1 11
HELIX 67 67 TYR F 281 VAL F 304 1 24
SHEET 1 A 8 ARG E 11 VAL E 14 0
SHEET 2 A 8 SER E 17 THR E 24 -1 O SER E 17 N VAL E 14
SHEET 3 A 8 HIS E 57 PRO E 61 -1 O ALA E 60 N ARG E 22
SHEET 4 A 8 VAL E 31 LEU E 35 1 N VAL E 32 O ILE E 59
SHEET 5 A 8 ALA E 97 GLN E 102 1 O TYR E 98 N LEU E 33
SHEET 6 A 8 VAL E 120 MET E 126 1 O ALA E 124 N LEU E 99
SHEET 7 A 8 LYS E 244 PRO E 251 1 O LEU E 245 N PHE E 125
SHEET 8 A 8 CYS E 270 GLY E 278 1 O ALA E 271 N LEU E 246
SHEET 1 B 8 ARG A 10 VAL A 14 0
SHEET 2 B 8 SER A 17 THR A 24 -1 O TYR A 21 N ARG A 10
SHEET 3 B 8 HIS A 57 PRO A 61 -1 O ALA A 60 N ARG A 22
SHEET 4 B 8 VAL A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 B 8 ALA A 97 GLN A 102 1 O TYR A 98 N LEU A 33
SHEET 6 B 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 B 8 LYS A 244 PRO A 251 1 O LEU A 245 N PHE A 125
SHEET 8 B 8 CYS A 270 GLY A 278 1 O ILE A 273 N LEU A 246
SHEET 1 C 8 ARG B 10 VAL B 14 0
SHEET 2 C 8 SER B 17 THR B 24 -1 O MET B 19 N ALA B 12
SHEET 3 C 8 HIS B 57 PRO B 61 -1 O ALA B 60 N ARG B 22
SHEET 4 C 8 VAL B 31 LEU B 35 1 N VAL B 32 O ILE B 59
SHEET 5 C 8 ALA B 97 GLN B 102 1 O VAL B 100 N LEU B 35
SHEET 6 C 8 VAL B 120 MET B 126 1 O ALA B 124 N LEU B 99
SHEET 7 C 8 LYS B 244 PRO B 251 1 O LEU B 245 N PHE B 125
SHEET 8 C 8 CYS B 270 GLY B 278 1 O ILE B 273 N LEU B 246
SHEET 1 D 8 ARG F 11 VAL F 14 0
SHEET 2 D 8 SER F 17 THR F 24 -1 O MET F 19 N ALA F 12
SHEET 3 D 8 HIS F 57 PRO F 61 -1 O CYS F 58 N THR F 24
SHEET 4 D 8 VAL F 31 LEU F 35 1 N VAL F 32 O ILE F 59
SHEET 5 D 8 ALA F 97 GLN F 102 1 O VAL F 100 N LEU F 35
SHEET 6 D 8 VAL F 120 MET F 126 1 O ALA F 124 N LEU F 99
SHEET 7 D 8 LYS F 244 PRO F 251 1 O LEU F 245 N PHE F 125
SHEET 8 D 8 CYS F 270 GLY F 278 1 O LEU F 275 N THR F 248
CISPEP 1 ASN E 38 PRO E 39 0 -13.51
CISPEP 2 GLU E 222 PRO E 223 0 -3.63
CISPEP 3 GLU E 250 PRO E 251 0 3.58
CISPEP 4 ASN A 38 PRO A 39 0 -15.44
CISPEP 5 GLU A 222 PRO A 223 0 -4.50
CISPEP 6 GLU A 250 PRO A 251 0 1.15
CISPEP 7 ASN B 38 PRO B 39 0 -14.36
CISPEP 8 GLU B 222 PRO B 223 0 -5.27
CISPEP 9 GLU B 250 PRO B 251 0 1.30
CISPEP 10 ASN F 38 PRO F 39 0 -10.50
CISPEP 11 GLU F 222 PRO F 223 0 -4.14
CISPEP 12 GLU F 250 PRO F 251 0 1.93
SITE 1 AC1 5 ASN E 38 TRP E 104 PHE E 213 PRO E 214
SITE 2 AC1 5 HOH E1162
SITE 1 AC2 5 ASN A 38 TRP A 104 PHE A 213 PRO A 214
SITE 2 AC2 5 HOH A 772
SITE 1 AC3 5 ASN B 38 TRP B 104 PHE B 213 PRO B 214
SITE 2 AC3 5 HOH B 567
SITE 1 AC4 5 ASN F 38 TRP F 104 PHE F 213 PRO F 214
SITE 2 AC4 5 HOH F 974
CRYST1 212.855 117.843 55.796 90.00 90.00 90.00 P 21 21 2 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 0.004698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017922 0.00000
TER 2352 HIS E 316
TER 4703 HIS A 316
TER 7074 HIS B 316
TER 9425 HIS F 316
MASTER 421 0 4 67 32 0 8 610525 4 0 100
END |