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HEADER HYDROLASE 29-JAN-20 6XY9
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE DBEA-M1 LOOP VARIANT FROM
TITLE 2 BRADYRHIZOBIUM ELKANII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM ELKANII USDA 94;
SOURCE 3 ORGANISM_TAXID: 398524;
SOURCE 4 GENE: DBEA, DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-21B
KEYWDS HALOALAKANE DEHALOGENASE, MICROBIAL HYDROLASE, LOOP-HELIX
KEYWDS 2 ENGINEERING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PRUDNIKOVA,P.REZACOVA,I.KUTA SMATANOVA,R.CHALOUPKOVA,J.DAMBORSKY
REVDAT 1 22-JUL-20 6XY9 0
JRNL AUTH M.MAREK,R.CHALOUPKOVA,T.PRUDNIKOVA,Y.SATO,P.REZACOVA,
JRNL AUTH 2 Y.NAGATA,I.KUTA SMATANOVA,J.DAMBORSKY
JRNL TITL STRUCTURAL AND CATALYTIC EFFECTS OF SURFACE LOOP-HELIX
JRNL TITL 2 TRANSPLANTATION WITHIN HALOALKANE DEHALOGENASE FAMILY.
JRNL REF COMPUT STRUCT BIOTECHNOL J V. 18 1352 2020
JRNL REFN ISSN 2001-0370
JRNL PMID 32612758
JRNL DOI 10.1016/J.CSBJ.2020.05.019
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 36818
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1938
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2664
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4647
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 352
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65000
REMARK 3 B22 (A**2) : 1.93000
REMARK 3 B33 (A**2) : -1.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.459
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4816 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6550 ; 1.878 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 611 ; 6.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;33.917 ;22.591
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 726 ;14.741 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;19.410 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 714 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3739 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6XY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1292106526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR555 FLAT PANEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38810
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.740
REMARK 200 R MERGE (I) : 0.13800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.51500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.350
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: 4K2A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 130 MM CALCIUM ACETATE,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 66.87500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.56500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.87500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.56500
REMARK 290 SMTRY3 4 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: 2960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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 ALA A 5
REMARK 465 GLU A 145
REMARK 465 ALA A 310
REMARK 465 ALA A 311
REMARK 465 LEU A 312
REMARK 465 GLU A 313
REMARK 465 GLU B 145
REMARK 465 GLU B 146
REMARK 465 ARG B 308
REMARK 465 HIS B 309
REMARK 465 ALA B 310
REMARK 465 ALA B 311
REMARK 465 LEU B 312
REMARK 465 GLU B 313
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 O HOH B 691 O HOH B 757 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 662 O HOH B 686 4545 2.15
REMARK 500 O HOH B 678 O HOH B 760 2656 2.18
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 LEU A 15 -127.06 45.92
REMARK 500 SER A 17 -150.17 -154.04
REMARK 500 PRO A 39 56.20 -114.25
REMARK 500 THR A 40 -161.16 -101.83
REMARK 500 ALA A 53 -35.79 -39.82
REMARK 500 ASP A 103 -128.34 64.53
REMARK 500 ALA A 253 -84.68 -100.39
REMARK 500 SER B 17 -154.54 -135.23
REMARK 500 PRO B 39 53.49 -108.57
REMARK 500 THR B 40 -154.51 -98.88
REMARK 500 ASP B 103 -133.25 67.88
REMARK 500 ALA B 253 -78.00 -86.03
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 CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 503
DBREF 6XY9 A 5 311 UNP E2RV62 E2RV62_BRAEL 5 302
DBREF 6XY9 B 5 311 UNP E2RV62 E2RV62_BRAEL 5 302
SEQADV 6XY9 VAL A 143 UNP E2RV62 INSERTION
SEQADV 6XY9 ALA A 144 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU A 145 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU A 146 UNP E2RV62 INSERTION
SEQADV 6XY9 GLN A 147 UNP E2RV62 INSERTION
SEQADV 6XY9 ASP A 148 UNP E2RV62 INSERTION
SEQADV 6XY9 HIS A 149 UNP E2RV62 INSERTION
SEQADV 6XY9 ALA A 150 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU A 151 UNP E2RV62 INSERTION
SEQADV 6XY9 LEU A 312 UNP E2RV62 EXPRESSION TAG
SEQADV 6XY9 GLU A 313 UNP E2RV62 EXPRESSION TAG
SEQADV 6XY9 VAL B 143 UNP E2RV62 INSERTION
SEQADV 6XY9 ALA B 144 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU B 145 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU B 146 UNP E2RV62 INSERTION
SEQADV 6XY9 GLN B 147 UNP E2RV62 INSERTION
SEQADV 6XY9 ASP B 148 UNP E2RV62 INSERTION
SEQADV 6XY9 HIS B 149 UNP E2RV62 INSERTION
SEQADV 6XY9 ALA B 150 UNP E2RV62 INSERTION
SEQADV 6XY9 GLU B 151 UNP E2RV62 INSERTION
SEQADV 6XY9 LEU B 312 UNP E2RV62 EXPRESSION TAG
SEQADV 6XY9 GLU B 313 UNP E2RV62 EXPRESSION TAG
SEQRES 1 A 309 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 A 309 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 A 309 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 A 309 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 A 309 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 A 309 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 A 309 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 A 309 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 A 309 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 A 309 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 A 309 TRP SER ASP PHE HIS GLN HIS ASP VAL ALA GLU GLU GLN
SEQRES 12 A 309 ASP HIS ALA GLU ALA ALA ARG GLU THR PHE ARG LYS PHE
SEQRES 13 A 309 ARG THR PRO GLY VAL GLY GLU ALA MET ILE LEU ASP ASN
SEQRES 14 A 309 ASN ALA PHE VAL GLU ARG VAL LEU PRO GLY SER ILE LEU
SEQRES 15 A 309 ARG THR LEU SER GLU GLU GLU MET ALA ALA TYR ARG ALA
SEQRES 16 A 309 PRO PHE ALA THR ARG GLU SER ARG MET PRO THR LEU MET
SEQRES 17 A 309 LEU PRO ARG GLU LEU PRO ILE ALA GLY GLU PRO ALA ASP
SEQRES 18 A 309 VAL THR GLN ALA LEU THR ALA ALA HIS ALA ALA LEU ALA
SEQRES 19 A 309 ALA SER THR TYR PRO LYS LEU LEU PHE VAL GLY SER PRO
SEQRES 20 A 309 GLY ALA LEU VAL SER PRO ALA PHE ALA ALA GLU PHE ALA
SEQRES 21 A 309 LYS THR LEU LYS HIS CYS ALA VAL ILE GLN LEU GLY ALA
SEQRES 22 A 309 GLY GLY HIS TYR LEU GLN GLU ASP HIS PRO GLU ALA ILE
SEQRES 23 A 309 GLY ARG SER VAL ALA GLY TRP ILE ALA GLY ILE GLU ALA
SEQRES 24 A 309 ALA SER ALA GLN ARG HIS ALA ALA LEU GLU
SEQRES 1 B 309 ALA ASP ILE SER LEU HIS HIS ARG ALA VAL LEU GLY SER
SEQRES 2 B 309 THR MET ALA TYR ARG GLU THR GLY ARG SER ASP ALA PRO
SEQRES 3 B 309 HIS VAL LEU PHE LEU HIS GLY ASN PRO THR SER SER TYR
SEQRES 4 B 309 ILE TRP ARG ASN ILE MET PRO LEU VAL ALA PRO VAL GLY
SEQRES 5 B 309 HIS CYS ILE ALA PRO ASP LEU ILE GLY TYR GLY GLN SER
SEQRES 6 B 309 GLY LYS PRO ASP ILE SER TYR ARG PHE PHE ASP GLN ALA
SEQRES 7 B 309 ASP TYR LEU ASP ALA LEU ILE ASP GLU LEU GLY ILE ALA
SEQRES 8 B 309 SER ALA TYR LEU VAL ALA GLN ASP TRP GLY THR ALA LEU
SEQRES 9 B 309 ALA PHE HIS LEU ALA ALA ARG ARG PRO GLN LEU VAL ARG
SEQRES 10 B 309 GLY LEU ALA PHE MET GLU PHE ILE ARG PRO MET ARG ASP
SEQRES 11 B 309 TRP SER ASP PHE HIS GLN HIS ASP VAL ALA GLU GLU GLN
SEQRES 12 B 309 ASP HIS ALA GLU ALA ALA ARG GLU THR PHE ARG LYS PHE
SEQRES 13 B 309 ARG THR PRO GLY VAL GLY GLU ALA MET ILE LEU ASP ASN
SEQRES 14 B 309 ASN ALA PHE VAL GLU ARG VAL LEU PRO GLY SER ILE LEU
SEQRES 15 B 309 ARG THR LEU SER GLU GLU GLU MET ALA ALA TYR ARG ALA
SEQRES 16 B 309 PRO PHE ALA THR ARG GLU SER ARG MET PRO THR LEU MET
SEQRES 17 B 309 LEU PRO ARG GLU LEU PRO ILE ALA GLY GLU PRO ALA ASP
SEQRES 18 B 309 VAL THR GLN ALA LEU THR ALA ALA HIS ALA ALA LEU ALA
SEQRES 19 B 309 ALA SER THR TYR PRO LYS LEU LEU PHE VAL GLY SER PRO
SEQRES 20 B 309 GLY ALA LEU VAL SER PRO ALA PHE ALA ALA GLU PHE ALA
SEQRES 21 B 309 LYS THR LEU LYS HIS CYS ALA VAL ILE GLN LEU GLY ALA
SEQRES 22 B 309 GLY GLY HIS TYR LEU GLN GLU ASP HIS PRO GLU ALA ILE
SEQRES 23 B 309 GLY ARG SER VAL ALA GLY TRP ILE ALA GLY ILE GLU ALA
SEQRES 24 B 309 ALA SER ALA GLN ARG HIS ALA ALA LEU GLU
HET CL A 501 1
HET CL A 502 1
HET ACT A 503 4
HET CL B 501 1
HET CL B 502 1
HET ACT B 503 4
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 3 CL 4(CL 1-)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 9 HOH *352(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 1 6
HELIX 3 AA3 ARG A 77 LEU A 92 1 16
HELIX 4 AA4 ASP A 103 ARG A 116 1 14
HELIX 5 AA5 GLN A 147 THR A 162 1 16
HELIX 6 AA6 GLY A 164 LEU A 171 1 8
HELIX 7 AA7 ASN A 174 ARG A 179 1 6
HELIX 8 AA8 ARG A 179 SER A 184 1 6
HELIX 9 AA9 SER A 190 ALA A 199 1 10
HELIX 10 AB1 PRO A 200 ALA A 202 5 3
HELIX 11 AB2 ARG A 204 SER A 206 5 3
HELIX 12 AB3 ARG A 207 LEU A 217 1 11
HELIX 13 AB4 PRO A 223 SER A 240 1 18
HELIX 14 AB5 SER A 256 LYS A 265 1 10
HELIX 15 AB6 HIS A 286 HIS A 309 1 24
HELIX 16 AB7 SER B 41 ARG B 46 5 6
HELIX 17 AB8 ILE B 48 ALA B 53 1 6
HELIX 18 AB9 ARG B 77 GLY B 93 1 17
HELIX 19 AC1 ASP B 103 ARG B 116 1 14
HELIX 20 AC2 ASP B 134 PHE B 138 5 5
HELIX 21 AC3 ASP B 148 ARG B 161 1 14
HELIX 22 AC4 GLY B 164 LEU B 171 1 8
HELIX 23 AC5 ASN B 174 ARG B 179 1 6
HELIX 24 AC6 ARG B 179 SER B 184 1 6
HELIX 25 AC7 SER B 190 ALA B 199 1 10
HELIX 26 AC8 PRO B 200 ALA B 202 5 3
HELIX 27 AC9 ARG B 204 SER B 206 5 3
HELIX 28 AD1 ARG B 207 LEU B 213 1 7
HELIX 29 AD2 PRO B 214 LEU B 217 5 4
HELIX 30 AD3 PRO B 223 SER B 240 1 18
HELIX 31 AD4 SER B 256 THR B 266 1 11
HELIX 32 AD5 TYR B 281 HIS B 286 1 6
HELIX 33 AD6 HIS B 286 ALA B 306 1 21
SHEET 1 AA1 8 SER A 8 VAL A 14 0
SHEET 2 AA1 8 SER A 17 THR A 24 -1 O MET A 19 N ARG A 12
SHEET 3 AA1 8 HIS A 57 PRO A 61 -1 O ALA A 60 N ARG A 22
SHEET 4 AA1 8 HIS A 31 LEU A 35 1 N VAL A 32 O ILE A 59
SHEET 5 AA1 8 ALA A 97 GLN A 102 1 O TYR A 98 N LEU A 33
SHEET 6 AA1 8 VAL A 120 MET A 126 1 O ALA A 124 N LEU A 99
SHEET 7 AA1 8 LYS A 244 SER A 250 1 O LEU A 245 N PHE A 125
SHEET 8 AA1 8 CYS A 270 ALA A 277 1 O ALA A 271 N LEU A 246
SHEET 1 AA2 8 SER B 8 VAL B 14 0
SHEET 2 AA2 8 SER B 17 THR B 24 -1 O MET B 19 N ARG B 12
SHEET 3 AA2 8 HIS B 57 PRO B 61 -1 O ALA B 60 N ARG B 22
SHEET 4 AA2 8 HIS B 31 LEU B 35 1 N VAL B 32 O ILE B 59
SHEET 5 AA2 8 ALA B 97 GLN B 102 1 O TYR B 98 N HIS B 31
SHEET 6 AA2 8 VAL B 120 MET B 126 1 O ALA B 124 N LEU B 99
SHEET 7 AA2 8 LYS B 244 PRO B 251 1 O LEU B 245 N PHE B 125
SHEET 8 AA2 8 CYS B 270 GLY B 278 1 O LEU B 275 N VAL B 248
CISPEP 1 ASN A 38 PRO A 39 0 -2.86
CISPEP 2 GLU A 222 PRO A 223 0 -5.35
CISPEP 3 SER A 250 PRO A 251 0 6.02
CISPEP 4 ASN B 38 PRO B 39 0 -4.25
CISPEP 5 GLU B 222 PRO B 223 0 -5.44
CISPEP 6 SER B 250 PRO B 251 0 -5.10
SITE 1 AC1 5 ASN A 38 TRP A 104 PHE A 176 PRO A 214
SITE 2 AC1 5 HOH A 604
SITE 1 AC2 4 GLY A 37 THR A 40 GLN A 102 GLN A 283
SITE 1 AC3 5 HIS A 286 PRO A 287 GLU A 288 ALA A 289
SITE 2 AC3 5 HOH A 653
SITE 1 AC4 5 ASN B 38 TRP B 104 PHE B 176 PRO B 214
SITE 2 AC4 5 HOH B 623
SITE 1 AC5 4 GLY B 37 THR B 40 GLN B 102 GLN B 283
SITE 1 AC6 6 HIS B 286 PRO B 287 GLU B 288 ALA B 289
SITE 2 AC6 6 HOH B 607 HOH B 617
CRYST1 133.750 75.130 77.600 90.00 91.90 90.00 C 1 2 1 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 0.007477 0.000000 0.000248 0.00000
SCALE2 0.000000 0.013310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012894 0.00000
TER 2342 HIS A 309
TER 4684 GLN B 307
MASTER 343 0 6 33 16 0 10 6 5011 2 8 48
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