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HEADER OXIDOREDUCTASE 28-FEB-03 1ONL TITLE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS HB8 H-PROTEIN OF TITLE 2 THE GLYCINE CLEAVAGE SYSTEM COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCINE CLEAVAGE SYSTEM H PROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 GENE: GCVH; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A-GCVH KEYWDS HYBRID BARREL-SANDWICH STRUCTURE, STRUCTURAL GENOMICS, KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI EXPDTA X-RAY DIFFRACTION AUTHOR T.NAKAI,J.ISHIJIMA,R.MASUI,S.KURAMITSU,N.KAMIYA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 1 26-AUG-03 1ONL 0 JRNL AUTH T.NAKAI,J.ISHIJIMA,R.MASUI,S.KURAMITSU,N.KAMIYA JRNL TITL STRUCTURE OF THERMUS THERMOPHILUS HB8 H-PROTEIN OF JRNL TITL 2 THE GLYCINE-CLEAVAGE SYSTEM, RESOLVED BY A JRNL TITL 3 SIX-DIMENSIONAL MOLECULAR-REPLACEMENT METHOD. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 1610 2003 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 220770.620 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 11137 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) : 0.186 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.400 REMARK 3 FREE R VALUE TEST SET COUNT : 1155 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 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) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1609 REMARK 3 BIN R VALUE (WORKING SET) : 0.2430 REMARK 3 BIN FREE R VALUE : 0.3160 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 181 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2955 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 115 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.70000 REMARK 3 B22 (A**2) : 2.70000 REMARK 3 B33 (A**2) : -5.40000 REMARK 3 B12 (A**2) : 5.83000 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) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : 0.27 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) : 0.36 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.20 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.74 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) : 1.250 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.040 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 1.940 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.860 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.36 REMARK 3 BSOL : 36.89 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 1ONL 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 RCSB018475. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JUN-2001 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.30 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) : 1.00 REMARK 200 MONOCHROMATOR : SI111 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 : 11730 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.010 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 11.500 REMARK 200 R MERGE (I) : 0.10900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5 REMARK 200 DATA REDUNDANCY IN SHELL : 5.40 REMARK 200 R MERGE FOR SHELL (I) : 0.35500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: PDB ENTRY 1HPC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 37.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, GLYCEROL, PH REMARK 280 4.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X-Y,X,5/6+Z REMARK 290 3555 -Y,X-Y,2/3+Z REMARK 290 4555 -X,-Y,1/2+Z REMARK 290 5555 -X+Y,-X,1/3+Z REMARK 290 6555 Y,-X+Y,1/6+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 159.32500 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 127.46000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 95.59500 REMARK 290 SMTRY1 5 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.73000 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 31.86500 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 3 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 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: 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: 3 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 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 MET B 1 REMARK 465 MET C 1 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 LEU A 24 N - CA - C ANGL. DEV. = -7.4 DEGREES REMARK 500 VAL A 49 N - CA - C ANGL. DEV. = -7.7 DEGREES REMARK 500 LEU B 24 N - CA - C ANGL. DEV. = -7.8 DEGREES REMARK 500 SER B 61 N - CA - C ANGL. DEV. = -8.2 DEGREES REMARK 500 ILE C 76 N - CA - C ANGL. DEV. = -7.7 DEGREES REMARK 500 LYS C 104 N - CA - C ANGL. DEV. = -8.0 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: TTK003000357.1 RELATED DB: TARGETDB DBREF 1ONL A 1 128 UNP P83697 P83697_THETH 1 128 DBREF 1ONL B 1 128 UNP P83697 P83697_THETH 1 128 DBREF 1ONL C 1 128 UNP P83697 P83697_THETH 1 128 SEQRES 1 A 128 MET ASP ILE PRO LYS ASP ARG PHE TYR THR LYS THR HIS SEQRES 2 A 128 GLU TRP ALA LEU PRO GLU GLY ASP THR VAL LEU VAL GLY SEQRES 3 A 128 ILE THR ASP TYR ALA GLN ASP ALA LEU GLY ASP VAL VAL SEQRES 4 A 128 TYR VAL GLU LEU PRO GLU VAL GLY ARG VAL VAL GLU LYS SEQRES 5 A 128 GLY GLU ALA VAL ALA VAL VAL GLU SER VAL LYS THR ALA SEQRES 6 A 128 SER ASP ILE TYR ALA PRO VAL ALA GLY GLU ILE VAL GLU SEQRES 7 A 128 VAL ASN LEU ALA LEU GLU LYS THR PRO GLU LEU VAL ASN SEQRES 8 A 128 GLN ASP PRO TYR GLY GLU GLY TRP ILE PHE ARG LEU LYS SEQRES 9 A 128 PRO ARG ASP MET GLY ASP LEU ASP GLU LEU LEU ASP ALA SEQRES 10 A 128 GLY GLY TYR GLN GLU VAL LEU GLU SER GLU ALA SEQRES 1 B 128 MET ASP ILE PRO LYS ASP ARG PHE TYR THR LYS THR HIS SEQRES 2 B 128 GLU TRP ALA LEU PRO GLU GLY ASP THR VAL LEU VAL GLY SEQRES 3 B 128 ILE THR ASP TYR ALA GLN ASP ALA LEU GLY ASP VAL VAL SEQRES 4 B 128 TYR VAL GLU LEU PRO GLU VAL GLY ARG VAL VAL GLU LYS SEQRES 5 B 128 GLY GLU ALA VAL ALA VAL VAL GLU SER VAL LYS THR ALA SEQRES 6 B 128 SER ASP ILE TYR ALA PRO VAL ALA GLY GLU ILE VAL GLU SEQRES 7 B 128 VAL ASN LEU ALA LEU GLU LYS THR PRO GLU LEU VAL ASN SEQRES 8 B 128 GLN ASP PRO TYR GLY GLU GLY TRP ILE PHE ARG LEU LYS SEQRES 9 B 128 PRO ARG ASP MET GLY ASP LEU ASP GLU LEU LEU ASP ALA SEQRES 10 B 128 GLY GLY TYR GLN GLU VAL LEU GLU SER GLU ALA SEQRES 1 C 128 MET ASP ILE PRO LYS ASP ARG PHE TYR THR LYS THR HIS SEQRES 2 C 128 GLU TRP ALA LEU PRO GLU GLY ASP THR VAL LEU VAL GLY SEQRES 3 C 128 ILE THR ASP TYR ALA GLN ASP ALA LEU GLY ASP VAL VAL SEQRES 4 C 128 TYR VAL GLU LEU PRO GLU VAL GLY ARG VAL VAL GLU LYS SEQRES 5 C 128 GLY GLU ALA VAL ALA VAL VAL GLU SER VAL LYS THR ALA SEQRES 6 C 128 SER ASP ILE TYR ALA PRO VAL ALA GLY GLU ILE VAL GLU SEQRES 7 C 128 VAL ASN LEU ALA LEU GLU LYS THR PRO GLU LEU VAL ASN SEQRES 8 C 128 GLN ASP PRO TYR GLY GLU GLY TRP ILE PHE ARG LEU LYS SEQRES 9 C 128 PRO ARG ASP MET GLY ASP LEU ASP GLU LEU LEU ASP ALA SEQRES 10 C 128 GLY GLY TYR GLN GLU VAL LEU GLU SER GLU ALA FORMUL 4 HOH *115(H2 O) HELIX 1 1 THR A 28 GLY A 36 1 9 HELIX 2 2 LEU A 81 THR A 86 1 6 HELIX 3 3 GLU A 88 ASP A 93 1 6 HELIX 4 4 ASP A 107 LEU A 114 5 8 HELIX 5 5 ASP A 116 GLU A 127 1 12 HELIX 6 6 THR B 28 GLY B 36 1 9 HELIX 7 7 LEU B 81 THR B 86 1 6 HELIX 8 8 GLU B 88 ASP B 93 1 6 HELIX 9 9 ASP B 107 LEU B 114 5 8 HELIX 10 10 ASP B 116 SER B 126 1 11 HELIX 11 11 THR C 28 GLY C 36 1 9 HELIX 12 12 LEU C 81 THR C 86 1 6 HELIX 13 13 GLU C 88 ASP C 93 1 6 HELIX 14 14 ASP C 107 LEU C 114 5 8 HELIX 15 15 ASP C 116 GLU C 127 1 12 SHEET 1 A 6 PHE A 8 TYR A 9 0 SHEET 2 A 6 GLU A 14 GLU A 19 -1 O ALA A 16 N PHE A 8 SHEET 3 A 6 THR A 22 ILE A 27 -1 O THR A 22 N GLU A 19 SHEET 4 A 6 PHE A 101 PRO A 105 -1 O LEU A 103 N VAL A 23 SHEET 5 A 6 GLY A 74 VAL A 79 -1 N GLU A 75 O LYS A 104 SHEET 6 A 6 VAL A 49 VAL A 50 -1 N VAL A 50 O GLY A 74 SHEET 1 B 3 VAL A 38 GLU A 42 0 SHEET 2 B 3 ALA A 55 SER A 61 -1 O VAL A 58 N GLU A 42 SHEET 3 B 3 ALA A 65 TYR A 69 -1 O ILE A 68 N ALA A 57 SHEET 1 C 6 PHE B 8 TYR B 9 0 SHEET 2 C 6 GLU B 14 GLU B 19 -1 O ALA B 16 N PHE B 8 SHEET 3 C 6 THR B 22 ILE B 27 -1 O LEU B 24 N LEU B 17 SHEET 4 C 6 PHE B 101 PRO B 105 -1 O LEU B 103 N VAL B 23 SHEET 5 C 6 GLY B 74 VAL B 79 -1 N GLU B 75 O LYS B 104 SHEET 6 C 6 VAL B 49 VAL B 50 -1 N VAL B 50 O GLY B 74 SHEET 1 D 3 VAL B 38 GLU B 42 0 SHEET 2 D 3 ALA B 55 SER B 61 -1 O VAL B 58 N GLU B 42 SHEET 3 D 3 ALA B 65 TYR B 69 -1 O ILE B 68 N ALA B 57 SHEET 1 E 6 PHE C 8 TYR C 9 0 SHEET 2 E 6 GLU C 14 GLU C 19 -1 O ALA C 16 N PHE C 8 SHEET 3 E 6 THR C 22 ILE C 27 -1 O GLY C 26 N TRP C 15 SHEET 4 E 6 PHE C 101 PRO C 105 -1 O PHE C 101 N VAL C 25 SHEET 5 E 6 GLY C 74 VAL C 79 -1 N GLU C 78 O ARG C 102 SHEET 6 E 6 VAL C 49 VAL C 50 -1 N VAL C 50 O GLY C 74 SHEET 1 F 3 VAL C 38 GLU C 42 0 SHEET 2 F 3 ALA C 55 SER C 61 -1 O GLU C 60 N TYR C 40 SHEET 3 F 3 ALA C 65 TYR C 69 -1 O ILE C 68 N ALA C 57 CRYST1 55.775 55.775 191.190 90.00 90.00 120.00 P 65 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 0.017929 0.010351 0.000000 0.00000 SCALE2 0.000000 0.020703 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005230 0.00000