HEADER LYASE 09-JUN-04 1TLU
TITLE CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA S-ADENOSYLMETHIONINE
TITLE 2 DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME, ADOMETDC,
COMPND 3 SAMDC;
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 4.1.1.50;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: SPEH, TM0655;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS TWO-LAYER ALPHA BETA-SANDWICH, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.V.TOMS,C.KINSLAND,D.E.MCCLOSKEY,A.E.PEGG,S.E.EALICK
REVDAT 4 14-FEB-24 1TLU 1 REMARK
REVDAT 3 24-FEB-09 1TLU 1 VERSN
REVDAT 2 10-AUG-04 1TLU 1 JRNL
REVDAT 1 29-JUN-04 1TLU 0
JRNL AUTH A.V.TOMS,C.KINSLAND,D.E.MCCLOSKEY,A.E.PEGG,S.E.EALICK
JRNL TITL EVOLUTIONARY LINKS AS REVEALED BY THE STRUCTURE OF
JRNL TITL 2 THERMOTOGA MARITIMA S-ADENOSYLMETHIONINE DECARBOXYLASE.
JRNL REF J.BIOL.CHEM. V. 279 33837 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15150268
JRNL DOI 10.1074/JBC.M403369200
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 630823.030
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 39077
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3788
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6387
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 685
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 : 1868
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 162
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : 1.31000
REMARK 3 B12 (A**2) : 0.42000
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) : 0.16
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.030 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.030 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.250 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.44
REMARK 3 BSOL : 88.52
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 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TWINNING OPERATOR WAS USED TO ENSURE
REMARK 3 THAT PAIRS OF TWIN RELATED REFLECTIONS WERE IN THE SAME SET
REMARK 4
REMARK 4 1TLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022753.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 8-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39077
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 24.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SINGLE WAVELENGTH
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 (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM FORMATE, HEPES, PH 8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295.4K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 1.000000 0.000000 0.000000 52.49700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.30916
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.23167
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 52.49700
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 30.30916
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.23167
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 52.49700
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 30.30916
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.23167
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.61831
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 46.46333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 60.61831
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 46.46333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 60.61831
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 46.46333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 BIOLOGICAL ASSEMBLY IS A DIMER. THE ASYMMETRIC UNIT
REMARK 300 CONTAINS 1 BIOLOGICAL UNIT.
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: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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 GLY A 119
REMARK 465 ILE A 120
REMARK 465 PRO A 121
REMARK 465 GLU A 122
REMARK 465 ASP A 123
REMARK 465 SER A 124
REMARK 465 PRO A 125
REMARK 465 HIS A 126
REMARK 465 LYS A 127
REMARK 465 ALA A 128
REMARK 465 ALA A 129
REMARK 465 VAL A 130
REMARK 465 MET B 1
REMARK 465 GLY B 119
REMARK 465 ILE B 120
REMARK 465 PRO B 121
REMARK 465 GLU B 122
REMARK 465 ASP B 123
REMARK 465 SER B 124
REMARK 465 PRO B 125
REMARK 465 HIS B 126
REMARK 465 LYS B 127
REMARK 465 ALA B 128
REMARK 465 ALA B 129
REMARK 465 VAL B 130
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 LYS A 2 CG CD CE NZ
REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 49 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 2 CG CD CE NZ
REMARK 470 GLN B 24 CG CD OE1 NE2
REMARK 470 GLU B 85 CG CD OE1 OE2
REMARK 470 LYS B 98 CG CD CE NZ
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 63 -161.16 -165.76
REMARK 500 SER B 61 105.05 -57.88
REMARK 500 SER B 63 -157.58 -149.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TMI RELATED DB: PDB
REMARK 900 MUTANT PROENZYME
DBREF 1TLU A 1 130 UNP Q9WZC3 SPEH_THEMA 1 130
DBREF 1TLU B 1 130 UNP Q9WZC3 SPEH_THEMA 1 130
SEQRES 1 A 130 MET LYS SER LEU GLY ARG HIS LEU VAL ALA GLU PHE TYR
SEQRES 2 A 130 GLU CYS ASP ARG GLU VAL LEU ASP ASN VAL GLN LEU ILE
SEQRES 3 A 130 GLU GLN GLU MET LYS GLN ALA ALA TYR GLU SER GLY ALA
SEQRES 4 A 130 THR ILE VAL THR SER THR PHE HIS ARG PHE LEU PRO TYR
SEQRES 5 A 130 GLY VAL SER GLY VAL VAL VAL ILE SER GLU SER HIS LEU
SEQRES 6 A 130 THR ILE HIS THR TRP PRO GLU TYR GLY TYR ALA ALA ILE
SEQRES 7 A 130 ASP LEU PHE THR CYS GLY GLU ASP VAL ASP PRO TRP LYS
SEQRES 8 A 130 ALA PHE GLU HIS LEU LYS LYS ALA LEU LYS ALA LYS ARG
SEQRES 9 A 130 VAL HIS VAL VAL GLU HIS GLU ARG GLY ARG TYR ASP GLU
SEQRES 10 A 130 ILE GLY ILE PRO GLU ASP SER PRO HIS LYS ALA ALA VAL
SEQRES 1 B 130 MET LYS SER LEU GLY ARG HIS LEU VAL ALA GLU PHE TYR
SEQRES 2 B 130 GLU CYS ASP ARG GLU VAL LEU ASP ASN VAL GLN LEU ILE
SEQRES 3 B 130 GLU GLN GLU MET LYS GLN ALA ALA TYR GLU SER GLY ALA
SEQRES 4 B 130 THR ILE VAL THR SER THR PHE HIS ARG PHE LEU PRO TYR
SEQRES 5 B 130 GLY VAL SER GLY VAL VAL VAL ILE SER GLU SER HIS LEU
SEQRES 6 B 130 THR ILE HIS THR TRP PRO GLU TYR GLY TYR ALA ALA ILE
SEQRES 7 B 130 ASP LEU PHE THR CYS GLY GLU ASP VAL ASP PRO TRP LYS
SEQRES 8 B 130 ALA PHE GLU HIS LEU LYS LYS ALA LEU LYS ALA LYS ARG
SEQRES 9 B 130 VAL HIS VAL VAL GLU HIS GLU ARG GLY ARG TYR ASP GLU
SEQRES 10 B 130 ILE GLY ILE PRO GLU ASP SER PRO HIS LYS ALA ALA VAL
FORMUL 3 HOH *162(H2 O)
HELIX 1 1 ASP A 16 ASP A 21 1 6
HELIX 2 2 ASN A 22 GLY A 38 1 17
HELIX 3 3 PRO A 71 GLY A 74 5 4
HELIX 4 4 ASP A 88 LYS A 101 1 14
HELIX 5 5 ASP B 16 ASP B 21 1 6
HELIX 6 6 ASN B 22 GLY B 38 1 17
HELIX 7 7 PRO B 71 GLY B 74 5 4
HELIX 8 8 ASP B 88 LYS B 101 1 14
SHEET 1 A 6 ILE A 41 ARG A 48 0
SHEET 2 A 6 VAL A 54 ILE A 60 -1 O VAL A 59 N VAL A 42
SHEET 3 A 6 SER A 63 TRP A 70 -1 O LEU A 65 N VAL A 58
SHEET 4 A 6 TYR A 75 CYS A 83 -1 O PHE A 81 N HIS A 64
SHEET 5 A 6 SER A 3 TYR A 13 -1 N ALA A 10 O ILE A 78
SHEET 6 A 6 ARG A 104 ARG A 114 -1 O HIS A 110 N HIS A 7
SHEET 1 B 6 ILE B 41 ARG B 48 0
SHEET 2 B 6 VAL B 54 ILE B 60 -1 O SER B 55 N HIS B 47
SHEET 3 B 6 SER B 63 TRP B 70 -1 O LEU B 65 N VAL B 58
SHEET 4 B 6 TYR B 75 CYS B 83 -1 O ALA B 77 N HIS B 68
SHEET 5 B 6 SER B 3 TYR B 13 -1 N ARG B 6 O THR B 82
SHEET 6 B 6 ARG B 104 ARG B 114 -1 O HIS B 110 N HIS B 7
CISPEP 1 LEU A 50 PRO A 51 0 0.03
CISPEP 2 LEU B 50 PRO B 51 0 0.34
CRYST1 104.994 104.994 69.695 90.00 90.00 120.00 H 3 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 0.009524 0.005499 0.000000 0.00000
SCALE2 0.000000 0.010998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
