HEADER TRANSFERASE 02-NOV-01 1KAM
TITLE STRUCTURE OF BACILLUS SUBTILIS NICOTINIC ACID MONONUCLEOTIDE ADENYLYL
TITLE 2 TRANSFERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DEAMIDO-NAD(+) PYROPHOSPHORYLASE; DEAMIDO-NAD(+)
COMPND 5 DIPHOSPHORYLASE; NICOTINATE MONONUCLEOTIDE ADENYLYLTRANSFERASE; NAMN
COMPND 6 ADENYLYLTRANSFERASE; YQEJ;
COMPND 7 EC: 2.7.7.18;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: NADD;
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: PML208
KEYWDS ROSSMANN FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.OLLAND,K.W.UNDERWOOD,R.M.CZERWINSKI,M.C.LO,A.AULABAUGH,J.BARD,
AUTHOR 2 M.L.STAHL,W.S.SOMERS,F.X.SULLIVAN,R.CHOPRA
REVDAT 4 07-FEB-24 1KAM 1 SEQADV
REVDAT 3 12-NOV-14 1KAM 1 KEYWDS
REVDAT 2 24-FEB-09 1KAM 1 VERSN
REVDAT 1 12-JUL-02 1KAM 0
JRNL AUTH A.M.OLLAND,K.W.UNDERWOOD,R.M.CZERWINSKI,M.C.LO,A.AULABAUGH,
JRNL AUTH 2 J.BARD,M.L.STAHL,W.S.SOMERS,F.X.SULLIVAN,R.CHOPRA
JRNL TITL IDENTIFICATION, CHARACTERIZATION, AND CRYSTAL STRUCTURE OF
JRNL TITL 2 BACILLUS SUBTILIS NICOTINIC ACID MONONUCLEOTIDE
JRNL TITL 3 ADENYLYLTRANSFERASE.
JRNL REF J.BIOL.CHEM. V. 277 3698 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11704676
JRNL DOI 10.1074/JBC.M109670200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 43266
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) : 0.222
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2163
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2764
REMARK 3 BIN FREE R VALUE : 0.4063
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 41
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5845
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 139
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.347
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1KAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-01
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792, 0.9567
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51628
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 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) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, MAGNESIUM CHLORIDE, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP AT 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.05150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 HIS A -4
REMARK 465 MET A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 GLY A 0
REMARK 465 PRO A 43
REMARK 465 HIS A 44
REMARK 465 LYS A 45
REMARK 465 GLN A 46
REMARK 465 ASN A 47
REMARK 465 GLU A 48
REMARK 465 ASP A 49
REMARK 465 TYR A 50
REMARK 465 THR A 51
REMARK 465 HIS B -4
REMARK 465 MET B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 LYS B 45
REMARK 465 GLN B 46
REMARK 465 ASN B 47
REMARK 465 GLU B 48
REMARK 465 ASP B 49
REMARK 465 TYR B 50
REMARK 465 LEU B 119
REMARK 465 ASP B 120
REMARK 465 GLU B 121
REMARK 465 LEU B 122
REMARK 465 LEU B 123
REMARK 465 ASN B 124
REMARK 465 LEU B 125
REMARK 465 SER B 189
REMARK 465 HIS C -4
REMARK 465 MET C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 GLY C 0
REMARK 465 PRO C 43
REMARK 465 HIS C 44
REMARK 465 LYS C 45
REMARK 465 GLN C 46
REMARK 465 ASN C 47
REMARK 465 GLU C 48
REMARK 465 ASP C 49
REMARK 465 TYR C 50
REMARK 465 THR C 51
REMARK 465 SER C 189
REMARK 465 HIS D -4
REMARK 465 MET D -3
REMARK 465 PRO D -2
REMARK 465 GLY D -1
REMARK 465 GLY D 0
REMARK 465 PRO D 42
REMARK 465 PRO D 43
REMARK 465 HIS D 44
REMARK 465 LYS D 45
REMARK 465 GLN D 46
REMARK 465 ASN D 47
REMARK 465 GLU D 48
REMARK 465 ASP D 49
REMARK 465 TYR D 50
REMARK 465 ASP D 120
REMARK 465 GLU D 121
REMARK 465 LEU D 122
REMARK 465 LEU D 123
REMARK 465 ASN D 124
REMARK 465 SER D 189
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 82 C - N - CA ANGL. DEV. = 13.6 DEGREES
REMARK 500 PRO D 82 C - N - CD ANGL. DEV. = -23.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 136 116.14 52.72
REMARK 500 THR A 140 25.94 -179.48
REMARK 500 PRO A 141 56.48 -1.39
REMARK 500 PRO A 143 -93.66 -47.42
REMARK 500 LEU A 144 128.33 52.54
REMARK 500 TYR A 187 16.06 54.58
REMARK 500 PRO B 43 78.98 -34.82
REMARK 500 ALA B 107 47.39 -149.53
REMARK 500 TYR B 171 -4.82 69.62
REMARK 500 PHE C 136 137.32 64.38
REMARK 500 GLU C 139 -100.71 -52.19
REMARK 500 THR C 140 118.05 -6.62
REMARK 500 PRO D 82 -3.95 53.15
REMARK 500 ALA D 107 43.99 -146.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KAQ RELATED DB: PDB
DBREF 1KAM A 1 189 UNP P54455 NADD_BACSU 1 189
DBREF 1KAM B 1 189 UNP P54455 NADD_BACSU 1 189
DBREF 1KAM C 1 189 UNP P54455 NADD_BACSU 1 189
DBREF 1KAM D 1 189 UNP P54455 NADD_BACSU 1 189
SEQADV 1KAM HIS A -4 UNP P54455 EXPRESSION TAG
SEQADV 1KAM MET A -3 UNP P54455 EXPRESSION TAG
SEQADV 1KAM PRO A -2 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY A -1 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY A 0 UNP P54455 EXPRESSION TAG
SEQADV 1KAM SER A 1 UNP P54455 MET 1 CLONING ARTIFACT
SEQADV 1KAM HIS B -4 UNP P54455 EXPRESSION TAG
SEQADV 1KAM MET B -3 UNP P54455 EXPRESSION TAG
SEQADV 1KAM PRO B -2 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY B -1 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY B 0 UNP P54455 EXPRESSION TAG
SEQADV 1KAM SER B 1 UNP P54455 MET 1 CLONING ARTIFACT
SEQADV 1KAM HIS C -4 UNP P54455 EXPRESSION TAG
SEQADV 1KAM MET C -3 UNP P54455 EXPRESSION TAG
SEQADV 1KAM PRO C -2 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY C -1 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY C 0 UNP P54455 EXPRESSION TAG
SEQADV 1KAM SER C 1 UNP P54455 MET 1 CLONING ARTIFACT
SEQADV 1KAM HIS D -4 UNP P54455 EXPRESSION TAG
SEQADV 1KAM MET D -3 UNP P54455 EXPRESSION TAG
SEQADV 1KAM PRO D -2 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY D -1 UNP P54455 EXPRESSION TAG
SEQADV 1KAM GLY D 0 UNP P54455 EXPRESSION TAG
SEQADV 1KAM SER D 1 UNP P54455 MET 1 CLONING ARTIFACT
SEQRES 1 A 194 HIS MET PRO GLY GLY SER LYS LYS ILE GLY ILE PHE GLY
SEQRES 2 A 194 GLY THR PHE ASP PRO PRO HIS ASN GLY HIS LEU LEU MET
SEQRES 3 A 194 ALA ASN GLU VAL LEU TYR GLN ALA GLY LEU ASP GLU ILE
SEQRES 4 A 194 TRP PHE MET PRO ASN GLN ILE PRO PRO HIS LYS GLN ASN
SEQRES 5 A 194 GLU ASP TYR THR ASP SER PHE HIS ARG VAL GLU MET LEU
SEQRES 6 A 194 LYS LEU ALA ILE GLN SER ASN PRO SER PHE LYS LEU GLU
SEQRES 7 A 194 LEU VAL GLU MET GLU ARG GLU GLY PRO SER TYR THR PHE
SEQRES 8 A 194 ASP THR VAL SER LEU LEU LYS GLN ARG TYR PRO ASN ASP
SEQRES 9 A 194 GLN LEU PHE PHE ILE ILE GLY ALA ASP MET ILE GLU TYR
SEQRES 10 A 194 LEU PRO LYS TRP TYR LYS LEU ASP GLU LEU LEU ASN LEU
SEQRES 11 A 194 ILE GLN PHE ILE GLY VAL LYS ARG PRO GLY PHE HIS VAL
SEQRES 12 A 194 GLU THR PRO TYR PRO LEU LEU PHE ALA ASP VAL PRO GLU
SEQRES 13 A 194 PHE GLU VAL SER SER THR MET ILE ARG GLU ARG PHE LYS
SEQRES 14 A 194 SER LYS LYS PRO THR ASP TYR LEU ILE PRO ASP LYS VAL
SEQRES 15 A 194 LYS LYS TYR VAL GLU GLU ASN GLY LEU TYR GLU SER
SEQRES 1 B 194 HIS MET PRO GLY GLY SER LYS LYS ILE GLY ILE PHE GLY
SEQRES 2 B 194 GLY THR PHE ASP PRO PRO HIS ASN GLY HIS LEU LEU MET
SEQRES 3 B 194 ALA ASN GLU VAL LEU TYR GLN ALA GLY LEU ASP GLU ILE
SEQRES 4 B 194 TRP PHE MET PRO ASN GLN ILE PRO PRO HIS LYS GLN ASN
SEQRES 5 B 194 GLU ASP TYR THR ASP SER PHE HIS ARG VAL GLU MET LEU
SEQRES 6 B 194 LYS LEU ALA ILE GLN SER ASN PRO SER PHE LYS LEU GLU
SEQRES 7 B 194 LEU VAL GLU MET GLU ARG GLU GLY PRO SER TYR THR PHE
SEQRES 8 B 194 ASP THR VAL SER LEU LEU LYS GLN ARG TYR PRO ASN ASP
SEQRES 9 B 194 GLN LEU PHE PHE ILE ILE GLY ALA ASP MET ILE GLU TYR
SEQRES 10 B 194 LEU PRO LYS TRP TYR LYS LEU ASP GLU LEU LEU ASN LEU
SEQRES 11 B 194 ILE GLN PHE ILE GLY VAL LYS ARG PRO GLY PHE HIS VAL
SEQRES 12 B 194 GLU THR PRO TYR PRO LEU LEU PHE ALA ASP VAL PRO GLU
SEQRES 13 B 194 PHE GLU VAL SER SER THR MET ILE ARG GLU ARG PHE LYS
SEQRES 14 B 194 SER LYS LYS PRO THR ASP TYR LEU ILE PRO ASP LYS VAL
SEQRES 15 B 194 LYS LYS TYR VAL GLU GLU ASN GLY LEU TYR GLU SER
SEQRES 1 C 194 HIS MET PRO GLY GLY SER LYS LYS ILE GLY ILE PHE GLY
SEQRES 2 C 194 GLY THR PHE ASP PRO PRO HIS ASN GLY HIS LEU LEU MET
SEQRES 3 C 194 ALA ASN GLU VAL LEU TYR GLN ALA GLY LEU ASP GLU ILE
SEQRES 4 C 194 TRP PHE MET PRO ASN GLN ILE PRO PRO HIS LYS GLN ASN
SEQRES 5 C 194 GLU ASP TYR THR ASP SER PHE HIS ARG VAL GLU MET LEU
SEQRES 6 C 194 LYS LEU ALA ILE GLN SER ASN PRO SER PHE LYS LEU GLU
SEQRES 7 C 194 LEU VAL GLU MET GLU ARG GLU GLY PRO SER TYR THR PHE
SEQRES 8 C 194 ASP THR VAL SER LEU LEU LYS GLN ARG TYR PRO ASN ASP
SEQRES 9 C 194 GLN LEU PHE PHE ILE ILE GLY ALA ASP MET ILE GLU TYR
SEQRES 10 C 194 LEU PRO LYS TRP TYR LYS LEU ASP GLU LEU LEU ASN LEU
SEQRES 11 C 194 ILE GLN PHE ILE GLY VAL LYS ARG PRO GLY PHE HIS VAL
SEQRES 12 C 194 GLU THR PRO TYR PRO LEU LEU PHE ALA ASP VAL PRO GLU
SEQRES 13 C 194 PHE GLU VAL SER SER THR MET ILE ARG GLU ARG PHE LYS
SEQRES 14 C 194 SER LYS LYS PRO THR ASP TYR LEU ILE PRO ASP LYS VAL
SEQRES 15 C 194 LYS LYS TYR VAL GLU GLU ASN GLY LEU TYR GLU SER
SEQRES 1 D 194 HIS MET PRO GLY GLY SER LYS LYS ILE GLY ILE PHE GLY
SEQRES 2 D 194 GLY THR PHE ASP PRO PRO HIS ASN GLY HIS LEU LEU MET
SEQRES 3 D 194 ALA ASN GLU VAL LEU TYR GLN ALA GLY LEU ASP GLU ILE
SEQRES 4 D 194 TRP PHE MET PRO ASN GLN ILE PRO PRO HIS LYS GLN ASN
SEQRES 5 D 194 GLU ASP TYR THR ASP SER PHE HIS ARG VAL GLU MET LEU
SEQRES 6 D 194 LYS LEU ALA ILE GLN SER ASN PRO SER PHE LYS LEU GLU
SEQRES 7 D 194 LEU VAL GLU MET GLU ARG GLU GLY PRO SER TYR THR PHE
SEQRES 8 D 194 ASP THR VAL SER LEU LEU LYS GLN ARG TYR PRO ASN ASP
SEQRES 9 D 194 GLN LEU PHE PHE ILE ILE GLY ALA ASP MET ILE GLU TYR
SEQRES 10 D 194 LEU PRO LYS TRP TYR LYS LEU ASP GLU LEU LEU ASN LEU
SEQRES 11 D 194 ILE GLN PHE ILE GLY VAL LYS ARG PRO GLY PHE HIS VAL
SEQRES 12 D 194 GLU THR PRO TYR PRO LEU LEU PHE ALA ASP VAL PRO GLU
SEQRES 13 D 194 PHE GLU VAL SER SER THR MET ILE ARG GLU ARG PHE LYS
SEQRES 14 D 194 SER LYS LYS PRO THR ASP TYR LEU ILE PRO ASP LYS VAL
SEQRES 15 D 194 LYS LYS TYR VAL GLU GLU ASN GLY LEU TYR GLU SER
FORMUL 5 HOH *139(H2 O)
HELIX 1 1 HIS A 15 ALA A 29 1 15
HELIX 2 2 ASP A 52 GLN A 65 1 14
HELIX 3 3 LEU A 74 GLU A 78 5 5
HELIX 4 4 TYR A 84 TYR A 96 1 13
HELIX 5 5 TRP A 116 ILE A 126 1 11
HELIX 6 6 SER A 155 LYS A 166 1 12
HELIX 7 7 PRO A 174 ASN A 184 1 11
HELIX 8 8 HIS B 15 ALA B 29 1 15
HELIX 9 9 ASP B 52 GLN B 65 1 14
HELIX 10 10 LEU B 74 GLU B 78 5 5
HELIX 11 11 ASP B 87 TYR B 96 1 10
HELIX 12 12 SER B 155 LYS B 166 1 12
HELIX 13 13 PRO B 174 ASN B 184 1 11
HELIX 14 14 HIS C 15 ALA C 29 1 15
HELIX 15 15 ASP C 52 GLN C 65 1 14
HELIX 16 16 LEU C 74 GLU C 78 5 5
HELIX 17 17 TYR C 84 TYR C 96 1 13
HELIX 18 18 TRP C 116 ILE C 126 1 11
HELIX 19 19 SER C 155 SER C 165 1 11
HELIX 20 20 PRO C 174 ASN C 184 1 11
HELIX 21 21 HIS D 15 ALA D 29 1 15
HELIX 22 22 ASP D 52 GLN D 65 1 14
HELIX 23 23 LEU D 74 GLU D 78 5 5
HELIX 24 24 ASP D 87 TYR D 96 1 10
HELIX 25 25 SER D 155 SER D 165 1 11
HELIX 26 26 PRO D 174 ASN D 184 1 11
SHEET 1 A 6 PHE A 70 LEU A 72 0
SHEET 2 A 6 GLU A 33 PRO A 38 1 N PHE A 36 O LYS A 71
SHEET 3 A 6 LYS A 3 GLY A 9 1 N PHE A 7 O TRP A 35
SHEET 4 A 6 GLN A 100 GLY A 106 1 O PHE A 102 N ILE A 6
SHEET 5 A 6 GLN A 127 LYS A 132 1 O ILE A 129 N PHE A 103
SHEET 6 A 6 LEU A 145 ASP A 148 1 O LEU A 145 N GLY A 130
SHEET 1 B 6 PHE B 70 LEU B 72 0
SHEET 2 B 6 GLU B 33 PRO B 38 1 N PHE B 36 O LYS B 71
SHEET 3 B 6 LYS B 3 GLY B 9 1 N GLY B 5 O TRP B 35
SHEET 4 B 6 GLN B 100 GLY B 106 1 O PHE B 102 N ILE B 4
SHEET 5 B 6 GLN B 127 LYS B 132 1 O GLN B 127 N PHE B 103
SHEET 6 B 6 LEU B 145 ASP B 148 1 O ALA B 147 N GLY B 130
SHEET 1 C 6 PHE C 70 LEU C 72 0
SHEET 2 C 6 GLU C 33 PRO C 38 1 N PHE C 36 O LYS C 71
SHEET 3 C 6 LYS C 3 GLY C 9 1 N PHE C 7 O TRP C 35
SHEET 4 C 6 GLN C 100 GLY C 106 1 O PHE C 102 N ILE C 6
SHEET 5 C 6 GLN C 127 LYS C 132 1 O VAL C 131 N ILE C 105
SHEET 6 C 6 LEU C 145 ASP C 148 1 O LEU C 145 N GLY C 130
SHEET 1 D 6 PHE D 70 LEU D 72 0
SHEET 2 D 6 GLU D 33 PRO D 38 1 N PHE D 36 O LYS D 71
SHEET 3 D 6 LYS D 3 GLY D 9 1 N GLY D 5 O TRP D 35
SHEET 4 D 6 GLN D 100 GLY D 106 1 O PHE D 102 N ILE D 4
SHEET 5 D 6 ILE D 126 LYS D 132 1 O GLN D 127 N PHE D 103
SHEET 6 D 6 LEU D 145 ASP D 148 1 O ALA D 147 N GLY D 130
CISPEP 1 ASP A 12 PRO A 13 0 -0.04
CISPEP 2 ASP B 12 PRO B 13 0 -0.06
CISPEP 3 ASP C 12 PRO C 13 0 0.62
CISPEP 4 ASP D 12 PRO D 13 0 0.20
CRYST1 43.977 126.103 70.579 90.00 92.73 90.00 P 1 21 1 8
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 0.022739 0.000000 0.001084 0.00000
SCALE2 0.000000 0.007930 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014185 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
