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HEADER HYDROLASE 02-DEC-22 8HM5
TITLE EPOXIDE HYDROLASE FROM CABALLERONIA SORDIDICOLA PAMC 26510
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CABALLERONIA SORDIDICOLA;
SOURCE 3 ORGANISM_TAXID: 196367;
SOURCE 4 GENE: PAMC26510_32755;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACTERIAL EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HWANG,M.J.LEE,H.DO,J.H.LEE
REVDAT 1 06-DEC-23 8HM5 0
JRNL AUTH J.HWANG,M.J.LEE,H.DO,J.H.LEE
JRNL TITL EPOXIDE HYDROLASE FROM CABALLERONIA SORDIDICOLA PAMC 26510
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 20329
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 974
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.43
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1913
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4942
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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 : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8HM5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-22.
REMARK 100 THE DEPOSITION ID IS D_1300033749.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-20
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CONFOCAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 81.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.100
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 (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM FORMATE AND 20% (W/V)
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
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 40.60500
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 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 MET A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 ASP A 4
REMARK 465 ILE A 5
REMARK 465 THR A 6
REMARK 465 LEU A 323
REMARK 465 SER A 324
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 ASP B 4
REMARK 465 ILE B 5
REMARK 465 THR B 6
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU A 310 CB - CA - C ANGL. DEV. = 12.6 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 ASP A 106 -129.22 62.14
REMARK 500 SER A 130 -45.48 70.58
REMARK 500 TRP A 299 57.85 -90.98
REMARK 500 ASP B 106 -126.69 63.74
REMARK 500 SER B 130 -51.80 73.51
REMARK 500 PRO B 206 53.19 -92.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 277 -13.43
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 8HM5 A 1 324 UNP A0A242M8J4_9BURK
DBREF2 8HM5 A A0A242M8J4 6 329
DBREF1 8HM5 B 1 324 UNP A0A242M8J4_9BURK
DBREF2 8HM5 B A0A242M8J4 6 329
SEQRES 1 A 324 MET THR SER ASP ILE THR GLY GLY VAL LYS GLU TYR ASP
SEQRES 2 A 324 ILE ALA THR ASN GLY ILE SER LEU HIS VAL THR GLU GLN
SEQRES 3 A 324 GLY ALA GLY PRO ALA VAL LEU PHE CYS HIS GLY PHE PRO
SEQRES 4 A 324 ASP THR SER TYR THR TRP ARG ARG GLN MET ASN ALA ILE
SEQRES 5 A 324 ALA SER ALA GLY TYR ARG ALA ILE ALA PRO ASP MET ARG
SEQRES 6 A 324 GLY TYR GLY ARG SER SER ALA PRO ALA ASP ALA SER LEU
SEQRES 7 A 324 TYR THR PRO LEU HIS THR THR GLY ASP LEU ILE GLY LEU
SEQRES 8 A 324 LEU ASP ALA LEU LYS ILE SER SER ALA VAL LEU VAL GLY
SEQRES 9 A 324 HIS ASP TRP GLY ALA THR HIS ALA TRP ASN ALA ALA LEU
SEQRES 10 A 324 MET ARG PRO ASP ARG PHE LYS ALA VAL PHE GLY LEU SER
SEQRES 11 A 324 VAL PRO PHE VAL THR ARG GLY GLU SER SER VAL PHE GLU
SEQRES 12 A 324 ARG MET ARG GLU SER GLY ARG GLN ASP ASP PHE TYR MET
SEQRES 13 A 324 PHE GLU GLN ILE ARG PRO ASP ALA ASP GLN ILE TRP ALA
SEQRES 14 A 324 ASP ALA ALA VAL THR ILE PRO GLY ILE LEU TYR TRP ALA
SEQRES 15 A 324 SER GLY SER ALA PRO GLU GLY GLU GLN TRP SER PRO LEU
SEQRES 16 A 324 ASP ARG THR ARG SER LEU TYR ARG ALA ALA PRO GLY PRO
SEQRES 17 A 324 LEU PRO SER TRP ALA GLU ALA ASP TYR VAL ALA HIS ASN
SEQRES 18 A 324 ILE ALA GLU PHE ARG ARG THR GLY PHE HIS GLY GLY LEU
SEQRES 19 A 324 ASN TYR TYR ARG ALA ALA GLU PRO TYR PHE THR LEU SER
SEQRES 20 A 324 ALA PRO TRP LYS GLY ALA LYS ILE THR GLN PRO SER PHE
SEQRES 21 A 324 PHE ILE TRP GLY LYS SER ASP GLY LEU LYS GLU LEU TYR
SEQRES 22 A 324 PRO PHE THR LEU GLN GLN MET ARG ALA GLY LEU PRO GLY
SEQRES 23 A 324 LEU MET GLY GLY LEU GLU LEU ASP ASN VAL GLY HIS TRP
SEQRES 24 A 324 VAL GLN HIS GLU ALA SER ALA GLU VAL SER GLU GLN LEU
SEQRES 25 A 324 VAL ARG PHE LEU ARG THR VAL ASP ALA VAL LEU SER
SEQRES 1 B 324 MET THR SER ASP ILE THR GLY GLY VAL LYS GLU TYR ASP
SEQRES 2 B 324 ILE ALA THR ASN GLY ILE SER LEU HIS VAL THR GLU GLN
SEQRES 3 B 324 GLY ALA GLY PRO ALA VAL LEU PHE CYS HIS GLY PHE PRO
SEQRES 4 B 324 ASP THR SER TYR THR TRP ARG ARG GLN MET ASN ALA ILE
SEQRES 5 B 324 ALA SER ALA GLY TYR ARG ALA ILE ALA PRO ASP MET ARG
SEQRES 6 B 324 GLY TYR GLY ARG SER SER ALA PRO ALA ASP ALA SER LEU
SEQRES 7 B 324 TYR THR PRO LEU HIS THR THR GLY ASP LEU ILE GLY LEU
SEQRES 8 B 324 LEU ASP ALA LEU LYS ILE SER SER ALA VAL LEU VAL GLY
SEQRES 9 B 324 HIS ASP TRP GLY ALA THR HIS ALA TRP ASN ALA ALA LEU
SEQRES 10 B 324 MET ARG PRO ASP ARG PHE LYS ALA VAL PHE GLY LEU SER
SEQRES 11 B 324 VAL PRO PHE VAL THR ARG GLY GLU SER SER VAL PHE GLU
SEQRES 12 B 324 ARG MET ARG GLU SER GLY ARG GLN ASP ASP PHE TYR MET
SEQRES 13 B 324 PHE GLU GLN ILE ARG PRO ASP ALA ASP GLN ILE TRP ALA
SEQRES 14 B 324 ASP ALA ALA VAL THR ILE PRO GLY ILE LEU TYR TRP ALA
SEQRES 15 B 324 SER GLY SER ALA PRO GLU GLY GLU GLN TRP SER PRO LEU
SEQRES 16 B 324 ASP ARG THR ARG SER LEU TYR ARG ALA ALA PRO GLY PRO
SEQRES 17 B 324 LEU PRO SER TRP ALA GLU ALA ASP TYR VAL ALA HIS ASN
SEQRES 18 B 324 ILE ALA GLU PHE ARG ARG THR GLY PHE HIS GLY GLY LEU
SEQRES 19 B 324 ASN TYR TYR ARG ALA ALA GLU PRO TYR PHE THR LEU SER
SEQRES 20 B 324 ALA PRO TRP LYS GLY ALA LYS ILE THR GLN PRO SER PHE
SEQRES 21 B 324 PHE ILE TRP GLY LYS SER ASP GLY LEU LYS GLU LEU TYR
SEQRES 22 B 324 PRO PHE THR LEU GLN GLN MET ARG ALA GLY LEU PRO GLY
SEQRES 23 B 324 LEU MET GLY GLY LEU GLU LEU ASP ASN VAL GLY HIS TRP
SEQRES 24 B 324 VAL GLN HIS GLU ALA SER ALA GLU VAL SER GLU GLN LEU
SEQRES 25 B 324 VAL ARG PHE LEU ARG THR VAL ASP ALA VAL LEU SER
FORMUL 3 HOH *182(H2 O)
HELIX 1 AA1 THR A 41 THR A 44 5 4
HELIX 2 AA2 TRP A 45 ALA A 55 1 11
HELIX 3 AA3 ASP A 75 TYR A 79 5 5
HELIX 4 AA4 THR A 80 LEU A 95 1 16
HELIX 5 AA5 ASP A 106 ARG A 119 1 14
HELIX 6 AA6 SER A 140 SER A 148 1 9
HELIX 7 AA7 PHE A 154 ARG A 161 1 8
HELIX 8 AA8 ASP A 163 ALA A 169 1 7
HELIX 9 AA9 ASP A 170 ALA A 182 1 13
HELIX 10 AB1 GLU A 214 GLY A 229 1 16
HELIX 11 AB2 PHE A 230 SER A 247 1 18
HELIX 12 AB3 ALA A 248 LYS A 251 5 4
HELIX 13 AB4 ASP A 267 TYR A 273 5 7
HELIX 14 AB5 THR A 276 ARG A 281 1 6
HELIX 15 AB6 TRP A 299 ALA A 304 1 6
HELIX 16 AB7 ALA A 304 VAL A 322 1 19
HELIX 17 AB8 THR B 41 THR B 44 5 4
HELIX 18 AB9 TRP B 45 SER B 54 1 10
HELIX 19 AC1 ASP B 75 TYR B 79 5 5
HELIX 20 AC2 THR B 80 LEU B 95 1 16
HELIX 21 AC3 ASP B 106 ARG B 119 1 14
HELIX 22 AC4 SER B 140 SER B 148 1 9
HELIX 23 AC5 PHE B 154 ARG B 161 1 8
HELIX 24 AC6 ASP B 163 ALA B 169 1 7
HELIX 25 AC7 ASP B 170 ALA B 182 1 13
HELIX 26 AC8 GLU B 214 GLY B 229 1 16
HELIX 27 AC9 PHE B 230 SER B 247 1 18
HELIX 28 AD1 ALA B 248 LYS B 251 5 4
HELIX 29 AD2 ASP B 267 TYR B 273 5 7
HELIX 30 AD3 TRP B 299 ALA B 304 1 6
HELIX 31 AD4 ALA B 304 SER B 324 1 21
SHEET 1 AA1 8 LYS A 10 THR A 16 0
SHEET 2 AA1 8 ILE A 19 GLN A 26 -1 O VAL A 23 N TYR A 12
SHEET 3 AA1 8 ARG A 58 PRO A 62 -1 O ALA A 59 N GLN A 26
SHEET 4 AA1 8 ALA A 31 CYS A 35 1 N PHE A 34 O ILE A 60
SHEET 5 AA1 8 ALA A 100 HIS A 105 1 O VAL A 101 N LEU A 33
SHEET 6 AA1 8 PHE A 123 LEU A 129 1 O ALA A 125 N LEU A 102
SHEET 7 AA1 8 SER A 259 GLY A 264 1 O PHE A 260 N GLY A 128
SHEET 8 AA1 8 LEU A 287 LEU A 293 1 O MET A 288 N SER A 259
SHEET 1 AA2 8 LYS B 10 THR B 16 0
SHEET 2 AA2 8 ILE B 19 GLY B 27 -1 O LEU B 21 N ILE B 14
SHEET 3 AA2 8 ARG B 58 PRO B 62 -1 O ALA B 61 N THR B 24
SHEET 4 AA2 8 ALA B 31 CYS B 35 1 N VAL B 32 O ILE B 60
SHEET 5 AA2 8 ALA B 100 HIS B 105 1 O VAL B 103 N CYS B 35
SHEET 6 AA2 8 PHE B 123 LEU B 129 1 O PHE B 127 N LEU B 102
SHEET 7 AA2 8 SER B 259 GLY B 264 1 O PHE B 260 N GLY B 128
SHEET 8 AA2 8 LEU B 287 LEU B 293 1 O MET B 288 N SER B 259
CISPEP 1 PHE A 38 PRO A 39 0 -26.02
CISPEP 2 PHE B 38 PRO B 39 0 -23.13
CRYST1 43.470 81.210 79.830 90.00 93.11 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 0.023004 0.000000 0.001250 0.00000
SCALE2 0.000000 0.012314 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012545 0.00000
TER 2465 VAL A 322
TER 4944 SER B 324
MASTER 302 0 0 31 16 0 0 6 5124 2 0 50
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