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HEADER HYDROLASE 30-AUG-20 7CWQ
TITLE CRYSTAL STRUCTURE OF A NOVEL HYDROLASE FROM BURKHOLDERIALES BACTERIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DLH DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIALES BACTERIUM
SOURCE 3 RIFCSPLOWO2_02_FULL_57_36;
SOURCE 4 ORGANISM_TAXID: 1797562;
SOURCE 5 GENE: A3I66_11710;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS SUBSTRATE BINDING, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
REVDAT 1 26-MAY-21 7CWQ 0
JRNL AUTH X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL HYDROLASE FROM BURKHOLDERIALES
JRNL TITL 2 BACTERIUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0266
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 64801
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3381
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4602
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 525
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.36000
REMARK 3 B12 (A**2) : -0.06000
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): 0.088
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.715
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4214 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 3752 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5772 ; 1.491 ; 1.653
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8682 ; 1.471 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 538 ; 6.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;34.337 ;22.527
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 608 ;12.340 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;19.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4850 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 956 ; 0.002 ; 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 : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7CWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-20.
REMARK 100 THE DEPOSITION ID IS D_1300018348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68361
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 30.30
REMARK 200 R MERGE (I) : 0.21100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.33700
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: PHASER
REMARK 200 STARTING MODEL: 5XFY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 6000, GLYCEROL,
REMARK 280 MES, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 254.59333
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 127.29667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 190.94500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.64833
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 318.24167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 254.59333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 127.29667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 63.64833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 190.94500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 318.24167
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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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 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 A 290 -122.58 60.51
REMARK 500 HIS A 344 -90.62 -130.49
REMARK 500 CYS A 404 -9.73 -140.72
REMARK 500 SER B 290 -117.70 59.73
REMARK 500 HIS B 344 -88.90 -129.32
REMARK 500 CYS B 424 150.26 -48.62
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 A 878 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 879 DISTANCE = 6.69 ANGSTROMS
DBREF1 7CWQ A 158 426 UNP A0A1F4JXW8_9BURK
DBREF2 7CWQ A A0A1F4JXW8 158 426
DBREF1 7CWQ B 158 426 UNP A0A1F4JXW8_9BURK
DBREF2 7CWQ B A0A1F4JXW8 158 426
SEQADV 7CWQ MET A 157 UNP A0A1F4JXW INITIATING METHIONINE
SEQADV 7CWQ MET B 157 UNP A0A1F4JXW INITIATING METHIONINE
SEQRES 1 A 270 MET ASN PRO PHE GLU LYS GLY PRO ASP PRO THR LYS THR
SEQRES 2 A 270 MET LEU GLU ALA SER THR GLY PRO PHE THR TYR THR THR
SEQRES 3 A 270 THR THR VAL SER SER THR THR ALA SER GLY TYR ARG GLN
SEQRES 4 A 270 GLY THR ILE TYR HIS PRO THR ASN VAL THR GLY PRO PHE
SEQRES 5 A 270 ALA ALA VAL ALA VAL VAL PRO GLY TYR LEU ALA SER GLN
SEQRES 6 A 270 SER SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 270 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR SER
SEQRES 8 A 270 ASP GLN PRO PRO SER ARG ALA THR GLN LEU MET ALA ALA
SEQRES 9 A 270 LEU ASN GLN LEU LYS THR PHE SER ASN THR SER SER HIS
SEQRES 10 A 270 PRO ILE TYR ARG LYS VAL ASP PRO ASN ARG LEU GLY VAL
SEQRES 11 A 270 MET GLY TRP SER MET GLY GLY GLY GLY THR LEU ILE ALA
SEQRES 12 A 270 ALA ARG ASP ASN PRO THR LEU LYS ALA ALA ILE PRO PHE
SEQRES 13 A 270 ALA PRO TRP ASN SER SER THR ASN PHE SER THR VAL SER
SEQRES 14 A 270 VAL PRO THR LEU ILE ILE ALA CYS GLU SER ASP SER THR
SEQRES 15 A 270 ALA PRO VAL ASN SER HIS ALA SER PRO PHE TYR ASN SER
SEQRES 16 A 270 LEU PRO SER THR THR LYS LYS ALA TYR LEU GLU MET ASN
SEQRES 17 A 270 ASN GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN
SEQRES 18 A 270 ALA GLY LEU ILE GLY LYS TYR GLY VAL SER TRP MET LYS
SEQRES 19 A 270 ARG PHE MET ASP ASN ASP THR ARG PHE SER PRO TYR LEU
SEQRES 20 A 270 CYS GLY ALA PRO HIS GLN ALA ASP LEU SER LEU THR ALA
SEQRES 21 A 270 ILE ASP GLU TYR ARG GLU ASN CYS PRO TYR
SEQRES 1 B 270 MET ASN PRO PHE GLU LYS GLY PRO ASP PRO THR LYS THR
SEQRES 2 B 270 MET LEU GLU ALA SER THR GLY PRO PHE THR TYR THR THR
SEQRES 3 B 270 THR THR VAL SER SER THR THR ALA SER GLY TYR ARG GLN
SEQRES 4 B 270 GLY THR ILE TYR HIS PRO THR ASN VAL THR GLY PRO PHE
SEQRES 5 B 270 ALA ALA VAL ALA VAL VAL PRO GLY TYR LEU ALA SER GLN
SEQRES 6 B 270 SER SER ILE ASN TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 B 270 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR SER
SEQRES 8 B 270 ASP GLN PRO PRO SER ARG ALA THR GLN LEU MET ALA ALA
SEQRES 9 B 270 LEU ASN GLN LEU LYS THR PHE SER ASN THR SER SER HIS
SEQRES 10 B 270 PRO ILE TYR ARG LYS VAL ASP PRO ASN ARG LEU GLY VAL
SEQRES 11 B 270 MET GLY TRP SER MET GLY GLY GLY GLY THR LEU ILE ALA
SEQRES 12 B 270 ALA ARG ASP ASN PRO THR LEU LYS ALA ALA ILE PRO PHE
SEQRES 13 B 270 ALA PRO TRP ASN SER SER THR ASN PHE SER THR VAL SER
SEQRES 14 B 270 VAL PRO THR LEU ILE ILE ALA CYS GLU SER ASP SER THR
SEQRES 15 B 270 ALA PRO VAL ASN SER HIS ALA SER PRO PHE TYR ASN SER
SEQRES 16 B 270 LEU PRO SER THR THR LYS LYS ALA TYR LEU GLU MET ASN
SEQRES 17 B 270 ASN GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN
SEQRES 18 B 270 ALA GLY LEU ILE GLY LYS TYR GLY VAL SER TRP MET LYS
SEQRES 19 B 270 ARG PHE MET ASP ASN ASP THR ARG PHE SER PRO TYR LEU
SEQRES 20 B 270 CYS GLY ALA PRO HIS GLN ALA ASP LEU SER LEU THR ALA
SEQRES 21 B 270 ILE ASP GLU TYR ARG GLU ASN CYS PRO TYR
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 B 501 5
HET SO4 B 502 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *525(H2 O)
HELIX 1 AA1 THR A 167 ALA A 173 1 7
HELIX 2 AA2 SER A 220 ASN A 225 5 6
HELIX 3 AA3 TRP A 226 SER A 233 1 8
HELIX 4 AA4 GLN A 249 ASN A 269 1 21
HELIX 5 AA5 SER A 290 ASN A 303 1 14
HELIX 6 AA6 HIS A 344 LEU A 352 1 9
HELIX 7 AA7 ASN A 377 ASP A 394 1 18
HELIX 8 AA8 ASP A 396 ARG A 398 5 3
HELIX 9 AA9 PHE A 399 GLY A 405 1 7
HELIX 10 AB1 GLY A 405 LEU A 412 1 8
HELIX 11 AB2 THR B 167 ALA B 173 1 7
HELIX 12 AB3 SER B 220 ASN B 225 5 6
HELIX 13 AB4 TRP B 226 SER B 233 1 8
HELIX 14 AB5 GLN B 249 ASN B 269 1 21
HELIX 15 AB6 SER B 290 ASN B 303 1 14
HELIX 16 AB7 HIS B 344 LEU B 352 1 9
HELIX 17 AB8 ASN B 377 ASP B 394 1 18
HELIX 18 AB9 ASP B 396 ARG B 398 5 3
HELIX 19 AC1 PHE B 399 GLY B 405 1 7
HELIX 20 AC2 GLY B 405 LEU B 412 1 8
SHEET 1 AA1 6 TYR A 180 VAL A 185 0
SHEET 2 AA1 6 GLN A 195 PRO A 201 -1 O ILE A 198 N THR A 183
SHEET 3 AA1 6 VAL A 237 ASP A 242 -1 O VAL A 238 N TYR A 199
SHEET 4 AA1 6 PHE A 208 VAL A 214 1 N VAL A 211 O VAL A 237
SHEET 5 AA1 6 VAL A 279 TRP A 289 1 O ASP A 280 N PHE A 208
SHEET 6 AA1 6 ALA A 308 PHE A 312 1 O PHE A 312 N GLY A 288
SHEET 1 AA2 3 THR A 328 CYS A 333 0
SHEET 2 AA2 3 LYS A 358 MET A 363 1 O LEU A 361 N ALA A 332
SHEET 3 AA2 3 ILE A 417 GLU A 422 -1 O GLU A 419 N GLU A 362
SHEET 1 AA3 6 THR B 179 VAL B 185 0
SHEET 2 AA3 6 GLN B 195 THR B 202 -1 O ILE B 198 N THR B 183
SHEET 3 AA3 6 VAL B 237 ASP B 242 -1 O VAL B 238 N TYR B 199
SHEET 4 AA3 6 PHE B 208 VAL B 214 1 N VAL B 211 O ILE B 239
SHEET 5 AA3 6 VAL B 279 TRP B 289 1 O ASP B 280 N PHE B 208
SHEET 6 AA3 6 ALA B 308 PHE B 312 1 O PHE B 312 N GLY B 288
SHEET 1 AA4 3 THR B 328 CYS B 333 0
SHEET 2 AA4 3 LYS B 358 MET B 363 1 O LEU B 361 N ALA B 332
SHEET 3 AA4 3 ILE B 417 GLU B 422 -1 O GLU B 419 N GLU B 362
SSBOND 1 CYS A 333 CYS A 370 1555 1555 2.04
SSBOND 2 CYS A 404 CYS A 424 1555 1555 2.12
SSBOND 3 CYS B 333 CYS B 370 1555 1555 2.07
SSBOND 4 CYS B 404 CYS B 424 1555 1555 2.11
CISPEP 1 GLY A 206 PRO A 207 0 2.92
CISPEP 2 CYS A 424 PRO A 425 0 -4.71
CISPEP 3 GLY B 206 PRO B 207 0 -1.97
CISPEP 4 CYS B 424 PRO B 425 0 8.34
CRYST1 69.967 69.967 381.890 90.00 90.00 120.00 P 65 2 2 24
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 0.014292 0.008252 0.000000 0.00000
SCALE2 0.000000 0.016504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002619 0.00000
TER 2038 TYR A 426
TER 4076 TYR B 426
MASTER 308 0 4 20 18 0 0 6 4619 2 28 42
END |