HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 12-JAN-06 2DCT
TITLE CRYSTAL STRUCTURE OF THE TT1209 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN TTHA0104;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TT1209 PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS STRUCTURAL GENOMICS, THERMUS THERMOPHILUS HB8, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ASADA,M.SUGAHARA,K.SHIMIZU,H.YAMAMOTO,H.SHIMADA,T.NAKAMOTO,N.ONO,
AUTHOR 2 N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2DCT 1 REMARK LINK
REVDAT 3 13-JUL-11 2DCT 1 VERSN
REVDAT 2 24-FEB-09 2DCT 1 VERSN
REVDAT 1 24-JAN-06 2DCT 0
JRNL AUTH Y.ASADA,M.SUGAHARA,K.SHIMIZU,H.YAMAMOTO,H.SHIMADA,Y.MISUMI,
JRNL AUTH 2 T.NAKAMOTO,N.ONO,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF THE TT1209 FROM THERMUS THERMOPHILUS
JRNL TITL 2 HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 53541
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RAMDOM
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2670
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 347
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1616
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 378
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.23000
REMARK 3 B22 (A**2) : 1.23000
REMARK 3 B33 (A**2) : -2.47000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.11
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000025262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BENDING MAGNET
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.190
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PERON
REMARK 200 STARTING MODEL: 1V70.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA CITR 0.4M, HEPES 0.1M, PH 7.1,
REMARK 280 MICROBATCH, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.55500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.12050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.12050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.33250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.12050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.12050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.77750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.12050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.12050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 113.33250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.12050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.12050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.77750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.55500
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 300 REMARK: THE BIOLOGOCAL ASSEMBLY IS DIMER
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: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL B2001 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2125 LIES ON A SPECIAL POSITION.
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 44 NE2
REMARK 620 2 VAL A 45 O 77.1
REMARK 620 3 HOH A1012 O 95.8 73.7
REMARK 620 4 HOH A1017 O 89.5 93.8 164.9
REMARK 620 5 HOH A1045 O 172.2 95.3 83.6 89.2
REMARK 620 6 HOH A1158 O 88.5 165.4 105.5 88.7 99.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001209.2 RELATED DB: TARGETDB
DBREF 2DCT A 1 105 GB 55980073 YP_143370 1 105
DBREF 2DCT B 1 105 GB 55980073 YP_143370 1 105
SEQRES 1 A 105 MET GLU ILE LYS ASP LEU LYS ARG LEU ALA ARG TYR ASN
SEQRES 2 A 105 PRO GLU LYS MET ALA LYS ILE PRO VAL PHE GLN SER GLU
SEQRES 3 A 105 ARG MET LEU TYR ASP LEU TYR ALA LEU LEU PRO GLY GLN
SEQRES 4 A 105 ALA GLN LYS VAL HIS VAL HIS GLU GLY SER ASP LYS VAL
SEQRES 5 A 105 TYR TYR ALA LEU GLU GLY GLU VAL VAL VAL ARG VAL GLY
SEQRES 6 A 105 GLU GLU GLU ALA LEU LEU ALA PRO GLY MET ALA ALA PHE
SEQRES 7 A 105 ALA PRO ALA GLY ALA PRO HIS GLY VAL ARG ASN GLU SER
SEQRES 8 A 105 ALA SER PRO ALA LEU LEU LEU VAL VAL THR ALA PRO ARG
SEQRES 9 A 105 PRO
SEQRES 1 B 105 MET GLU ILE LYS ASP LEU LYS ARG LEU ALA ARG TYR ASN
SEQRES 2 B 105 PRO GLU LYS MET ALA LYS ILE PRO VAL PHE GLN SER GLU
SEQRES 3 B 105 ARG MET LEU TYR ASP LEU TYR ALA LEU LEU PRO GLY GLN
SEQRES 4 B 105 ALA GLN LYS VAL HIS VAL HIS GLU GLY SER ASP LYS VAL
SEQRES 5 B 105 TYR TYR ALA LEU GLU GLY GLU VAL VAL VAL ARG VAL GLY
SEQRES 6 B 105 GLU GLU GLU ALA LEU LEU ALA PRO GLY MET ALA ALA PHE
SEQRES 7 B 105 ALA PRO ALA GLY ALA PRO HIS GLY VAL ARG ASN GLU SER
SEQRES 8 B 105 ALA SER PRO ALA LEU LEU LEU VAL VAL THR ALA PRO ARG
SEQRES 9 B 105 PRO
HET NA A1001 1
HET CL B2001 1
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 NA NA 1+
FORMUL 4 CL CL 1-
FORMUL 5 HOH *378(H2 O)
HELIX 1 1 LYS A 7 ALA A 10 5 4
HELIX 2 2 LEU B 6 ALA B 10 1 5
SHEET 1 A 6 GLU A 2 ASP A 5 0
SHEET 2 A 6 MET B 75 ALA B 79 -1 O PHE B 78 N GLU A 2
SHEET 3 A 6 ASP B 50 GLU B 57 -1 N LYS B 51 O ALA B 79
SHEET 4 A 6 ALA B 95 ALA B 102 -1 O ALA B 102 N ASP B 50
SHEET 5 A 6 LEU B 29 LEU B 35 -1 N ASP B 31 O VAL B 99
SHEET 6 A 6 ALA B 18 GLN B 24 -1 N ILE B 20 O LEU B 32
SHEET 1 B 6 ALA A 18 GLN A 24 0
SHEET 2 B 6 LEU A 29 LEU A 35 -1 O LEU A 32 N ILE A 20
SHEET 3 B 6 ALA A 95 ALA A 102 -1 O VAL A 99 N ASP A 31
SHEET 4 B 6 ASP A 50 GLU A 57 -1 N ASP A 50 O ALA A 102
SHEET 5 B 6 MET A 75 ALA A 79 -1 O ALA A 79 N LYS A 51
SHEET 6 B 6 GLU B 2 ASP B 5 -1 O GLU B 2 N PHE A 78
SHEET 1 C 4 ALA A 40 HIS A 44 0
SHEET 2 C 4 HIS A 85 ARG A 88 -1 O HIS A 85 N HIS A 44
SHEET 3 C 4 VAL A 60 VAL A 64 -1 N ARG A 63 O GLY A 86
SHEET 4 C 4 GLU A 67 LEU A 71 -1 O LEU A 71 N VAL A 60
SHEET 1 D 4 ALA B 40 HIS B 44 0
SHEET 2 D 4 HIS B 85 ARG B 88 -1 O VAL B 87 N GLN B 41
SHEET 3 D 4 VAL B 60 VAL B 64 -1 N VAL B 61 O ARG B 88
SHEET 4 D 4 GLU B 67 LEU B 71 -1 O LEU B 71 N VAL B 60
LINK NE2 HIS A 44 NA NA A1001 1555 1555 2.91
LINK O VAL A 45 NA NA A1001 1555 1555 2.41
LINK NA NA A1001 O HOH A1012 1555 1555 1.99
LINK NA NA A1001 O HOH A1017 1555 1555 2.46
LINK NA NA A1001 O HOH A1045 1555 6455 2.12
LINK NA NA A1001 O HOH A1158 1555 1555 2.57
CISPEP 1 ALA A 102 PRO A 103 0 -0.57
CISPEP 2 ALA B 102 PRO B 103 0 -0.17
SITE 1 AC1 6 HIS A 44 VAL A 45 HOH A1012 HOH A1017
SITE 2 AC1 6 HOH A1045 HOH A1158
SITE 1 AC2 2 ARG B 104 HOH B2181
CRYST1 62.241 62.241 151.110 90.00 90.00 90.00 P 43 21 2 16
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 0.016067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006618 0.00000
(ATOM LINES ARE NOT SHOWN.)
END