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HEADER HYDROLASE 29-NOV-06 2O2G
TITLE CRYSTAL STRUCTURE OF DIENELACTONE HYDROLASE (YP_324580.1)
TITLE 2 FROM ANABAENA VARIABILIS ATCC 29413 AT 1.92 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANABAENA VARIABILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: YP_324580.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS YP_324580.1, DIENELACTONE HYDROLASE, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 19-DEC-06 2O2G 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF DIENELACTONE HYDROLASE
JRNL TITL 2 (YP_324580.1) FROM ANABAENA VARIABILIS ATCC 29413
JRNL TITL 3 AT 1.92 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 14828
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 740
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 849
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 1822
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.74000
REMARK 3 B22 (A**2) : -1.24000
REMARK 3 B33 (A**2) : -1.50000
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): 0.190
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.172
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.103
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1688 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1576 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2308 ; 1.688 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3644 ; 0.917 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 225 ; 3.660 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;31.827 ;23.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 261 ;10.201 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;15.158 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 269 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1904 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 325 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 343 ; 0.214 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1619 ; 0.167 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 808 ; 0.175 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 1012 ; 0.083 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 216 ; 0.197 ; 0.500
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): 7 ; 0.103 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 58 ; 0.226 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.143 ; 0.500
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): 1110 ; 2.115 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 446 ; 0.620 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1745 ; 2.977 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 640 ; 5.410 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 558 ; 6.990 ;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 7 A 222
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1491 4.2548 15.1916
REMARK 3 T TENSOR
REMARK 3 T11: -0.1706 T22: -0.1423
REMARK 3 T33: -0.1384 T12: -0.0084
REMARK 3 T13: 0.0055 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.1062 L22: 2.0487
REMARK 3 L33: 1.8003 L12: -0.6773
REMARK 3 L13: 0.1588 L23: 0.3537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0565 S12: -0.0549 S13: -0.0105
REMARK 3 S21: 0.0035 S22: 0.0985 S23: 0.0002
REMARK 3 S31: -0.0339 S32: 0.0407 S33: -0.0420
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 0.70 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
REMARK 3 PARTIAL S-MET INCORPORATION. 4. TWO SULFATE MOLECULES FROM
REMARK 3 CRYSTALLIZATION SOLUTION AND TWO ETHYLENE GLYCOL MOLECULES
REMARK 3 (CRYOPROTECTANT) ARE INCLUDED IN THE MODEL. 5. ELECTRON
REMARK 3 DENSITY CORRESPONDING TO RESIDUES 1-6 WAS DISORDERED AND THESE
REMARK 3 RESIDUES WERE NOT MODELED.
REMARK 4
REMARK 4 2O2G COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-2006.
REMARK 100 THE RCSB ID CODE IS RCSB040602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94645, 0.97942, 0.97921
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS
REMARK 200 IN K-B GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR MAR300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14877
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 39.163
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.27500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.857
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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 (%): 41.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M (NH4)2SO4, 0.2M NACL, 0.1M
REMARK 280 CHES PH 9.5, VAPOR DIFFUSION, SITTING DROP, NANODROP,
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 23.94750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.99900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.23250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.99900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.94750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.23250
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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 GLY A 0
REMARK 465 MSE A 1
REMARK 465 ASP A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 THR A 6
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 HIS A 7 CB CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 8 CG CD OE1 NE2
REMARK 470 LYS A 22 CD CE NZ
REMARK 470 GLU A 78 CD OE1 OE2
REMARK 470 ARG A 82 CD NE CZ NH1 NH2
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LEU A 171 CG CD1 CD2
REMARK 470 ARG A 222 NE CZ NH1 NH2
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
REMARK 500 OE2 GLU A 11 ND2 ASN A 26 2.18
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 26 CB ASN A 26 CG 0.088
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 370216 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED
REMARK 999 WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0)
REMARK 999 FOLLOWED BY THE TARGET SEQUENCE.
DBREF 2O2G A 1 222 UNP Q3M5Q1 Q3M5Q1_ANAVT 1 222
SEQADV 2O2G GLY A 0 UNP Q3M5Q1 LEADER SEQUENCE
SEQADV 2O2G MSE A 1 UNP Q3M5Q1 MET 1 MODIFIED RESIDUE
SEQADV 2O2G MSE A 176 UNP Q3M5Q1 MET 176 MODIFIED RESIDUE
SEQADV 2O2G MSE A 218 UNP Q3M5Q1 MET 218 MODIFIED RESIDUE
SEQRES 1 A 223 GLY MSE ASP ARG THR LEU THR HIS GLN PRO GLN GLU TYR
SEQRES 2 A 223 ALA VAL SER VAL SER VAL GLY GLU VAL LYS LEU LYS GLY
SEQRES 3 A 223 ASN LEU VAL ILE PRO ASN GLY ALA THR GLY ILE VAL LEU
SEQRES 4 A 223 PHE ALA HIS GLY SER GLY SER SER ARG TYR SER PRO ARG
SEQRES 5 A 223 ASN ARG TYR VAL ALA GLU VAL LEU GLN GLN ALA GLY LEU
SEQRES 6 A 223 ALA THR LEU LEU ILE ASP LEU LEU THR GLN GLU GLU GLU
SEQRES 7 A 223 GLU ILE ASP LEU ARG THR ARG HIS LEU ARG PHE ASP ILE
SEQRES 8 A 223 GLY LEU LEU ALA SER ARG LEU VAL GLY ALA THR ASP TRP
SEQRES 9 A 223 LEU THR HIS ASN PRO ASP THR GLN HIS LEU LYS VAL GLY
SEQRES 10 A 223 TYR PHE GLY ALA SER THR GLY GLY GLY ALA ALA LEU VAL
SEQRES 11 A 223 ALA ALA ALA GLU ARG PRO GLU THR VAL GLN ALA VAL VAL
SEQRES 12 A 223 SER ARG GLY GLY ARG PRO ASP LEU ALA PRO SER ALA LEU
SEQRES 13 A 223 PRO HIS VAL LYS ALA PRO THR LEU LEU ILE VAL GLY GLY
SEQRES 14 A 223 TYR ASP LEU PRO VAL ILE ALA MSE ASN GLU ASP ALA LEU
SEQRES 15 A 223 GLU GLN LEU GLN THR SER LYS ARG LEU VAL ILE ILE PRO
SEQRES 16 A 223 ARG ALA SER HIS LEU PHE GLU GLU PRO GLY ALA LEU THR
SEQRES 17 A 223 ALA VAL ALA GLN LEU ALA SER GLU TRP PHE MSE HIS TYR
SEQRES 18 A 223 LEU ARG
MODRES 2O2G MSE A 176 MET SELENOMETHIONINE
MODRES 2O2G MSE A 218 MET SELENOMETHIONINE
HET MSE A 176 8
HET MSE A 218 13
HET SO4 1 5
HET SO4 2 5
HET EDO 3 4
HET EDO 4 4
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 2(C5 H11 N1 O2 SE1)
FORMUL 2 SO4 2(O4 S1 2-)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 6 HOH *168(H2 O1)
HELIX 1 1 SER A 49 ALA A 62 1 14
HELIX 2 2 THR A 73 ARG A 84 1 12
HELIX 3 3 ASP A 89 ASN A 107 1 19
HELIX 4 4 SER A 121 ARG A 134 1 14
HELIX 5 5 ARG A 147 ALA A 151 5 5
HELIX 6 6 ALA A 154 VAL A 158 5 5
HELIX 7 7 ASP A 170 LEU A 184 1 15
HELIX 8 8 GLY A 204 LEU A 221 1 18
SHEET 1 A 8 GLU A 11 VAL A 18 0
SHEET 2 A 8 VAL A 21 VAL A 28 -1 O VAL A 21 N VAL A 18
SHEET 3 A 8 ALA A 65 ILE A 69 -1 O LEU A 68 N ASN A 26
SHEET 4 A 8 GLY A 35 ALA A 40 1 N GLY A 35 O ALA A 65
SHEET 5 A 8 LYS A 114 ALA A 120 1 O GLY A 116 N LEU A 38
SHEET 6 A 8 VAL A 138 ARG A 144 1 O GLN A 139 N VAL A 115
SHEET 7 A 8 THR A 162 GLY A 167 1 O ILE A 165 N SER A 143
SHEET 8 A 8 LYS A 188 ILE A 193 1 O ARG A 189 N LEU A 164
CRYST1 47.895 62.465 67.998 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 0.020879 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014706 0.00000
TER 1637 ARG A 222
MASTER 315 0 6 8 8 0 0 6 1822 1 39 18
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