| content |
HEADER HYDROLASE 22-NOV-24 9EH6
TITLE CRYSTAL STRUCTURE OF AROC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-5 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDILINEA AEROPHILA;
SOURCE 3 ORGANISM_TAXID: 133453;
SOURCE 4 STRAIN: CALDILINEA AEROPHILA;
SOURCE 5 GENE: CLDAP_20430;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENZYME CATALYSIS, PET, SSNS, THERMOSTABILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.HU,K.KLUPT,D.ZECHEL,Z.JIA,G.HOWE
REVDAT 1 26-FEB-25 9EH6 0
JRNL AUTH Z.HU,K.KLUPT,D.ZECHEL,Z.JIA,G.HOWE
JRNL TITL MINING THERMOPHILE GENOMES FOR NEW PETASES WITH EXCEPTIONAL
JRNL TITL 2 STABILITIES USING SEQUENCE SIMILARITY NETWORKS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0415
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 18673
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 : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.831
REMARK 3 FREE R VALUE TEST SET COUNT : 902
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1288
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3286
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12100
REMARK 3 B22 (A**2) : 0.13200
REMARK 3 B33 (A**2) : 0.11300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.88600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.386
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.241
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.732
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3371 ; 0.006 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4607 ; 1.456 ; 1.644
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 433 ; 7.253 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 22 ; 6.257 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 466 ;17.086 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 504 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2700 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1461 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2266 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 131 ; 0.144 ; 0.200
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): 1741 ; 2.368 ; 1.922
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2171 ; 4.051 ; 3.440
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1630 ; 2.867 ; 2.160
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2436 ; 4.497 ; 3.839
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 BULK SOLVENT
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 NOT BEEN USED
REMARK 4
REMARK 4 9EH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-24.
REMARK 100 THE DEPOSITION ID IS D_1000290367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95299
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18709
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 46.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 4.5 8%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.40850
REMARK 290 SMTRY3 2 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: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 HIS A 1
REMARK 465 GLY A 220
REMARK 465 GLY A 221
REMARK 465 PHE A 222
REMARK 465 LEU A 223
REMARK 465 GLU A 224
REMARK 465 HIS A 225
REMARK 465 HIS A 226
REMARK 465 HIS A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 HIS A 230
REMARK 465 HIS B 1
REMARK 465 GLY B 220
REMARK 465 GLY B 221
REMARK 465 PHE B 222
REMARK 465 LEU B 223
REMARK 465 GLU B 224
REMARK 465 HIS B 225
REMARK 465 HIS B 226
REMARK 465 HIS B 227
REMARK 465 HIS B 228
REMARK 465 HIS B 229
REMARK 465 HIS B 230
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 MET A 2 SD CE
REMARK 470 MET B 2 SD CE
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 ASP A 16 -148.48 -125.07
REMARK 500 ALA A 33 -110.78 -59.16
REMARK 500 PHE A 79 -88.74 -97.50
REMARK 500 ASP A 80 74.29 59.37
REMARK 500 SER A 103 -124.33 62.28
REMARK 500 ASN A 180 -169.09 -122.00
REMARK 500 TRP A 186 74.22 -117.26
REMARK 500 TYR A 187 -155.72 -129.12
REMARK 500 ALA B 33 -94.23 -105.16
REMARK 500 VAL B 78 52.59 -91.92
REMARK 500 ARG B 83 -8.64 -55.80
REMARK 500 SER B 103 -130.27 62.79
REMARK 500 TYR B 187 -148.42 -134.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 188 GLU A 189 149.37
REMARK 500 GLY B 188 GLU B 189 139.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 36 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9EH6 A 3 222 UNP I0I495 I0I495_CALAS 26 245
DBREF 9EH6 B 3 222 UNP I0I495 I0I495_CALAS 26 245
SEQADV 9EH6 HIS A 1 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 MET A 2 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 LEU A 223 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 GLU A 224 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 225 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 226 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 227 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 228 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 229 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS A 230 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 1 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 MET B 2 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 LEU B 223 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 GLU B 224 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 225 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 226 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 227 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 228 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 229 UNP I0I495 EXPRESSION TAG
SEQADV 9EH6 HIS B 230 UNP I0I495 EXPRESSION TAG
SEQRES 1 A 230 HIS MET LEU GLN PRO MET ALA GLN ALA LEU ALA SER LEU
SEQRES 2 A 230 GLN GLY ASP ASP ARG VAL GLY VAL ILE GLU GLY ARG TRP
SEQRES 3 A 230 ILE VAL PHE GLN PRO LEU ALA ALA PRO ARG SER THR GLY
SEQRES 4 A 230 PHE ILE PHE TYR PRO GLY GLY ARG VAL ASP PRO ARG ALA
SEQRES 5 A 230 TYR ALA PRO GLN ALA ARG ALA ILE ALA GLU GLN GLY PHE
SEQRES 6 A 230 LEU VAL VAL ILE THR PRO MET PRO LEU ASN LEU ALA VAL
SEQRES 7 A 230 PHE ASP ALA ASP ARG ALA SER GLU VAL MET ALA ALA PHE
SEQRES 8 A 230 PRO GLU ILE GLU HIS TRP VAL ILE GLY GLY HIS SER LEU
SEQRES 9 A 230 GLY GLY ALA MET ALA ALA ASN PHE ALA HIS ASN HIS ILE
SEQRES 10 A 230 GLY ALA VAL GLU GLY VAL VAL PHE TRP ALA ALA TYR PRO
SEQRES 11 A 230 ALA GLN SER ASP SER LEU ALA ASP ARG ASP ASP LEU THR
SEQRES 12 A 230 VAL TYR SER ILE TYR GLY THR LEU ASP GLY LEU ALA THR
SEQRES 13 A 230 PRO ASP LYS ILE GLU ALA SER ARG ALA LEU LEU PRO ALA
SEQRES 14 A 230 THR ALA ARG PHE ILE PRO ILE GLU GLY GLY ASN HIS ALA
SEQRES 15 A 230 GLN PHE GLY TRP TYR GLY GLU GLN PRO GLY ASP ASN PRO
SEQRES 16 A 230 ALA THR ILE SER ARG ALA GLN GLN GLN GLN MET THR VAL
SEQRES 17 A 230 ASP ALA THR VAL GLU ALA LEU ALA VAL VAL ASP GLY GLY
SEQRES 18 A 230 PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 230 HIS MET LEU GLN PRO MET ALA GLN ALA LEU ALA SER LEU
SEQRES 2 B 230 GLN GLY ASP ASP ARG VAL GLY VAL ILE GLU GLY ARG TRP
SEQRES 3 B 230 ILE VAL PHE GLN PRO LEU ALA ALA PRO ARG SER THR GLY
SEQRES 4 B 230 PHE ILE PHE TYR PRO GLY GLY ARG VAL ASP PRO ARG ALA
SEQRES 5 B 230 TYR ALA PRO GLN ALA ARG ALA ILE ALA GLU GLN GLY PHE
SEQRES 6 B 230 LEU VAL VAL ILE THR PRO MET PRO LEU ASN LEU ALA VAL
SEQRES 7 B 230 PHE ASP ALA ASP ARG ALA SER GLU VAL MET ALA ALA PHE
SEQRES 8 B 230 PRO GLU ILE GLU HIS TRP VAL ILE GLY GLY HIS SER LEU
SEQRES 9 B 230 GLY GLY ALA MET ALA ALA ASN PHE ALA HIS ASN HIS ILE
SEQRES 10 B 230 GLY ALA VAL GLU GLY VAL VAL PHE TRP ALA ALA TYR PRO
SEQRES 11 B 230 ALA GLN SER ASP SER LEU ALA ASP ARG ASP ASP LEU THR
SEQRES 12 B 230 VAL TYR SER ILE TYR GLY THR LEU ASP GLY LEU ALA THR
SEQRES 13 B 230 PRO ASP LYS ILE GLU ALA SER ARG ALA LEU LEU PRO ALA
SEQRES 14 B 230 THR ALA ARG PHE ILE PRO ILE GLU GLY GLY ASN HIS ALA
SEQRES 15 B 230 GLN PHE GLY TRP TYR GLY GLU GLN PRO GLY ASP ASN PRO
SEQRES 16 B 230 ALA THR ILE SER ARG ALA GLN GLN GLN GLN MET THR VAL
SEQRES 17 B 230 ASP ALA THR VAL GLU ALA LEU ALA VAL VAL ASP GLY GLY
SEQRES 18 B 230 PHE LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *119(H2 O)
HELIX 1 AA1 ALA A 7 SER A 12 1 6
HELIX 2 AA2 ASP A 49 ALA A 52 5 4
HELIX 3 AA3 TYR A 53 GLN A 63 1 11
HELIX 4 AA4 ARG A 83 PHE A 91 1 9
HELIX 5 AA5 SER A 103 HIS A 116 1 14
HELIX 6 AA6 ALA A 131 SER A 135 5 5
HELIX 7 AA7 THR A 156 SER A 163 1 8
HELIX 8 AA8 ARG A 164 LEU A 167 5 4
HELIX 9 AA9 HIS A 181 GLY A 185 5 5
HELIX 10 AB1 SER A 199 ASP A 219 1 21
HELIX 11 AB2 MET B 6 LEU B 13 1 8
HELIX 12 AB3 ASP B 49 ALA B 52 5 4
HELIX 13 AB4 TYR B 53 GLU B 62 1 10
HELIX 14 AB5 ARG B 83 PHE B 91 1 9
HELIX 15 AB6 SER B 103 HIS B 116 1 14
HELIX 16 AB7 ALA B 131 SER B 135 5 5
HELIX 17 AB8 THR B 156 SER B 163 1 8
HELIX 18 AB9 ARG B 164 LEU B 167 5 4
HELIX 19 AC1 HIS B 181 GLY B 185 5 5
HELIX 20 AC2 SER B 199 ASP B 219 1 21
SHEET 1 AA1 8 VAL A 19 GLU A 23 0
SHEET 2 AA1 8 ILE A 27 PRO A 31 -1 O VAL A 28 N ILE A 22
SHEET 3 AA1 8 LEU A 66 ILE A 69 -1 O VAL A 67 N PHE A 29
SHEET 4 AA1 8 THR A 38 TYR A 43 1 N PHE A 42 O VAL A 68
SHEET 5 AA1 8 HIS A 96 HIS A 102 1 O VAL A 98 N ILE A 41
SHEET 6 AA1 8 GLY A 122 TRP A 126 1 O GLY A 122 N ILE A 99
SHEET 7 AA1 8 THR A 143 GLY A 149 1 O ILE A 147 N PHE A 125
SHEET 8 AA1 8 ARG A 172 ILE A 176 1 O ILE A 176 N TYR A 148
SHEET 1 AA2 8 VAL B 19 GLU B 23 0
SHEET 2 AA2 8 ILE B 27 PRO B 31 -1 O GLN B 30 N GLY B 20
SHEET 3 AA2 8 LEU B 66 ILE B 69 -1 O ILE B 69 N ILE B 27
SHEET 4 AA2 8 THR B 38 TYR B 43 1 N PHE B 40 O VAL B 68
SHEET 5 AA2 8 HIS B 96 HIS B 102 1 O HIS B 96 N GLY B 39
SHEET 6 AA2 8 GLY B 122 TRP B 126 1 O TRP B 126 N GLY B 101
SHEET 7 AA2 8 THR B 143 GLY B 149 1 O ILE B 147 N PHE B 125
SHEET 8 AA2 8 ARG B 172 ILE B 176 1 O ILE B 176 N TYR B 148
CRYST1 56.189 46.817 76.468 90.00 101.97 90.00 P 1 21 1 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 0.017797 0.000000 0.003773 0.00000
SCALE2 0.000000 0.021360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013368 0.00000
TER 1644 ASP A 219
TER 3288 ASP B 219
MASTER 328 0 0 20 16 0 0 6 3405 2 0 36
END |