HEADER TRANSFERASE 06-APR-11 3RFF
TITLE PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM MYCOBACTERIUM TUBERCULOSIS
TITLE 2 (1.76 A RESOLUTION)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-157;
COMPND 5 SYNONYM: DEPHOSPHO-COA PYROPHOSPHORYLASE, PANTETHEINE-PHOSPHATE
COMPND 6 ADENYLYLTRANSFERASE, PPAT;
COMPND 7 EC: 2.7.7.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: COAD, KDTB, RV2965C, MT3043, MTCY349.22, U0002E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.I.TIMOFEEV,E.A.SMIRNOVA,L.A.CHUPOVA,R.S.ESIPOV,I.P.KURANOVA
REVDAT 2 13-SEP-23 3RFF 1 REMARK
REVDAT 1 11-APR-12 3RFF 0
JRNL AUTH V.I.TIMOFEEV,E.A.SMIRNOVA,L.A.CHUPOVA,R.S.ESIPOV,
JRNL AUTH 2 I.P.KURANOVA
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF PHOSPHOPANTETHEINE
JRNL TITL 2 ADENYLYLTRANSFERASE FROM MYCOBACTERIUM TUBERCULOSIS IN THE
JRNL TITL 3 APO FORM AND IN COMPLEXES WITH COENZYME A AND D
JRNL REF CRYSTALLOGRAPHY REPORTS V. 57 96 2012
JRNL REFN ISSN 1063-7745
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.530
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 19710
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1003
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1230
REMARK 3 ANGLE : 0.889 1669
REMARK 3 CHIRALITY : 0.058 196
REMARK 3 PLANARITY : 0.004 219
REMARK 3 DIHEDRAL : 15.512 449
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28293
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1TFU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -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 SMTRY1 7 1.000000 0.000000 0.000000 49.33900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 28.48588
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.95167
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 49.33900
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 28.48588
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.95167
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 49.33900
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 28.48588
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.95167
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 49.33900
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 28.48588
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.95167
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 49.33900
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 28.48588
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.95167
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 49.33900
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 28.48588
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.95167
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 56.97177
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 75.90333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 56.97177
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 75.90333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 56.97177
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 75.90333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 56.97177
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 75.90333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 56.97177
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 75.90333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 56.97177
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 75.90333
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 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 -49.33900
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -85.45765
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 49.33900
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -85.45765
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 49.33900
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 -28.48588
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -37.95167
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 -113.94354
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 -37.95167
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 -49.33900
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 -28.48588
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 -37.95167
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 40
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 78 CZ NH1 NH2
REMARK 480 GLU A 96 CG CD OE1 OE2
REMARK 480 ASP A 154 OD1 OD2
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 LYS A 41 111.24 44.18
REMARK 500 THR A 42 13.48 170.47
REMARK 500 THR A 83 21.95 -141.12
REMARK 500 ALA A 109 -1.65 -140.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RHS RELATED DB: PDB
REMARK 900 RELATED ID: 3RFF RELATED DB: PDB
DBREF 3RFF A 1 157 UNP P0A530 COAD_MYCTU 1 157
SEQRES 1 A 157 MET THR GLY ALA VAL CYS PRO GLY SER PHE ASP PRO VAL
SEQRES 2 A 157 THR LEU GLY HIS VAL ASP ILE PHE GLU ARG ALA ALA ALA
SEQRES 3 A 157 GLN PHE ASP GLU VAL VAL VAL ALA ILE LEU VAL ASN PRO
SEQRES 4 A 157 ALA LYS THR GLY MET PHE ASP LEU ASP GLU ARG ILE ALA
SEQRES 5 A 157 MET VAL LYS GLU SER THR THR HIS LEU PRO ASN LEU ARG
SEQRES 6 A 157 VAL GLN VAL GLY HIS GLY LEU VAL VAL ASP PHE VAL ARG
SEQRES 7 A 157 SER CYS GLY MET THR ALA ILE VAL LYS GLY LEU ARG THR
SEQRES 8 A 157 GLY THR ASP PHE GLU TYR GLU LEU GLN MET ALA GLN MET
SEQRES 9 A 157 ASN LYS HIS ILE ALA GLY VAL ASP THR PHE PHE VAL ALA
SEQRES 10 A 157 THR ALA PRO ARG TYR SER PHE VAL SER SER SER LEU ALA
SEQRES 11 A 157 LYS GLU VAL ALA MET LEU GLY GLY ASP VAL SER GLU LEU
SEQRES 12 A 157 LEU PRO GLU PRO VAL ASN ARG ARG LEU ARG ASP ARG LEU
SEQRES 13 A 157 ASN
FORMUL 2 HOH *58(H2 O)
HELIX 1 1 THR A 14 PHE A 28 1 15
HELIX 2 2 ASP A 46 SER A 57 1 12
HELIX 3 3 LEU A 72 CYS A 80 1 9
HELIX 4 4 ASP A 94 GLY A 110 1 17
HELIX 5 5 ALA A 119 SER A 123 5 5
HELIX 6 6 SER A 126 LEU A 136 1 11
HELIX 7 7 VAL A 140 LEU A 144 5 5
HELIX 8 8 PRO A 145 ASN A 157 1 13
SHEET 1 A 3 GLY A 3 GLY A 8 0
SHEET 2 A 3 GLU A 30 LEU A 36 1 O VAL A 32 N CYS A 6
SHEET 3 A 3 LEU A 64 GLY A 69 1 O ARG A 65 N VAL A 33
SHEET 1 B 2 ALA A 84 LEU A 89 0
SHEET 2 B 2 ASP A 112 ALA A 117 1 O PHE A 114 N ILE A 85
CISPEP 1 ASP A 11 PRO A 12 0 -1.73
CRYST1 98.678 98.678 113.855 90.00 90.00 120.00 H 3 2 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 0.010134 0.005851 0.000000 0.00000
SCALE2 0.000000 0.011702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008783 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
