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HEADER HYDROLASE 03-JUN-03 1UFO
TITLE CRYSTAL STRUCTURE OF TT1662 FROM THERMUS THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TT1662;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS ALPHA-BETA FOLD, HYDROLASE, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MURAYAMA,M.SHIROUZU,T.TERADA,S.KURAMITSU,S.YOKOYAMA
REVDAT 1 03-DEC-03 1UFO 0
JRNL AUTH K.MURAYAMA,M.SHIROUZU,T.TERADA,S.KURAMITSU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTUR OF TT1662 FROM THERMUS
JRNL TITL 2 THERMOPHILUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2514544.480
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 174137
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 SET) : 0.170
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 17296
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 26064
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2853
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.005
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1835
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.60000
REMARK 3 B22 (A**2) : 1.60000
REMARK 3 B33 (A**2) : -3.21000
REMARK 3 B12 (A**2) : 1.13000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.07
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.024
REMARK 3 BOND ANGLES (DEGREES) : 2.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.49
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.550 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.47
REMARK 3 BSOL : 82.05
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UFO COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-2003.
REMARK 100 THE RCSB ID CODE IS RCSB005775.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174213
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32100
REMARK 200 FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG3350, 0.2M KF, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,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 23.37300
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 46.74600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 174 CB PRO A 174 CG 0.158
REMARK 500 PRO E 174 CB PRO E 174 CG 0.172
REMARK 500 PRO F 200 CB PRO F 200 CG -0.142
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL F 3 N - CA - C ANGL. DEV. = 12.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 113 -116.16 59.82
REMARK 500 SER B 113 -116.97 54.51
REMARK 500 SER D 113 -113.07 53.74
REMARK 500 SER E 113 -115.78 56.09
REMARK 500 SER F 113 -114.49 53.67
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1287 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH 1819 DISTANCE = 5.94 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN
REMARK 999 DOES NOT CURRENTLY EXIST.
SEQRES 1 A 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 A 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 A 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 A 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 A 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 A 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 A 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 A 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 A 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 A 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 A 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 A 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 A 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 A 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 A 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 A 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 A 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 A 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 A 238 LEU GLU ALA ARG
SEQRES 1 B 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 B 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 B 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 B 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 B 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 B 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 B 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 B 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 B 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 B 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 B 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 B 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 B 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 B 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 B 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 B 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 B 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 B 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 B 238 LEU GLU ALA ARG
SEQRES 1 C 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 C 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 C 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 C 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 C 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 C 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 C 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 C 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 C 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 C 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 C 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 C 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 C 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 C 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 C 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 C 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 C 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 C 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 C 238 LEU GLU ALA ARG
SEQRES 1 D 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 D 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 D 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 D 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 D 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 D 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 D 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 D 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 D 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 D 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 D 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 D 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 D 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 D 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 D 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 D 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 D 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 D 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 D 238 LEU GLU ALA ARG
SEQRES 1 E 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 E 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 E 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 E 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 E 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 E 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 E 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 E 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 E 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 E 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 E 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 E 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 E 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 E 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 E 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 E 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 E 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 E 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 E 238 LEU GLU ALA ARG
SEQRES 1 F 238 MSE ARG VAL ARG THR GLU ARG LEU THR LEU ALA GLY LEU
SEQRES 2 F 238 SER VAL LEU ALA ARG ILE PRO GLU ALA PRO LYS ALA LEU
SEQRES 3 F 238 LEU LEU ALA LEU HIS GLY LEU GLN GLY SER LYS GLU HIS
SEQRES 4 F 238 ILE LEU ALA LEU LEU PRO GLY TYR ALA GLU ARG GLY PHE
SEQRES 5 F 238 LEU LEU LEU ALA PHE ASP ALA PRO ARG HIS GLY GLU ARG
SEQRES 6 F 238 GLU GLY PRO PRO PRO SER SER LYS SER PRO ARG TYR VAL
SEQRES 7 F 238 GLU GLU VAL TYR ARG VAL ALA LEU GLY PHE LYS GLU GLU
SEQRES 8 F 238 ALA ARG ARG VAL ALA GLU GLU ALA GLU ARG ARG PHE GLY
SEQRES 9 F 238 LEU PRO LEU PHE LEU ALA GLY GLY SER LEU GLY ALA PHE
SEQRES 10 F 238 VAL ALA HIS LEU LEU LEU ALA GLU GLY PHE ARG PRO ARG
SEQRES 11 F 238 GLY VAL LEU ALA PHE ILE GLY SER GLY PHE PRO MSE LYS
SEQRES 12 F 238 LEU PRO GLN GLY GLN VAL VAL GLU ASP PRO GLY VAL LEU
SEQRES 13 F 238 ALA LEU TYR GLN ALA PRO PRO ALA THR ARG GLY GLU ALA
SEQRES 14 F 238 TYR GLY GLY VAL PRO LEU LEU HIS LEU HIS GLY SER ARG
SEQRES 15 F 238 ASP HIS ILE VAL PRO LEU ALA ARG MSE GLU LYS THR LEU
SEQRES 16 F 238 GLU ALA LEU ARG PRO HIS TYR PRO GLU GLY ARG LEU ALA
SEQRES 17 F 238 ARG PHE VAL GLU GLU GLY ALA GLY HIS THR LEU THR PRO
SEQRES 18 F 238 LEU MSE ALA ARG VAL GLY LEU ALA PHE LEU GLU HIS TRP
SEQRES 19 F 238 LEU GLU ALA ARG
MODRES 1UFO MSE A 1 MET SELENOMETHIONINE
MODRES 1UFO MSE A 142 MET SELENOMETHIONINE
MODRES 1UFO MSE A 191 MET SELENOMETHIONINE
MODRES 1UFO MSE A 223 MET SELENOMETHIONINE
MODRES 1UFO MSE B 1 MET SELENOMETHIONINE
MODRES 1UFO MSE B 142 MET SELENOMETHIONINE
MODRES 1UFO MSE B 191 MET SELENOMETHIONINE
MODRES 1UFO MSE B 223 MET SELENOMETHIONINE
MODRES 1UFO MSE C 1 MET SELENOMETHIONINE
MODRES 1UFO MSE C 142 MET SELENOMETHIONINE
MODRES 1UFO MSE C 191 MET SELENOMETHIONINE
MODRES 1UFO MSE C 223 MET SELENOMETHIONINE
MODRES 1UFO MSE D 1 MET SELENOMETHIONINE
MODRES 1UFO MSE D 142 MET SELENOMETHIONINE
MODRES 1UFO MSE D 191 MET SELENOMETHIONINE
MODRES 1UFO MSE D 223 MET SELENOMETHIONINE
MODRES 1UFO MSE E 1 MET SELENOMETHIONINE
MODRES 1UFO MSE E 142 MET SELENOMETHIONINE
MODRES 1UFO MSE E 191 MET SELENOMETHIONINE
MODRES 1UFO MSE E 223 MET SELENOMETHIONINE
MODRES 1UFO MSE F 1 MET SELENOMETHIONINE
MODRES 1UFO MSE F 142 MET SELENOMETHIONINE
MODRES 1UFO MSE F 191 MET SELENOMETHIONINE
MODRES 1UFO MSE F 223 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 142 8
HET MSE A 191 8
HET MSE A 223 8
HET MSE B 1 8
HET MSE B 142 8
HET MSE B 191 8
HET MSE B 223 8
HET MSE C 1 8
HET MSE C 142 8
HET MSE C 191 8
HET MSE C 223 8
HET MSE D 1 8
HET MSE D 142 8
HET MSE D 191 8
HET MSE D 223 8
HET MSE E 1 8
HET MSE E 142 8
HET MSE E 191 8
HET MSE E 223 8
HET MSE F 1 8
HET MSE F 142 8
HET MSE F 191 8
HET MSE F 223 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 24(C5 H11 N1 O2 SE1)
FORMUL 7 HOH *1835(H2 O1)
HELIX 1 1 SER A 36 LEU A 43 1 8
HELIX 2 2 TYR A 47 ARG A 50 5 4
HELIX 3 3 ARG A 76 GLY A 104 1 29
HELIX 4 4 SER A 113 GLU A 125 1 13
HELIX 5 5 ASP A 152 ALA A 161 1 10
HELIX 6 6 PRO A 162 GLY A 171 5 10
HELIX 7 7 PRO A 187 ARG A 199 1 13
HELIX 8 8 PRO A 200 TYR A 202 5 3
HELIX 9 9 THR A 220 ALA A 237 1 18
HELIX 10 10 SER B 36 LEU B 43 1 8
HELIX 11 11 TYR B 47 ARG B 50 5 4
HELIX 12 12 ARG B 76 GLY B 104 1 29
HELIX 13 13 SER B 113 GLU B 125 1 13
HELIX 14 14 ASP B 152 ALA B 161 1 10
HELIX 15 15 PRO B 162 TYR B 170 5 9
HELIX 16 16 PRO B 187 ARG B 199 1 13
HELIX 17 17 PRO B 200 TYR B 202 5 3
HELIX 18 18 THR B 220 GLU B 236 1 17
HELIX 19 19 SER C 36 LEU C 43 1 8
HELIX 20 20 TYR C 47 ARG C 50 5 4
HELIX 21 21 ARG C 76 GLY C 104 1 29
HELIX 22 22 SER C 113 GLU C 125 1 13
HELIX 23 23 ASP C 152 ALA C 161 1 10
HELIX 24 24 PRO C 162 GLY C 171 5 10
HELIX 25 25 PRO C 187 ARG C 199 1 13
HELIX 26 26 PRO C 200 TYR C 202 5 3
HELIX 27 27 THR C 220 ALA C 237 1 18
HELIX 28 28 SER D 36 LEU D 43 1 8
HELIX 29 29 TYR D 47 ARG D 50 5 4
HELIX 30 30 ARG D 76 GLY D 104 1 29
HELIX 31 31 SER D 113 GLU D 125 1 13
HELIX 32 32 ASP D 152 ALA D 161 1 10
HELIX 33 33 PRO D 162 GLY D 171 5 10
HELIX 34 34 PRO D 187 ARG D 199 1 13
HELIX 35 35 PRO D 200 TYR D 202 5 3
HELIX 36 36 THR D 220 ALA D 237 1 18
HELIX 37 37 SER E 36 LEU E 43 1 8
HELIX 38 38 TYR E 47 ARG E 50 5 4
HELIX 39 39 ARG E 76 GLY E 104 1 29
HELIX 40 40 SER E 113 GLU E 125 1 13
HELIX 41 41 ASP E 152 ALA E 161 1 10
HELIX 42 42 PRO E 162 GLY E 171 5 10
HELIX 43 43 PRO E 187 ARG E 199 1 13
HELIX 44 44 PRO E 200 TYR E 202 5 3
HELIX 45 45 THR E 220 ALA E 237 1 18
HELIX 46 46 SER F 36 LEU F 43 1 8
HELIX 47 47 TYR F 47 ARG F 50 5 4
HELIX 48 48 ARG F 76 GLY F 104 1 29
HELIX 49 49 SER F 113 GLU F 125 1 13
HELIX 50 50 ASP F 152 ALA F 161 1 10
HELIX 51 51 PRO F 162 GLY F 171 5 10
HELIX 52 52 PRO F 187 ARG F 199 1 13
HELIX 53 53 PRO F 200 TYR F 202 5 3
HELIX 54 54 THR F 220 ALA F 237 1 18
SHEET 1 A16 VAL A 3 LEU A 10 0
SHEET 2 A16 LEU A 13 PRO A 20 -1 O ALA A 17 N GLU A 6
SHEET 3 A16 PHE A 52 ALA A 56 -1 O ALA A 56 N LEU A 16
SHEET 4 A16 ALA A 25 LEU A 30 1 N ALA A 29 O LEU A 55
SHEET 5 A16 LEU A 107 GLY A 112 1 O GLY A 112 N LEU A 30
SHEET 6 A16 VAL A 132 PHE A 135 1 O PHE A 135 N GLY A 111
SHEET 7 A16 LEU A 175 GLY A 180 1 O LEU A 176 N ALA A 134
SHEET 8 A16 LEU A 207 GLU A 212 1 O PHE A 210 N HIS A 179
SHEET 9 A16 LEU B 207 GLU B 212 -1 O VAL B 211 N ARG A 209
SHEET 10 A16 LEU B 175 GLY B 180 1 N HIS B 179 O GLU B 212
SHEET 11 A16 VAL B 132 PHE B 135 1 N ALA B 134 O LEU B 176
SHEET 12 A16 LEU B 107 GLY B 112 1 N GLY B 111 O PHE B 135
SHEET 13 A16 ALA B 25 LEU B 30 1 N LEU B 30 O ALA B 110
SHEET 14 A16 PHE B 52 ALA B 56 1 O LEU B 55 N ALA B 29
SHEET 15 A16 LEU B 13 ILE B 19 -1 N LEU B 16 O ALA B 56
SHEET 16 A16 ARG B 4 LEU B 10 -1 N LEU B 10 O LEU B 13
SHEET 1 B16 VAL C 3 LEU C 10 0
SHEET 2 B16 LEU C 13 PRO C 20 -1 O VAL C 15 N LEU C 8
SHEET 3 B16 PHE C 52 PHE C 57 -1 O ALA C 56 N LEU C 16
SHEET 4 B16 ALA C 25 LEU C 30 1 N ALA C 25 O LEU C 53
SHEET 5 B16 LEU C 107 GLY C 112 1 O ALA C 110 N LEU C 30
SHEET 6 B16 VAL C 132 PHE C 135 1 O PHE C 135 N GLY C 111
SHEET 7 B16 LEU C 175 GLY C 180 1 O LEU C 176 N ALA C 134
SHEET 8 B16 LEU C 207 GLU C 212 1 O PHE C 210 N HIS C 179
SHEET 9 B16 LEU D 207 GLU D 213 -1 O VAL D 211 N ARG C 209
SHEET 10 B16 LEU D 175 GLY D 180 1 N HIS D 177 O PHE D 210
SHEET 11 B16 VAL D 132 PHE D 135 1 N ALA D 134 O LEU D 176
SHEET 12 B16 LEU D 107 GLY D 112 1 N GLY D 111 O PHE D 135
SHEET 13 B16 ALA D 25 LEU D 30 1 N LEU D 30 O GLY D 112
SHEET 14 B16 PHE D 52 PHE D 57 1 O LEU D 55 N ALA D 29
SHEET 15 B16 LEU D 13 ILE D 19 -1 N LEU D 16 O ALA D 56
SHEET 16 B16 ARG D 4 LEU D 10 -1 N LEU D 8 O VAL D 15
SHEET 1 C16 VAL E 3 LEU E 10 0
SHEET 2 C16 LEU E 13 PRO E 20 -1 O VAL E 15 N LEU E 8
SHEET 3 C16 PHE E 52 PHE E 57 -1 O ALA E 56 N LEU E 16
SHEET 4 C16 ALA E 25 LEU E 30 1 N ALA E 29 O LEU E 55
SHEET 5 C16 LEU E 107 GLY E 112 1 O GLY E 112 N LEU E 30
SHEET 6 C16 VAL E 132 PHE E 135 1 O PHE E 135 N GLY E 111
SHEET 7 C16 LEU E 175 GLY E 180 1 O LEU E 176 N ALA E 134
SHEET 8 C16 LEU E 207 GLU E 212 1 O GLU E 212 N HIS E 179
SHEET 9 C16 LEU F 207 GLU F 212 -1 O ARG F 209 N VAL E 211
SHEET 10 C16 LEU F 175 GLY F 180 1 N HIS F 177 O PHE F 210
SHEET 11 C16 VAL F 132 PHE F 135 1 N ALA F 134 O LEU F 176
SHEET 12 C16 LEU F 107 GLY F 112 1 N GLY F 111 O PHE F 135
SHEET 13 C16 ALA F 25 LEU F 30 1 N LEU F 30 O ALA F 110
SHEET 14 C16 PHE F 52 ALA F 56 1 O LEU F 53 N ALA F 25
SHEET 15 C16 LEU F 13 ILE F 19 -1 N LEU F 16 O ALA F 56
SHEET 16 C16 ARG F 4 LEU F 10 -1 N LEU F 8 O VAL F 15
CISPEP 1 GLY A 67 PRO A 68 0 0.49
CISPEP 2 GLY B 67 PRO B 68 0 -0.18
CISPEP 3 GLY C 67 PRO C 68 0 0.67
CISPEP 4 GLY D 67 PRO D 68 0 -0.26
CISPEP 5 GLY E 67 PRO E 68 0 0.41
CRYST1 129.857 129.857 70.119 90.00 90.00 120.00 P 31 18
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 0.007701 0.004446 0.000000 0.00000
SCALE2 0.000000 0.008892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014261 0.00000
TER 1862 ARG A 238
TER 3713 ARG B 238
TER 5580 ARG C 238
TER 7438 ARG D 238
TER 9300 ARG E 238
TER 11159 ARG F 238
MASTER 283 0 24 54 48 0 0 612988 6 192 114
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