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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 01-MAY-07 2YYS
TITLE CRYSTAL STRUCTURE OF THE PROLINE IMINOPEPTIDASE-RELATED
TITLE 2 PROTEIN TTHA1809 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE-RELATED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS TTHA1809, CRYSTAL STRUCTURE, PROLINE IMINOPEPTIDASE-RELATED
KEYWDS 2 PROTEIN, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.OKAI,Y.MIYAUCHI,A.EBIHARA,W.C.LEE,K.NAGATA,M.TANOKURA
REVDAT 1 26-FEB-08 2YYS 0
JRNL AUTH M.OKAI,Y.MIYAUCHI,A.EBIHARA,W.C.LEE,K.NAGATA,
JRNL AUTH 2 M.TANOKURA
JRNL TITL CRYSTAL STRUCTURE OF THE PROLINE
JRNL TITL 2 IMINOPEPTIDASE-RELATED PROTEIN TTHA1809 FROM
JRNL TITL 3 THERMUS THERMOPHILUS HB8
JRNL REF PROTEINS V. 70 1646 2008
JRNL REFN ASTM PSFGEY US ISSN 0887-3585
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 51211
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2740
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3686
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE SET COUNT : 223
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4856
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99000
REMARK 3 B22 (A**2) : 0.99000
REMARK 3 B33 (A**2) : -1.48000
REMARK 3 B12 (A**2) : 0.49000
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): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.665
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4562 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4277 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6213 ; 1.229 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9865 ; 0.753 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 562 ; 5.734 ; 5.000
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): 666 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5126 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 981 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 876 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4623 ; 0.247 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2424 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 316 ; 0.173 ; 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): 10 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.306 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.109 ; 0.200
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): 2812 ; 0.686 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4479 ; 1.325 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1750 ; 1.760 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1734 ; 3.154 ; 4.500
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 : 0
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2YYS COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB027304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51211
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES-NA, 0.85M POTASSIUM
REMARK 280 SODIUM TARTRATE TETRAHYDRATE, PH 7.2, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,1/3-Z
REMARK 290 6555 -X,-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.19667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.09833
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 38.09833
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 76.19667
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: MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 VAL A 285
REMARK 465 ASP A 286
REMARK 465 ARG B 281
REMARK 465 GLY B 282
REMARK 465 PRO B 283
REMARK 465 LEU B 284
REMARK 465 VAL B 285
REMARK 465 ASP B 286
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 LEU A 284 O
REMARK 470 MET B 1 CG SD CE
REMARK 470 LEU B 280 O
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 SER A 232 -41.44 -136.40
REMARK 500 VAL B 129 -41.83 -131.34
REMARK 500 SER B 232 -36.42 -140.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 502
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE B 1500
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE B 1501
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE B 1502
DBREF 2YYS A 1 286 UNP Q5SHC1 Q5SHC1_THET8 1 286
DBREF 2YYS B 1 286 UNP Q5SHC1 Q5SHC1_THET8 1 286
SEQRES 1 A 286 MET ARG GLU GLU ILE GLY TYR VAL PRO VAL GLY GLU ALA
SEQRES 2 A 286 GLU LEU TYR VAL GLU ASP VAL GLY PRO VAL GLU GLY PRO
SEQRES 3 A 286 ALA LEU PHE VAL LEU HIS GLY GLY PRO GLY GLY ASN ALA
SEQRES 4 A 286 TYR VAL LEU ARG GLU GLY LEU GLN ASP TYR LEU GLU GLY
SEQRES 5 A 286 PHE ARG VAL VAL TYR PHE ASP GLN ARG GLY SER GLY ARG
SEQRES 6 A 286 SER LEU GLU LEU PRO GLN ASP PRO ARG LEU PHE THR VAL
SEQRES 7 A 286 ASP ALA LEU VAL GLU ASP THR LEU LEU LEU ALA GLU ALA
SEQRES 8 A 286 LEU GLY VAL GLU ARG PHE GLY LEU LEU ALA HIS GLY PHE
SEQRES 9 A 286 GLY ALA VAL VAL ALA LEU GLU VAL LEU ARG ARG PHE PRO
SEQRES 10 A 286 GLN ALA GLU GLY ALA ILE LEU LEU ALA PRO TRP VAL ASN
SEQRES 11 A 286 PHE PRO TRP LEU ALA ALA ARG LEU ALA GLU ALA ALA GLY
SEQRES 12 A 286 LEU ALA PRO LEU PRO ASP PRO GLU GLU ASN LEU LYS GLU
SEQRES 13 A 286 ALA LEU LYS ARG GLU GLU PRO LYS ALA LEU PHE ASP ARG
SEQRES 14 A 286 LEU MET PHE PRO THR PRO ARG GLY ARG MET ALA TYR GLU
SEQRES 15 A 286 TRP LEU ALA GLU GLY ALA GLY ILE LEU GLY SER ASP ALA
SEQRES 16 A 286 PRO GLY LEU ALA PHE LEU ARG ASN GLY LEU TRP ARG LEU
SEQRES 17 A 286 ASP TYR THR PRO TYR LEU THR PRO GLU ARG ARG PRO LEU
SEQRES 18 A 286 TYR VAL LEU VAL GLY GLU ARG ASP GLY THR SER TYR PRO
SEQRES 19 A 286 TYR ALA GLU GLU VAL ALA SER ARG LEU ARG ALA PRO ILE
SEQRES 20 A 286 ARG VAL LEU PRO GLU ALA GLY HIS TYR LEU TRP ILE ASP
SEQRES 21 A 286 ALA PRO GLU ALA PHE GLU GLU ALA PHE LYS GLU ALA LEU
SEQRES 22 A 286 ALA ALA LEU VAL PRO ALA LEU ARG GLY PRO LEU VAL ASP
SEQRES 1 B 286 MET ARG GLU GLU ILE GLY TYR VAL PRO VAL GLY GLU ALA
SEQRES 2 B 286 GLU LEU TYR VAL GLU ASP VAL GLY PRO VAL GLU GLY PRO
SEQRES 3 B 286 ALA LEU PHE VAL LEU HIS GLY GLY PRO GLY GLY ASN ALA
SEQRES 4 B 286 TYR VAL LEU ARG GLU GLY LEU GLN ASP TYR LEU GLU GLY
SEQRES 5 B 286 PHE ARG VAL VAL TYR PHE ASP GLN ARG GLY SER GLY ARG
SEQRES 6 B 286 SER LEU GLU LEU PRO GLN ASP PRO ARG LEU PHE THR VAL
SEQRES 7 B 286 ASP ALA LEU VAL GLU ASP THR LEU LEU LEU ALA GLU ALA
SEQRES 8 B 286 LEU GLY VAL GLU ARG PHE GLY LEU LEU ALA HIS GLY PHE
SEQRES 9 B 286 GLY ALA VAL VAL ALA LEU GLU VAL LEU ARG ARG PHE PRO
SEQRES 10 B 286 GLN ALA GLU GLY ALA ILE LEU LEU ALA PRO TRP VAL ASN
SEQRES 11 B 286 PHE PRO TRP LEU ALA ALA ARG LEU ALA GLU ALA ALA GLY
SEQRES 12 B 286 LEU ALA PRO LEU PRO ASP PRO GLU GLU ASN LEU LYS GLU
SEQRES 13 B 286 ALA LEU LYS ARG GLU GLU PRO LYS ALA LEU PHE ASP ARG
SEQRES 14 B 286 LEU MET PHE PRO THR PRO ARG GLY ARG MET ALA TYR GLU
SEQRES 15 B 286 TRP LEU ALA GLU GLY ALA GLY ILE LEU GLY SER ASP ALA
SEQRES 16 B 286 PRO GLY LEU ALA PHE LEU ARG ASN GLY LEU TRP ARG LEU
SEQRES 17 B 286 ASP TYR THR PRO TYR LEU THR PRO GLU ARG ARG PRO LEU
SEQRES 18 B 286 TYR VAL LEU VAL GLY GLU ARG ASP GLY THR SER TYR PRO
SEQRES 19 B 286 TYR ALA GLU GLU VAL ALA SER ARG LEU ARG ALA PRO ILE
SEQRES 20 B 286 ARG VAL LEU PRO GLU ALA GLY HIS TYR LEU TRP ILE ASP
SEQRES 21 B 286 ALA PRO GLU ALA PHE GLU GLU ALA PHE LYS GLU ALA LEU
SEQRES 22 B 286 ALA ALA LEU VAL PRO ALA LEU ARG GLY PRO LEU VAL ASP
HET GOL A 500 6
HET GOL A 501 6
HET GOL A 502 6
HET GOL B1500 6
HET GOL B1501 6
HET GOL B1502 6
HETNAM GOL GLYCEROL
FORMUL 3 GOL 6(C3 H8 O3)
FORMUL 9 HOH *413(H2 O)
HELIX 1 1 ALA A 39 GLN A 47 1 9
HELIX 2 2 ASP A 48 LEU A 50 5 3
HELIX 3 3 ASP A 72 PHE A 76 5 5
HELIX 4 4 THR A 77 LEU A 92 1 16
HELIX 5 5 PHE A 104 PHE A 116 1 13
HELIX 6 6 ASN A 130 ALA A 142 1 13
HELIX 7 7 ASP A 149 GLU A 161 1 13
HELIX 8 8 GLU A 162 PHE A 172 1 11
HELIX 9 9 THR A 174 ALA A 188 1 15
HELIX 10 10 ASP A 194 ASN A 203 1 10
HELIX 11 11 GLY A 204 LEU A 208 5 5
HELIX 12 12 TYR A 210 LEU A 214 5 5
HELIX 13 13 TYR A 235 ARG A 244 1 10
HELIX 14 14 TYR A 256 ALA A 261 1 6
HELIX 15 15 ALA A 261 ALA A 275 1 15
HELIX 16 16 VAL A 277 GLY A 282 1 6
HELIX 17 17 ALA B 39 GLN B 47 1 9
HELIX 18 18 ASP B 48 LEU B 50 5 3
HELIX 19 19 THR B 77 LEU B 92 1 16
HELIX 20 20 PHE B 104 PHE B 116 1 13
HELIX 21 21 ASN B 130 ALA B 142 1 13
HELIX 22 22 ASP B 149 GLU B 161 1 13
HELIX 23 23 GLU B 162 PHE B 172 1 11
HELIX 24 24 THR B 174 ALA B 188 1 15
HELIX 25 25 ASP B 194 ASN B 203 1 10
HELIX 26 26 GLY B 204 LEU B 208 5 5
HELIX 27 27 TYR B 210 LEU B 214 5 5
HELIX 28 28 PRO B 234 ARG B 244 1 11
HELIX 29 29 TYR B 256 ALA B 261 1 6
HELIX 30 30 ALA B 261 VAL B 277 1 17
SHEET 1 A 8 GLU A 3 PRO A 9 0
SHEET 2 A 8 GLU A 14 VAL A 20 -1 O ASP A 19 N GLU A 4
SHEET 3 A 8 ARG A 54 PHE A 58 -1 O TYR A 57 N GLU A 18
SHEET 4 A 8 ALA A 27 LEU A 31 1 N LEU A 28 O VAL A 56
SHEET 5 A 8 PHE A 97 HIS A 102 1 O LEU A 100 N LEU A 31
SHEET 6 A 8 ALA A 119 LEU A 125 1 O LEU A 125 N ALA A 101
SHEET 7 A 8 LEU A 221 GLY A 226 1 O TYR A 222 N LEU A 124
SHEET 8 A 8 ILE A 247 LEU A 250 1 O LEU A 250 N VAL A 225
SHEET 1 B 8 GLU B 3 VAL B 10 0
SHEET 2 B 8 ALA B 13 VAL B 20 -1 O ALA B 13 N VAL B 10
SHEET 3 B 8 ARG B 54 PHE B 58 -1 O TYR B 57 N GLU B 18
SHEET 4 B 8 ALA B 27 LEU B 31 1 N LEU B 28 O VAL B 56
SHEET 5 B 8 PHE B 97 HIS B 102 1 O LEU B 100 N LEU B 31
SHEET 6 B 8 ALA B 119 LEU B 125 1 O LEU B 125 N ALA B 101
SHEET 7 B 8 LEU B 221 GLY B 226 1 O TYR B 222 N LEU B 124
SHEET 8 B 8 ILE B 247 LEU B 250 1 O ARG B 248 N VAL B 225
CISPEP 1 GLY A 34 PRO A 35 0 2.37
CISPEP 2 TYR A 233 PRO A 234 0 5.39
CISPEP 3 GLY B 34 PRO B 35 0 2.26
CISPEP 4 TYR B 233 PRO B 234 0 1.46
SITE 1 AC1 5 GLY A 34 TRP A 128 HOH A 604 HOH A 747
SITE 2 AC1 5 HOH A 750
SITE 1 AC2 5 PRO A 26 ALA A 27 GLY A 98 GLU A 120
SITE 2 AC2 5 HOH A 645
SITE 1 AC3 6 GLU A 4 ILE A 5 GLY A 6 HOH A 546
SITE 2 AC3 6 HOH A 655 HOH A 660
SITE 1 AC4 5 GLY B 34 TRP B 128 HOH B1556 HOH B1638
SITE 2 AC4 5 HOH B1640
SITE 1 AC5 9 ARG A 137 GLU A 140 GLU B 44 ALA B 180
SITE 2 AC5 9 ILE B 259 HOH B1528 HOH B1530 HOH B1534
SITE 3 AC5 9 HOH B1576
SITE 1 AC6 6 ALA A 145 HOH A 692 TYR B 40 ARG B 43
SITE 2 AC6 6 GLN B 47 HOH B1584
CRYST1 126.930 126.930 114.295 90.00 90.00 120.00 P 32 2 1 12
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 0.007878 0.004549 0.000000 0.00000
SCALE2 0.000000 0.009097 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008749 0.00000
TER 2221 LEU A 284
TER 4409 LEU B 280
MASTER 300 0 6 30 16 0 13 6 4856 2 36 44
END |