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HEADER HYDROLASE 17-JUL-14 4U2F
TITLE CRYSTAL STRUCTURE OF DIENELACTONE HYDROLASE B-1 VARIANT (Q35H, F38L,
TITLE 2 Y64H, Q110L, C123S, Y137C, Y145C, N154D, E199G, S208G AND G211D) AT
TITLE 3 1.80 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYMETHYLENEBUTENOLIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIENELACTONE HYDROLASE,DLH;
COMPND 5 EC: 3.1.1.45;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 65741;
SOURCE 4 STRAIN: B13;
SOURCE 5 GENE: CLCD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA]
KEYWDS HYDROLASE, A/B HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.PORTER,C.A.COLLYER,D.L.OLLIS
REVDAT 1 10-DEC-14 4U2F 0
JRNL AUTH J.L.PORTER,P.L.BOON,T.P.MURRAY,T.HUBER,C.A.COLLYER,D.L.OLLIS
JRNL TITL DIRECTED EVOLUTION OF NEW AND IMPROVED ENZYME FUNCTIONS
JRNL TITL 2 USING AN EVOLUTIONARY INTERMEDIATE AND MULTI-DIRECTIONAL
JRNL TITL 3 SEARCH.
JRNL REF ACS CHEM.BIOL. 2014
JRNL REFN ESSN 1554-8937
JRNL PMID 25419863
JRNL DOI 10.1021/CB500809F
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 22895
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1204
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1544
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.34000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 0.02000
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): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.944
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1827 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2496 ; 1.571 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 244 ; 5.185 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;30.093 ;23.902
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 269 ;12.675 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.923 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 270 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1441 ; 0.009 ; 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 : 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4U2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27036
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 51.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, AMMONIUM SULPHATE
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.46700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.13200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.14750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.13200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.46700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.14750
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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 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 LYS A 234
REMARK 465 LYS A 235
REMARK 465 PRO A 236
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 ALA A 68 O HOH A 556 2.19
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 ASN A 41 -162.66 -121.21
REMARK 500 ALA A 68 108.30 -171.36
REMARK 500 ALA A 72 82.47 -151.49
REMARK 500 SER A 123 -121.84 58.19
REMARK 500 SER A 203 43.42 -106.93
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 SO4 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4U2B RELATED DB: PDB
REMARK 900 RELATED ID: 4U2C RELATED DB: PDB
REMARK 900 RELATED ID: 4U2D RELATED DB: PDB
REMARK 900 RELATED ID: 4U2E RELATED DB: PDB
REMARK 900 RELATED ID: 4U2G RELATED DB: PDB
DBREF 4U2F A 1 236 UNP P0A115 CLCD_PSESB 1 236
SEQADV 4U2F HIS A 35 UNP P0A115 GLN 35 ENGINEERED MUTATION
SEQADV 4U2F LEU A 38 UNP P0A115 PHE 38 ENGINEERED MUTATION
SEQADV 4U2F HIS A 64 UNP P0A115 TYR 64 ENGINEERED MUTATION
SEQADV 4U2F ALA A 79 UNP P0A115 ARG 79 CONFLICT
SEQADV 4U2F LEU A 110 UNP P0A115 GLN 110 ENGINEERED MUTATION
SEQADV 4U2F SER A 123 UNP P0A115 CYS 123 ENGINEERED MUTATION
SEQADV 4U2F CYS A 137 UNP P0A115 TYR 137 ENGINEERED MUTATION
SEQADV 4U2F CYS A 145 UNP P0A115 TYR 145 ENGINEERED MUTATION
SEQADV 4U2F ASP A 154 UNP P0A115 LYS 154 ENGINEERED MUTATION
SEQADV 4U2F GLY A 199 UNP P0A115 GLU 199 ENGINEERED MUTATION
SEQADV 4U2F GLY A 208 UNP P0A115 SER 208 ENGINEERED MUTATION
SEQADV 4U2F ASP A 211 UNP P0A115 GLY 211 ENGINEERED MUTATION
SEQADV 4U2F THR A 224 UNP P0A115 ARG 224 CONFLICT
SEQRES 1 A 236 MET LEU THR GLU GLY ILE SER ILE GLN SER TYR ASP GLY
SEQRES 2 A 236 HIS THR PHE GLY ALA LEU VAL GLY SER PRO ALA LYS ALA
SEQRES 3 A 236 PRO ALA PRO VAL ILE VAL ILE ALA HIS GLU ILE LEU GLY
SEQRES 4 A 236 VAL ASN ALA PHE MET ARG GLU THR VAL SER TRP LEU VAL
SEQRES 5 A 236 ASP GLN GLY TYR ALA ALA VAL CYS PRO ASP LEU HIS ALA
SEQRES 6 A 236 ARG GLN ALA PRO GLY THR ALA LEU ASP PRO GLN ASP GLU
SEQRES 7 A 236 ALA GLN ARG GLU GLN ALA TYR LYS LEU TRP GLN ALA PHE
SEQRES 8 A 236 ASP MET GLU ALA GLY VAL GLY ASP LEU GLU ALA ALA ILE
SEQRES 9 A 236 ARG TYR ALA ARG HIS LEU PRO TYR SER ASN GLY LYS VAL
SEQRES 10 A 236 GLY LEU VAL GLY TYR SER LEU GLY GLY ALA LEU ALA PHE
SEQRES 11 A 236 LEU VAL ALA ALA LYS GLY CYS VAL ASP ARG ALA VAL GLY
SEQRES 12 A 236 TYR CYS GLY VAL GLY LEU GLU LYS GLN LEU ASP LYS VAL
SEQRES 13 A 236 PRO GLU VAL LYS HIS PRO ALA LEU PHE HIS MET GLY GLY
SEQRES 14 A 236 GLN ASP HIS PHE VAL PRO ALA PRO SER ARG GLN LEU ILE
SEQRES 15 A 236 THR GLU GLY PHE GLY ALA ASN PRO LEU LEU GLN VAL HIS
SEQRES 16 A 236 TRP TYR GLU GLY ALA GLY HIS SER PHE ALA ARG THR GLY
SEQRES 17 A 236 SER SER ASP TYR VAL ALA SER ALA ALA ALA LEU ALA ASN
SEQRES 18 A 236 GLU ARG THR LEU ASP PHE LEU ALA PRO LEU GLN SER LYS
SEQRES 19 A 236 LYS PRO
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *173(H2 O)
HELIX 1 AA1 ASN A 41 GLN A 54 1 14
HELIX 2 AA2 LEU A 63 GLN A 67 5 5
HELIX 3 AA3 ASP A 77 PHE A 91 1 15
HELIX 4 AA4 ASP A 92 HIS A 109 1 18
HELIX 5 AA5 SER A 123 GLY A 136 1 14
HELIX 6 AA6 GLY A 148 VAL A 159 5 12
HELIX 7 AA7 PRO A 175 ALA A 188 1 14
HELIX 8 AA8 VAL A 213 ALA A 229 1 17
HELIX 9 AA9 PRO A 230 GLN A 232 5 3
SHEET 1 AA1 2 ILE A 8 GLN A 9 0
SHEET 2 AA1 2 THR A 15 PHE A 16 -1 O PHE A 16 N ILE A 8
SHEET 1 AA2 7 ALA A 18 GLY A 21 0
SHEET 2 AA2 7 ALA A 57 PRO A 61 -1 O CYS A 60 N LEU A 19
SHEET 3 AA2 7 ALA A 28 ALA A 34 1 N ILE A 33 O VAL A 59
SHEET 4 AA2 7 SER A 113 TYR A 122 1 O GLY A 118 N VAL A 32
SHEET 5 AA2 7 ARG A 140 TYR A 144 1 O TYR A 144 N GLY A 121
SHEET 6 AA2 7 ALA A 163 GLY A 168 1 O LEU A 164 N GLY A 143
SHEET 7 AA2 7 LEU A 192 TYR A 197 1 O HIS A 195 N PHE A 165
CISPEP 1 ALA A 26 PRO A 27 0 -2.45
SITE 1 AC1 3 MET A 1 ALA A 72 HOH A 554
CRYST1 48.934 70.295 74.264 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 0.020436 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014226 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013465 0.00000
TER 1780 SER A 233
MASTER 288 0 1 9 9 0 1 6 1928 1 5 19
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