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HEADER HYDROLASE 15-NOV-22 8HGU
TITLE EPOXIDE HYDROLASE FROM BOSEA SP. PAMC 26642
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOSEA SP. PAMC 26642;
SOURCE 3 ORGANISM_TAXID: 1792307;
SOURCE 4 GENE: AXW83_17570;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.LEE,J.HWANG,H.DO,J.H.LEE
REVDAT 1 22-NOV-23 8HGU 0
JRNL AUTH M.J.LEE,J.HWANG,H.DO,J.H.LEE
JRNL TITL EPOXIDE HYDROLASE FROM BOSEA SP. PAMC 26642
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 1.20.1_4487
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.450
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 101068
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 644
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.80
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): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8HGU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1300033594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-22
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 : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101095
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.230
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: 1EHY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M AMMONIUM FORMATE, 0.1 M SODIUM
REMARK 280 ACETATE PH 5.0, 8 % W/V PGA (NA+ FORM, LM), VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 296.15K
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 42.45650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 18.59263
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -96.45947
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 GLY A 297
REMARK 465 ARG A 298
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 297
REMARK 465 ARG B 298
REMARK 465 MET C 1
REMARK 465 GLY C 297
REMARK 465 ARG C 298
REMARK 465 MET D 1
REMARK 465 GLY D 297
REMARK 465 ARG D 298
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 HOH C 409 O HOH C 426 1.95
REMARK 500 O HOH D 404 O HOH D 450 2.01
REMARK 500 O HOH D 437 O HOH D 459 2.02
REMARK 500 O HOH A 438 O HOH A 445 2.04
REMARK 500 O HOH C 388 O HOH C 429 2.09
REMARK 500 O PRO A 9 O HOH A 301 2.12
REMARK 500 O HOH C 412 O HOH C 438 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 236 CG - CD - NE ANGL. DEV. = -15.5 DEGREES
REMARK 500 ARG D 19 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG D 19 NE - CZ - NH2 ANGL. DEV. = -5.7 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 ARG A 19 -129.63 50.63
REMARK 500 VAL A 82 67.78 -111.61
REMARK 500 ASP A 109 -129.54 59.66
REMARK 500 PHE A 278 66.30 -115.47
REMARK 500 ARG B 19 -126.58 47.13
REMARK 500 PHE B 44 -178.33 -171.07
REMARK 500 VAL B 82 65.13 -117.36
REMARK 500 ASP B 109 -129.00 60.52
REMARK 500 HIS B 122 57.38 -142.64
REMARK 500 PHE B 278 64.82 -113.80
REMARK 500 VAL C 82 65.72 -114.28
REMARK 500 ASP C 109 -133.13 62.64
REMARK 500 PHE C 278 71.42 -113.06
REMARK 500 ARG D 19 -127.37 42.75
REMARK 500 VAL D 82 64.98 -117.67
REMARK 500 ASP D 109 -136.75 58.81
REMARK 500 ASP D 266 85.88 -157.85
REMARK 500 PHE D 278 70.40 -111.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8HGU A 1 298 PDB 8HGU 8HGU 1 298
DBREF 8HGU B 1 298 PDB 8HGU 8HGU 1 298
DBREF 8HGU C 1 298 PDB 8HGU 8HGU 1 298
DBREF 8HGU D 1 298 PDB 8HGU 8HGU 1 298
SEQRES 1 A 298 MET SER SER ASP PHE ALA THR PRO PRO GLY LEU ARG HIS
SEQRES 2 A 298 ARG GLN ILE ALA VAL ARG ASP THR THR LEU HIS VAL ALA
SEQRES 3 A 298 GLU ILE GLY SER GLY GLY THR PRO VAL LEU LEU LEU HIS
SEQRES 4 A 298 GLY TRP PRO GLU PHE TRP ALA THR TRP LEU PRO LEU MET
SEQRES 5 A 298 ASN ARG LEU HIS ASP GLN PHE HIS LEU ILE ALA PRO ASP
SEQRES 6 A 298 LEU ARG GLY PHE GLY ASP SER GLU LYS SER ALA VAL PRO
SEQRES 7 A 298 ARG SER ASP VAL GLY ALA ASN SER HIS ALA ASP ASP MET
SEQRES 8 A 298 ALA ALA LEU LEU GLY ALA LEU GLY LEU GLU SER VAL GLY
SEQRES 9 A 298 VAL VAL GLY HIS ASP VAL GLY ALA TYR ALA ALA GLN ALA
SEQRES 10 A 298 LEU ALA ARG ARG HIS PRO GLN LEU VAL ASP ARG LEU LEU
SEQRES 11 A 298 PHE PHE ASN CYS PRO THR ALA SER VAL GLY GLY ALA TRP
SEQRES 12 A 298 VAL HIS HIS GLY HIS VAL ASN GLU VAL TRP TYR GLN SER
SEQRES 13 A 298 PHE GLN GLN LEU GLY LEU ALA GLU ALA LEU VAL GLY THR
SEQRES 14 A 298 SER ARG GLU THR CYS ALA LEU TYR PHE ARG HIS PHE LEU
SEQRES 15 A 298 GLU HIS TRP SER HIS ARG LYS ASP ALA PHE GLU PRO ALA
SEQRES 16 A 298 PHE GLU LEU TRP ILE ASP ASN PHE MET LYS PRO GLY ASN
SEQRES 17 A 298 LEU ARG GLY GLY PHE ASP TRP TYR ARG SER GLN ASN ALA
SEQRES 18 A 298 LEU ARG LEU ALA ALA ILE ASP GLY HIS PRO THR PRO SER
SEQRES 19 A 298 VAL ARG ILE HIS GLN PRO THR ARG VAL HIS TRP GLY ARG
SEQRES 20 A 298 HIS ASP PRO ILE LEU LYS SER GLU TRP SER ALA PHE VAL
SEQRES 21 A 298 PRO GLU HIS PHE ASP ASP ALA ARG ILE SER PHE CYS GLU
SEQRES 22 A 298 SER ALA GLY HIS PHE VAL HIS VAL GLU ALA PRO ASP GLU
SEQRES 23 A 298 ALA ALA ASP VAL LEU ALA GLU PHE PHE GLY GLY ARG
SEQRES 1 B 298 MET SER SER ASP PHE ALA THR PRO PRO GLY LEU ARG HIS
SEQRES 2 B 298 ARG GLN ILE ALA VAL ARG ASP THR THR LEU HIS VAL ALA
SEQRES 3 B 298 GLU ILE GLY SER GLY GLY THR PRO VAL LEU LEU LEU HIS
SEQRES 4 B 298 GLY TRP PRO GLU PHE TRP ALA THR TRP LEU PRO LEU MET
SEQRES 5 B 298 ASN ARG LEU HIS ASP GLN PHE HIS LEU ILE ALA PRO ASP
SEQRES 6 B 298 LEU ARG GLY PHE GLY ASP SER GLU LYS SER ALA VAL PRO
SEQRES 7 B 298 ARG SER ASP VAL GLY ALA ASN SER HIS ALA ASP ASP MET
SEQRES 8 B 298 ALA ALA LEU LEU GLY ALA LEU GLY LEU GLU SER VAL GLY
SEQRES 9 B 298 VAL VAL GLY HIS ASP VAL GLY ALA TYR ALA ALA GLN ALA
SEQRES 10 B 298 LEU ALA ARG ARG HIS PRO GLN LEU VAL ASP ARG LEU LEU
SEQRES 11 B 298 PHE PHE ASN CYS PRO THR ALA SER VAL GLY GLY ALA TRP
SEQRES 12 B 298 VAL HIS HIS GLY HIS VAL ASN GLU VAL TRP TYR GLN SER
SEQRES 13 B 298 PHE GLN GLN LEU GLY LEU ALA GLU ALA LEU VAL GLY THR
SEQRES 14 B 298 SER ARG GLU THR CYS ALA LEU TYR PHE ARG HIS PHE LEU
SEQRES 15 B 298 GLU HIS TRP SER HIS ARG LYS ASP ALA PHE GLU PRO ALA
SEQRES 16 B 298 PHE GLU LEU TRP ILE ASP ASN PHE MET LYS PRO GLY ASN
SEQRES 17 B 298 LEU ARG GLY GLY PHE ASP TRP TYR ARG SER GLN ASN ALA
SEQRES 18 B 298 LEU ARG LEU ALA ALA ILE ASP GLY HIS PRO THR PRO SER
SEQRES 19 B 298 VAL ARG ILE HIS GLN PRO THR ARG VAL HIS TRP GLY ARG
SEQRES 20 B 298 HIS ASP PRO ILE LEU LYS SER GLU TRP SER ALA PHE VAL
SEQRES 21 B 298 PRO GLU HIS PHE ASP ASP ALA ARG ILE SER PHE CYS GLU
SEQRES 22 B 298 SER ALA GLY HIS PHE VAL HIS VAL GLU ALA PRO ASP GLU
SEQRES 23 B 298 ALA ALA ASP VAL LEU ALA GLU PHE PHE GLY GLY ARG
SEQRES 1 C 298 MET SER SER ASP PHE ALA THR PRO PRO GLY LEU ARG HIS
SEQRES 2 C 298 ARG GLN ILE ALA VAL ARG ASP THR THR LEU HIS VAL ALA
SEQRES 3 C 298 GLU ILE GLY SER GLY GLY THR PRO VAL LEU LEU LEU HIS
SEQRES 4 C 298 GLY TRP PRO GLU PHE TRP ALA THR TRP LEU PRO LEU MET
SEQRES 5 C 298 ASN ARG LEU HIS ASP GLN PHE HIS LEU ILE ALA PRO ASP
SEQRES 6 C 298 LEU ARG GLY PHE GLY ASP SER GLU LYS SER ALA VAL PRO
SEQRES 7 C 298 ARG SER ASP VAL GLY ALA ASN SER HIS ALA ASP ASP MET
SEQRES 8 C 298 ALA ALA LEU LEU GLY ALA LEU GLY LEU GLU SER VAL GLY
SEQRES 9 C 298 VAL VAL GLY HIS ASP VAL GLY ALA TYR ALA ALA GLN ALA
SEQRES 10 C 298 LEU ALA ARG ARG HIS PRO GLN LEU VAL ASP ARG LEU LEU
SEQRES 11 C 298 PHE PHE ASN CYS PRO THR ALA SER VAL GLY GLY ALA TRP
SEQRES 12 C 298 VAL HIS HIS GLY HIS VAL ASN GLU VAL TRP TYR GLN SER
SEQRES 13 C 298 PHE GLN GLN LEU GLY LEU ALA GLU ALA LEU VAL GLY THR
SEQRES 14 C 298 SER ARG GLU THR CYS ALA LEU TYR PHE ARG HIS PHE LEU
SEQRES 15 C 298 GLU HIS TRP SER HIS ARG LYS ASP ALA PHE GLU PRO ALA
SEQRES 16 C 298 PHE GLU LEU TRP ILE ASP ASN PHE MET LYS PRO GLY ASN
SEQRES 17 C 298 LEU ARG GLY GLY PHE ASP TRP TYR ARG SER GLN ASN ALA
SEQRES 18 C 298 LEU ARG LEU ALA ALA ILE ASP GLY HIS PRO THR PRO SER
SEQRES 19 C 298 VAL ARG ILE HIS GLN PRO THR ARG VAL HIS TRP GLY ARG
SEQRES 20 C 298 HIS ASP PRO ILE LEU LYS SER GLU TRP SER ALA PHE VAL
SEQRES 21 C 298 PRO GLU HIS PHE ASP ASP ALA ARG ILE SER PHE CYS GLU
SEQRES 22 C 298 SER ALA GLY HIS PHE VAL HIS VAL GLU ALA PRO ASP GLU
SEQRES 23 C 298 ALA ALA ASP VAL LEU ALA GLU PHE PHE GLY GLY ARG
SEQRES 1 D 298 MET SER SER ASP PHE ALA THR PRO PRO GLY LEU ARG HIS
SEQRES 2 D 298 ARG GLN ILE ALA VAL ARG ASP THR THR LEU HIS VAL ALA
SEQRES 3 D 298 GLU ILE GLY SER GLY GLY THR PRO VAL LEU LEU LEU HIS
SEQRES 4 D 298 GLY TRP PRO GLU PHE TRP ALA THR TRP LEU PRO LEU MET
SEQRES 5 D 298 ASN ARG LEU HIS ASP GLN PHE HIS LEU ILE ALA PRO ASP
SEQRES 6 D 298 LEU ARG GLY PHE GLY ASP SER GLU LYS SER ALA VAL PRO
SEQRES 7 D 298 ARG SER ASP VAL GLY ALA ASN SER HIS ALA ASP ASP MET
SEQRES 8 D 298 ALA ALA LEU LEU GLY ALA LEU GLY LEU GLU SER VAL GLY
SEQRES 9 D 298 VAL VAL GLY HIS ASP VAL GLY ALA TYR ALA ALA GLN ALA
SEQRES 10 D 298 LEU ALA ARG ARG HIS PRO GLN LEU VAL ASP ARG LEU LEU
SEQRES 11 D 298 PHE PHE ASN CYS PRO THR ALA SER VAL GLY GLY ALA TRP
SEQRES 12 D 298 VAL HIS HIS GLY HIS VAL ASN GLU VAL TRP TYR GLN SER
SEQRES 13 D 298 PHE GLN GLN LEU GLY LEU ALA GLU ALA LEU VAL GLY THR
SEQRES 14 D 298 SER ARG GLU THR CYS ALA LEU TYR PHE ARG HIS PHE LEU
SEQRES 15 D 298 GLU HIS TRP SER HIS ARG LYS ASP ALA PHE GLU PRO ALA
SEQRES 16 D 298 PHE GLU LEU TRP ILE ASP ASN PHE MET LYS PRO GLY ASN
SEQRES 17 D 298 LEU ARG GLY GLY PHE ASP TRP TYR ARG SER GLN ASN ALA
SEQRES 18 D 298 LEU ARG LEU ALA ALA ILE ASP GLY HIS PRO THR PRO SER
SEQRES 19 D 298 VAL ARG ILE HIS GLN PRO THR ARG VAL HIS TRP GLY ARG
SEQRES 20 D 298 HIS ASP PRO ILE LEU LYS SER GLU TRP SER ALA PHE VAL
SEQRES 21 D 298 PRO GLU HIS PHE ASP ASP ALA ARG ILE SER PHE CYS GLU
SEQRES 22 D 298 SER ALA GLY HIS PHE VAL HIS VAL GLU ALA PRO ASP GLU
SEQRES 23 D 298 ALA ALA ASP VAL LEU ALA GLU PHE PHE GLY GLY ARG
FORMUL 5 HOH *644(H2 O)
HELIX 1 AA1 PHE A 44 THR A 47 5 4
HELIX 2 AA2 TRP A 48 HIS A 56 1 9
HELIX 3 AA3 GLY A 83 LEU A 98 1 16
HELIX 4 AA4 ASP A 109 HIS A 122 1 14
HELIX 5 AA5 VAL A 139 VAL A 144 5 6
HELIX 6 AA6 GLY A 147 GLU A 151 5 5
HELIX 7 AA7 VAL A 152 GLN A 158 1 7
HELIX 8 AA8 LEU A 160 GLY A 168 1 9
HELIX 9 AA9 SER A 170 TRP A 185 1 16
HELIX 10 AB1 PHE A 192 PRO A 194 5 3
HELIX 11 AB2 ALA A 195 LYS A 205 1 11
HELIX 12 AB3 GLY A 207 ASP A 228 1 22
HELIX 13 AB4 LYS A 253 VAL A 260 5 8
HELIX 14 AB5 PHE A 278 ALA A 283 1 6
HELIX 15 AB6 ALA A 283 PHE A 295 1 13
HELIX 16 AB7 PHE B 44 THR B 47 5 4
HELIX 17 AB8 TRP B 48 HIS B 56 1 9
HELIX 18 AB9 GLY B 83 LEU B 98 1 16
HELIX 19 AC1 ASP B 109 HIS B 122 1 14
HELIX 20 AC2 THR B 136 VAL B 144 5 9
HELIX 21 AC3 GLY B 147 GLU B 151 5 5
HELIX 22 AC4 VAL B 152 GLN B 158 1 7
HELIX 23 AC5 LEU B 160 GLY B 168 1 9
HELIX 24 AC6 SER B 170 TRP B 185 1 16
HELIX 25 AC7 PHE B 192 PRO B 194 5 3
HELIX 26 AC8 ALA B 195 LYS B 205 1 11
HELIX 27 AC9 GLY B 207 ASP B 228 1 22
HELIX 28 AD1 LYS B 253 ALA B 258 5 6
HELIX 29 AD2 PHE B 259 PHE B 264 1 6
HELIX 30 AD3 PHE B 278 ALA B 283 1 6
HELIX 31 AD4 ALA B 283 GLY B 296 1 14
HELIX 32 AD5 PHE C 44 THR C 47 5 4
HELIX 33 AD6 TRP C 48 HIS C 56 1 9
HELIX 34 AD7 GLY C 83 LEU C 98 1 16
HELIX 35 AD8 ASP C 109 HIS C 122 1 14
HELIX 36 AD9 VAL C 139 VAL C 144 5 6
HELIX 37 AE1 GLY C 147 GLU C 151 5 5
HELIX 38 AE2 VAL C 152 GLN C 158 1 7
HELIX 39 AE3 LEU C 160 GLY C 168 1 9
HELIX 40 AE4 SER C 170 TRP C 185 1 16
HELIX 41 AE5 PHE C 192 PRO C 194 5 3
HELIX 42 AE6 ALA C 195 LYS C 205 1 11
HELIX 43 AE7 GLY C 207 ASP C 228 1 22
HELIX 44 AE8 LYS C 253 HIS C 263 5 11
HELIX 45 AE9 PHE C 278 ALA C 283 1 6
HELIX 46 AF1 ALA C 283 GLY C 296 1 14
HELIX 47 AF2 PHE D 44 THR D 47 5 4
HELIX 48 AF3 TRP D 48 HIS D 56 1 9
HELIX 49 AF4 GLY D 83 LEU D 98 1 16
HELIX 50 AF5 ASP D 109 HIS D 122 1 14
HELIX 51 AF6 THR D 136 VAL D 144 5 9
HELIX 52 AF7 HIS D 148 GLN D 158 1 11
HELIX 53 AF8 LEU D 160 GLY D 168 1 9
HELIX 54 AF9 SER D 170 TRP D 185 1 16
HELIX 55 AG1 PHE D 192 PRO D 194 5 3
HELIX 56 AG2 ALA D 195 LYS D 205 1 11
HELIX 57 AG3 GLY D 207 ASP D 228 1 22
HELIX 58 AG4 LYS D 253 ALA D 258 5 6
HELIX 59 AG5 PHE D 259 PHE D 264 1 6
HELIX 60 AG6 PHE D 278 ALA D 283 1 6
HELIX 61 AG7 ALA D 283 GLY D 296 1 14
SHEET 1 AA1 8 ARG A 12 VAL A 18 0
SHEET 2 AA1 8 THR A 21 ILE A 28 -1 O LEU A 23 N ILE A 16
SHEET 3 AA1 8 LEU A 61 PRO A 64 -1 O ALA A 63 N ALA A 26
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N LEU A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 103 GLY A 107 1 O VAL A 106 N LEU A 38
SHEET 6 AA1 8 VAL A 126 PHE A 131 1 O LEU A 130 N VAL A 105
SHEET 7 AA1 8 THR A 241 GLY A 246 1 O HIS A 244 N PHE A 131
SHEET 8 AA1 8 ALA A 267 CYS A 272 1 O ARG A 268 N VAL A 243
SHEET 1 AA216 LEU B 11 VAL B 18 0
SHEET 2 AA216 THR B 21 ILE B 28 -1 O LEU B 23 N ILE B 16
SHEET 3 AA216 HIS B 60 PRO B 64 -1 O ALA B 63 N ALA B 26
SHEET 4 AA216 PRO B 34 LEU B 38 1 N VAL B 35 O HIS B 60
SHEET 5 AA216 VAL B 103 GLY B 107 1 O VAL B 106 N LEU B 36
SHEET 6 AA216 VAL B 126 PHE B 131 1 O LEU B 130 N VAL B 105
SHEET 7 AA216 THR B 241 GLY B 246 1 O HIS B 244 N PHE B 131
SHEET 8 AA216 ALA B 267 CYS B 272 1 O SER B 270 N VAL B 243
SHEET 9 AA216 ASP D 266 CYS D 272 -1 O ILE D 269 N ALA B 267
SHEET 10 AA216 THR D 241 GLY D 246 1 N TRP D 245 O CYS D 272
SHEET 11 AA216 VAL D 126 PHE D 131 1 N PHE D 131 O HIS D 244
SHEET 12 AA216 VAL D 103 GLY D 107 1 N VAL D 105 O LEU D 130
SHEET 13 AA216 THR D 33 LEU D 38 1 N LEU D 36 O VAL D 106
SHEET 14 AA216 PHE D 59 PRO D 64 1 O ILE D 62 N LEU D 37
SHEET 15 AA216 THR D 21 ILE D 28 -1 N ALA D 26 O ALA D 63
SHEET 16 AA216 ARG D 12 VAL D 18 -1 N ILE D 16 O LEU D 23
SHEET 1 AA3 8 ARG C 12 VAL C 18 0
SHEET 2 AA3 8 THR C 21 ILE C 28 -1 O LEU C 23 N ILE C 16
SHEET 3 AA3 8 PHE C 59 PRO C 64 -1 O ALA C 63 N ALA C 26
SHEET 4 AA3 8 THR C 33 LEU C 38 1 N LEU C 37 O ILE C 62
SHEET 5 AA3 8 VAL C 103 GLY C 107 1 O GLY C 104 N LEU C 36
SHEET 6 AA3 8 VAL C 126 PHE C 131 1 O LEU C 130 N VAL C 105
SHEET 7 AA3 8 THR C 241 GLY C 246 1 O HIS C 244 N PHE C 131
SHEET 8 AA3 8 ALA C 267 CYS C 272 1 O SER C 270 N VAL C 243
CISPEP 1 TRP A 41 PRO A 42 0 -0.53
CISPEP 2 TRP B 41 PRO B 42 0 4.12
CISPEP 3 TRP C 41 PRO C 42 0 5.46
CISPEP 4 TRP D 41 PRO D 42 0 -0.12
CRYST1 87.537 84.913 98.235 90.00 100.91 90.00 P 1 21 1 8
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 0.011424 0.000000 0.002202 0.00000
SCALE2 0.000000 0.011777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010367 0.00000
TER 2333 GLY A 296
TER 4660 GLY B 296
TER 6993 GLY C 296
TER 9326 GLY D 296
MASTER 294 0 0 61 32 0 0 6 9966 4 0 92
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