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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 12-MAR-03 1UAN TITLE CRYSTAL STRUCTURE OF THE CONSERVED PROTEIN TT1542 FROM TITLE 2 THERMUS THERMOPHILUS HB8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TT1542; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: CONSERVED PROTEIN TT1542; COMPND 5 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_STRAIN: B834(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS ROSSMANN-LIKE, STRUCTURAL GENOMICS, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI EXPDTA X-RAY DIFFRACTION AUTHOR N.HANDA,T.TERADA,J.R.H.TAME,S.-Y.PARK,K.KINOSHITA,M.OTA, AUTHOR 2 H.NAKAMURA,S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 1 05-AUG-03 1UAN 0 JRNL AUTH N.HANDA,T.TERADA,Y.KAMEWARI,H.HAMANA,J.R.H.TAME, JRNL AUTH 2 S.-Y.PARK,K.KINOSHITA,M.OTA,H.NAKAMURA,S.KURAMITSU, JRNL AUTH 3 M.SHIROUZU,S.YOKOYAMA JRNL TITL CRYSTAL STRUCTURE OF THE CONSERVED PROTEIN TT1542 JRNL TITL 2 FROM THERMUS THERMOPHILUS HB8 JRNL REF PROTEIN SCI. V. 12 1621 2003 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.19 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 42222 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) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.201 REMARK 3 FREE R VALUE : 0.243 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2245 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3071 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2470 REMARK 3 BIN FREE R VALUE SET COUNT : 166 REMARK 3 BIN FREE R VALUE : 0.2970 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 3565 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.65 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.02000 REMARK 3 B22 (A**2) : 1.02000 REMARK 3 B33 (A**2) : -1.53000 REMARK 3 B12 (A**2) : 0.51000 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): 0.146 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.143 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.522 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3499 ; 0.022 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4744 ; 1.763 ; 1.975 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 435 ; 5.519 ; 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): 504 ; 0.148 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2742 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1551 ; 0.212 ; 0.200 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): 154 ; 0.115 ; 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): 58 ; 0.229 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.177 ; 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): 2189 ; 1.224 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3485 ; 2.254 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1310 ; 3.510 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1259 ; 5.919 ; 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: NULL REMARK 4 REMARK 4 1UAN COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB005622. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-2002 REMARK 200 TEMPERATURE (KELVIN) : 93.0 REMARK 200 PH : 7.10 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) : 0.9821, 0.9808, 0.9803, 0.9752 REMARK 200 MONOCHROMATOR : SI 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 419321 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 9.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.03400 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.22300 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE/RESOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CHLORIDE, REMARK 280 HEPES, PH 7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-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 0.00000 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 0.00000 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 0.00000 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 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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 BIOMT1 2 -0.500000 -0.866025 0.000000 107.13400 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 53.56700 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 92.78077 REMARK 350 BIOMT3 3 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 GLY A 179 REMARK 465 GLU A 180 REMARK 465 ALA A 181 REMARK 465 ALA A 182 REMARK 465 SER A 183 REMARK 465 GLU A 184 REMARK 465 THR A 185 REMARK 465 THR B 178 REMARK 465 GLY B 179 REMARK 465 GLU B 180 REMARK 465 ALA B 181 REMARK 465 ALA B 182 REMARK 465 SER B 183 REMARK 465 GLU B 184 REMARK 465 THR B 185 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 ILE A 34 CG1 ILE A 34 CD1 0.141 REMARK 500 MET A 197 CB MET A 197 CG 0.265 REMARK 500 MET A 197 SD MET A 197 CE -0.140 REMARK 500 MET B 197 CB MET B 197 CG 0.170 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 MET A 1 CB - CG - SD ANGL. DEV. = 16.3 DEGREES REMARK 500 LEU A 2 N - CA - C ANGL. DEV. =-14.7 DEGREES REMARK 500 ARG A 24 CB - CG - CD ANGL. DEV. = 14.4 DEGREES REMARK 500 LEU A 30 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU A 30 CB - CG - CD2 ANGL. DEV. = 11.6 DEGREES REMARK 500 MET A 197 CG - SD - CE ANGL. DEV. =-15.8 DEGREES REMARK 500 GLY B 187 N - CA - C ANGL. DEV. = 18.7 DEGREES REMARK 500 MET B 197 CG - SD - CE ANGL. DEV. =-18.4 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: TTK003001542.1 RELATED DB: TARGETDB DBREF 1UAN A 1 227 UNP Q84BR2 Q84BR2_THETH 1 227 DBREF 1UAN B 1 227 UNP Q84BR2 Q84BR2_THETH 1 227 SEQRES 1 A 227 MET LEU ASP LEU LEU VAL VAL ALA PRO HIS PRO ASP ASP SEQRES 2 A 227 GLY GLU LEU GLY CYS GLY GLY THR LEU ALA ARG ALA LYS SEQRES 3 A 227 ALA GLU GLY LEU SER THR GLY ILE LEU ASP LEU THR ARG SEQRES 4 A 227 GLY GLU MET GLY SER LYS GLY THR PRO GLU GLU ARG GLU SEQRES 5 A 227 LYS GLU VAL ALA GLU ALA SER ARG ILE LEU GLY LEU ASP SEQRES 6 A 227 PHE ARG GLY ASN LEU GLY PHE PRO ASP GLY GLY LEU ALA SEQRES 7 A 227 ASP VAL PRO GLU GLN ARG LEU LYS LEU ALA GLN ALA LEU SEQRES 8 A 227 ARG ARG LEU ARG PRO ARG VAL VAL PHE ALA PRO LEU GLU SEQRES 9 A 227 ALA ASP ARG HIS PRO ASP HIS THR ALA ALA SER ARG LEU SEQRES 10 A 227 ALA VAL ALA ALA VAL HIS LEU ALA GLY LEU ARG LYS ALA SEQRES 11 A 227 PRO LEU GLU GLY GLU PRO PHE ARG VAL GLU ARG LEU PHE SEQRES 12 A 227 PHE TYR PRO GLY ASN HIS PRO PHE ALA PRO SER PHE LEU SEQRES 13 A 227 VAL LYS ILE SER ALA PHE ILE ASP GLN TRP GLU ALA ALA SEQRES 14 A 227 VAL LEU ALA TYR ARG SER GLN PHE THR GLY GLU ALA ALA SEQRES 15 A 227 SER GLU THR VAL GLY PRO LYS GLY VAL GLU ALA ARG LYS SEQRES 16 A 227 ALA MET ARG ARG TYR TRP GLY ASN TYR LEU GLY VAL ASP SEQRES 17 A 227 TYR ALA GLU PRO PHE VAL SER PRO LEU PRO VAL LEU TYR SEQRES 18 A 227 VAL PRO TRP SER ARG ALA SEQRES 1 B 227 MET LEU ASP LEU LEU VAL VAL ALA PRO HIS PRO ASP ASP SEQRES 2 B 227 GLY GLU LEU GLY CYS GLY GLY THR LEU ALA ARG ALA LYS SEQRES 3 B 227 ALA GLU GLY LEU SER THR GLY ILE LEU ASP LEU THR ARG SEQRES 4 B 227 GLY GLU MET GLY SER LYS GLY THR PRO GLU GLU ARG GLU SEQRES 5 B 227 LYS GLU VAL ALA GLU ALA SER ARG ILE LEU GLY LEU ASP SEQRES 6 B 227 PHE ARG GLY ASN LEU GLY PHE PRO ASP GLY GLY LEU ALA SEQRES 7 B 227 ASP VAL PRO GLU GLN ARG LEU LYS LEU ALA GLN ALA LEU SEQRES 8 B 227 ARG ARG LEU ARG PRO ARG VAL VAL PHE ALA PRO LEU GLU SEQRES 9 B 227 ALA ASP ARG HIS PRO ASP HIS THR ALA ALA SER ARG LEU SEQRES 10 B 227 ALA VAL ALA ALA VAL HIS LEU ALA GLY LEU ARG LYS ALA SEQRES 11 B 227 PRO LEU GLU GLY GLU PRO PHE ARG VAL GLU ARG LEU PHE SEQRES 12 B 227 PHE TYR PRO GLY ASN HIS PRO PHE ALA PRO SER PHE LEU SEQRES 13 B 227 VAL LYS ILE SER ALA PHE ILE ASP GLN TRP GLU ALA ALA SEQRES 14 B 227 VAL LEU ALA TYR ARG SER GLN PHE THR GLY GLU ALA ALA SEQRES 15 B 227 SER GLU THR VAL GLY PRO LYS GLY VAL GLU ALA ARG LYS SEQRES 16 B 227 ALA MET ARG ARG TYR TRP GLY ASN TYR LEU GLY VAL ASP SEQRES 17 B 227 TYR ALA GLU PRO PHE VAL SER PRO LEU PRO VAL LEU TYR SEQRES 18 B 227 VAL PRO TRP SER ARG ALA FORMUL 3 HOH *156(H2 O) HELIX 1 1 ASP A 12 GLU A 28 1 17 HELIX 2 2 THR A 47 GLY A 63 1 17 HELIX 3 3 VAL A 80 ARG A 95 1 16 HELIX 4 4 HIS A 108 GLY A 126 1 19 HELIX 5 5 PHE A 162 ALA A 172 1 11 HELIX 6 6 TYR A 173 THR A 178 1 6 HELIX 7 7 GLY A 187 LEU A 205 1 19 HELIX 8 8 ASP B 12 GLU B 28 1 17 HELIX 9 9 THR B 47 GLY B 63 1 17 HELIX 10 10 VAL B 80 ARG B 95 1 16 HELIX 11 11 HIS B 108 GLY B 126 1 19 HELIX 12 12 PHE B 162 ALA B 172 1 11 HELIX 13 13 GLY B 187 LEU B 205 1 19 SHEET 1 A 5 PHE A 66 PHE A 72 0 SHEET 2 A 5 THR A 32 THR A 38 1 N ASP A 36 O GLY A 68 SHEET 3 A 5 LEU A 2 ALA A 8 1 N ALA A 8 O LEU A 37 SHEET 4 A 5 PRO A 96 PRO A 102 1 O VAL A 98 N LEU A 5 SHEET 5 A 5 ARG A 141 TYR A 145 1 O ARG A 141 N VAL A 99 SHEET 1 B 3 ALA A 210 PHE A 213 0 SHEET 2 B 3 PHE A 155 LYS A 158 -1 N PHE A 155 O PHE A 213 SHEET 3 B 3 VAL B 219 LEU B 220 1 O VAL B 219 N LEU A 156 SHEET 1 C 3 VAL A 219 LEU A 220 0 SHEET 2 C 3 PHE B 155 LYS B 158 1 O LEU B 156 N VAL A 219 SHEET 3 C 3 ALA B 210 PHE B 213 -1 O GLU B 211 N VAL B 157 SHEET 1 D 5 PHE B 66 PHE B 72 0 SHEET 2 D 5 THR B 32 THR B 38 1 N ASP B 36 O GLY B 68 SHEET 3 D 5 LEU B 2 ALA B 8 1 N ALA B 8 O LEU B 37 SHEET 4 D 5 PRO B 96 PRO B 102 1 O VAL B 98 N LEU B 5 SHEET 5 D 5 ARG B 141 TYR B 145 1 O PHE B 143 N VAL B 99 CRYST1 107.134 107.134 98.617 90.00 90.00 120.00 P 3 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 0.009334 0.005389 0.000000 0.00000 SCALE2 0.000000 0.010778 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010140 0.00000