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HEADER HYDROLASE 10-JAN-08 3BWX
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE (YP_496220.1)
TITLE 2 FROM NOVOSPHINGOBIUM AROMATICIVORANS DSM 12444 AT 1.50 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOVOSPHINGOBIUM AROMATICIVORANS DSM
SOURCE 3 12444;
SOURCE 4 ORGANISM_COMMON: BACTERIA;
SOURCE 5 STRAIN: DSM 12444;
SOURCE 6 GENE: YP_496220.1, SARO_0941;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS YP_496220.1, AN ALPHA/BETA HYDROLASE, ALPHA/BETA HYDROLASE
KEYWDS 2 FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 22-JAN-08 3BWX 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF AN ALPHA/BETA HYDROLASE
JRNL TITL 2 (YP_496220.1) FROM NOVOSPHINGOBIUM AROMATICIVORANS
JRNL TITL 3 DSM 12444 AT 1.50 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 41469
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2095
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2838
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2604
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.06000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.080
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.960
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2303 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1617 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3110 ; 1.671 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3893 ; 1.041 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 290 ; 5.775 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 98 ;35.231 ;22.449
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 356 ;12.551 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;18.191 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 338 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2572 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 478 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 484 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1859 ; 0.211 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1119 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1173 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 244 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.091 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 22 ; 0.240 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 54 ; 0.280 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.204 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.020 ; 0.200
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): 1495 ; 2.061 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 580 ; 0.526 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2300 ; 2.605 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 947 ; 4.065 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 810 ; 5.445 ;11.000
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 0 A 284
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0076 36.5432 13.1223
REMARK 3 T TENSOR
REMARK 3 T11: -0.0244 T22: -0.0166
REMARK 3 T33: -0.0189 T12: 0.0009
REMARK 3 T13: -0.0031 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.2816 L22: 0.4219
REMARK 3 L33: 0.3725 L12: -0.1384
REMARK 3 L13: 0.0239 L23: -0.0571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: 0.0151 S13: -0.0262
REMARK 3 S21: -0.0119 S22: 0.0036 S23: 0.0211
REMARK 3 S31: 0.0050 S32: -0.0327 S33: -0.0092
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
REMARK 3 PARTIAL S-MET INCORPORATION. 4. CA IONS AND CL IONS WERE
REMARK 3 MODELED BASED ON CRYSTALLIZATION CONDITION, ETHYLENE GLYCOL
REMARK 3 (EDO) MOLECULES WERE MODELED BASED ON CRYO CONDITION.
REMARK 4
REMARK 4 3BWX COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-NOV-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41517
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 27.714
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.70400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M CACL2, 20.0% PEG
REMARK 280 3350, NO BUFFER PH 5.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 22.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.11000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.11000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.97500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 5 CD OE1 OE2
REMARK 470 LYS A 72 CE NZ
REMARK 470 GLU A 96 OE1 OE2
REMARK 470 LEU A 108 CD1 CD2
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 ARG A 140 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 147 CD OE1 NE2
REMARK 470 SER A 189 OG
REMARK 470 SER A 190 OG
REMARK 470 GLN A 214 CG CD OE1 NE2
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 179 NE - CZ - NH2 ANGL. DEV. = -4.1 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 A 104 -121.77 58.25
REMARK 500 ASN A 117 92.85 -178.09
REMARK 500 PHE A 205 -121.40 47.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 285 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 204 O
REMARK 620 2 ALA A 207 O 67.7
REMARK 620 3 HOH A 352 O 80.4 90.9
REMARK 620 4 HOH A 424 O 136.4 70.1 90.2
REMARK 620 5 HOH A 357 O 151.6 139.8 101.9 72.0
REMARK 620 6 HOH A 349 O 91.7 99.6 163.4 105.4 78.2
REMARK 620 7 HOH A 363 O 78.8 146.5 83.9 142.7 73.4 80.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 286 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 525 O
REMARK 620 2 HOH A 505 O 94.1
REMARK 620 3 HOH A 446 O 92.1 87.3
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 387108 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1. THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
REMARK 999 2. THE CONSTRUCT WAS ENGINEERED WITH THE FOLLOWING
REMARK 999 MUTATION: A209V.
DBREF 3BWX A 1 284 UNP Q2G9T7 Q2G9T7_NOVAD 1 284
SEQADV 3BWX GLY A 0 UNP Q2G9T7 LEADER SEQUENCE
SEQADV 3BWX VAL A 209 UNP Q2G9T7 ALA 209 ENGINEERED
SEQRES 1 A 285 GLY MSE ALA GLU TYR GLU ASP ARG TYR TRP THR SER SER
SEQRES 2 A 285 ASP GLY LEU ARG LEU HIS PHE ARG ALA TYR GLU GLY ASP
SEQRES 3 A 285 ILE SER ARG PRO PRO VAL LEU CYS LEU PRO GLY LEU THR
SEQRES 4 A 285 ARG ASN ALA ARG ASP PHE GLU ASP LEU ALA THR ARG LEU
SEQRES 5 A 285 ALA GLY ASP TRP ARG VAL LEU CYS PRO GLU MSE ARG GLY
SEQRES 6 A 285 ARG GLY ASP SER ASP TYR ALA LYS ASP PRO MSE THR TYR
SEQRES 7 A 285 GLN PRO MSE GLN TYR LEU GLN ASP LEU GLU ALA LEU LEU
SEQRES 8 A 285 ALA GLN GLU GLY ILE GLU ARG PHE VAL ALA ILE GLY THR
SEQRES 9 A 285 SER LEU GLY GLY LEU LEU THR MSE LEU LEU ALA ALA ALA
SEQRES 10 A 285 ASN PRO ALA ARG ILE ALA ALA ALA VAL LEU ASN ASP VAL
SEQRES 11 A 285 GLY PRO GLU VAL SER PRO GLU GLY LEU GLU ARG ILE ARG
SEQRES 12 A 285 GLY TYR VAL GLY GLN GLY ARG ASN PHE GLU THR TRP MSE
SEQRES 13 A 285 HIS ALA ALA ARG ALA LEU GLN GLU SER SER GLY ASP VAL
SEQRES 14 A 285 TYR PRO ASP TRP ASP ILE THR GLN TRP LEU ARG TYR ALA
SEQRES 15 A 285 LYS ARG ILE MSE VAL LEU GLY SER SER GLY ARG ILE ALA
SEQRES 16 A 285 PHE ASP TYR ASP MSE LYS ILE ALA GLU PRO PHE GLU ALA
SEQRES 17 A 285 PRO VAL GLY ALA THR PRO GLN VAL ASP MSE TRP PRO LEU
SEQRES 18 A 285 PHE ASP ALA LEU ALA THR ARG PRO LEU LEU VAL LEU ARG
SEQRES 19 A 285 GLY GLU THR SER ASP ILE LEU SER ALA GLN THR ALA ALA
SEQRES 20 A 285 LYS MSE ALA SER ARG PRO GLY VAL GLU LEU VAL THR LEU
SEQRES 21 A 285 PRO ARG ILE GLY HIS ALA PRO THR LEU ASP GLU PRO GLU
SEQRES 22 A 285 SER ILE ALA ALA ILE GLY ARG LEU LEU GLU ARG VAL
MODRES 3BWX MSE A 1 MET SELENOMETHIONINE
MODRES 3BWX MSE A 62 MET SELENOMETHIONINE
MODRES 3BWX MSE A 75 MET SELENOMETHIONINE
MODRES 3BWX MSE A 80 MET SELENOMETHIONINE
MODRES 3BWX MSE A 111 MET SELENOMETHIONINE
MODRES 3BWX MSE A 155 MET SELENOMETHIONINE
MODRES 3BWX MSE A 185 MET SELENOMETHIONINE
MODRES 3BWX MSE A 199 MET SELENOMETHIONINE
MODRES 3BWX MSE A 217 MET SELENOMETHIONINE
MODRES 3BWX MSE A 248 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 62 8
HET MSE A 75 8
HET MSE A 80 8
HET MSE A 111 8
HET MSE A 155 8
HET MSE A 185 8
HET MSE A 199 16
HET MSE A 217 8
HET MSE A 248 8
HET CA A 285 1
HET CA A 286 1
HET CL A 287 1
HET CL A 288 1
HET EDO A 289 4
HET EDO A 290 4
HET EDO A 291 4
HET EDO A 292 4
HET EDO A 293 4
HET EDO A 294 4
HET EDO A 295 4
HET EDO A 296 4
HET EDO A 297 4
HET EDO A 298 4
HET EDO A 299 4
HET EDO A 300 4
HET EDO A 301 4
HET EDO A 302 4
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 CA 2(CA 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 6 EDO 14(C2 H6 O2)
FORMUL 20 HOH *336(H2 O)
HELIX 1 1 ASN A 40 ASP A 43 5 4
HELIX 2 2 PHE A 44 ALA A 52 1 9
HELIX 3 3 ASP A 73 TYR A 77 5 5
HELIX 4 4 GLN A 78 GLY A 94 1 17
HELIX 5 5 SER A 104 ASN A 117 1 14
HELIX 6 6 SER A 134 VAL A 145 1 12
HELIX 7 7 THR A 153 GLY A 166 1 14
HELIX 8 8 ASP A 173 ILE A 184 1 12
HELIX 9 9 ASP A 198 GLU A 203 5 6
HELIX 10 10 MSE A 217 ALA A 225 1 9
HELIX 11 11 SER A 241 SER A 250 1 10
HELIX 12 12 GLU A 270 GLU A 282 1 13
SHEET 1 A 8 GLU A 5 THR A 10 0
SHEET 2 A 8 ARG A 16 TYR A 22 -1 O PHE A 19 N ARG A 7
SHEET 3 A 8 VAL A 57 PRO A 60 -1 O VAL A 57 N TYR A 22
SHEET 4 A 8 VAL A 31 LEU A 34 1 N VAL A 31 O LEU A 58
SHEET 5 A 8 PHE A 98 THR A 103 1 O VAL A 99 N LEU A 32
SHEET 6 A 8 ILE A 121 ASN A 127 1 O ASN A 127 N GLY A 102
SHEET 7 A 8 LEU A 229 GLY A 234 1 O LEU A 232 N LEU A 126
SHEET 8 A 8 VAL A 254 LEU A 259 1 O GLU A 255 N VAL A 231
SHEET 1 B 3 ASN A 150 PHE A 151 0
SHEET 2 B 3 ILE A 193 PHE A 195 -1 O ILE A 193 N PHE A 151
SHEET 3 B 3 MSE A 185 LEU A 187 -1 N VAL A 186 O ALA A 194
LINK O PRO A 204 CA CA A 285 1555 1555 2.47
LINK O ALA A 207 CA CA A 285 1555 1555 2.39
LINK CA CA A 285 O HOH A 352 1555 1555 2.39
LINK CA CA A 285 O HOH A 424 1555 1555 2.43
LINK CA CA A 285 O HOH A 357 1555 1555 2.63
LINK CA CA A 285 O HOH A 349 1555 1555 2.33
LINK CA CA A 285 O HOH A 363 1555 1555 2.44
LINK CA CA A 286 O HOH A 525 1555 1555 2.26
LINK CA CA A 286 O HOH A 505 1555 1555 2.36
LINK CA CA A 286 O HOH A 446 1555 1555 2.47
CISPEP 1 HIS A 264 ALA A 265 0 -5.47
CRYST1 44.480 69.950 82.220 90.00 90.00 90.00 P 21 21 21 4
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 0.022482 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012162 0.00000
TER 2209 VAL A 284
MASTER 346 0 28 12 11 0 0 6 2604 1 157 22
END |