HEADER SIGNALING PROTEIN,TRANSFERASE 23-DEC-05 2FH9
TITLE STRUCTURE AND DIMERIZATION OF THE KINASE DOMAIN FROM YEAST SNF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SNF1 KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBON CATABOLITE DEREPRESSING PROTEIN KINASE;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: SNF1, CAT1, CCR1, GLC2, PAS14;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET 1
KEYWDS KINASE DOMAIN; DIMER, SIGNALING PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.NAYAK
REVDAT 6 14-FEB-24 2FH9 1 REMARK
REVDAT 5 18-OCT-17 2FH9 1 REMARK
REVDAT 4 16-NOV-11 2FH9 1 HETATM
REVDAT 3 13-JUL-11 2FH9 1 VERSN
REVDAT 2 24-FEB-09 2FH9 1 VERSN
REVDAT 1 28-MAR-06 2FH9 0
JRNL AUTH V.NAYAK,K.ZHAO,A.WYCE,M.F.SCHWARTZ,W.S.LO,S.L.BERGER,
JRNL AUTH 2 R.MARMORSTEIN
JRNL TITL STRUCTURE AND DIMERIZATION OF THE KINASE DOMAIN FROM YEAST
JRNL TITL 2 SNF1, A MEMBER OF THE SNF1/AMPK PROTEIN FAMILY
JRNL REF STRUCTURE V. 14 477 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16531232
JRNL DOI 10.1016/J.STR.2005.12.008
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 8763
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) : 0.215
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 897
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2057
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.71800
REMARK 3 B22 (A**2) : -2.71800
REMARK 3 B33 (A**2) : 5.43600
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) : 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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.383
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : 37.86
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000035876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686, 0.9796, 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8763
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
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) : 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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE 2.02, RESOLVE 2.02
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.33850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.33850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.33850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.33850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.33850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.33850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.33850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.33850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 0.000000 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 61.62000
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 HOH A 344 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 354 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 357 LIES ON A SPECIAL POSITION.
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 VAL A 90
REMARK 465 LEU A 91
REMARK 465 ALA A 92
REMARK 465 LYS A 93
REMARK 465 SER A 94
REMARK 465 ASP A 95
REMARK 465 MET A 96
REMARK 465 GLN A 97
REMARK 465 LYS A 123
REMARK 465 SER A 124
REMARK 465 LYS A 125
REMARK 465 ASP A 126
REMARK 465 SER A 199
REMARK 465 ASN A 200
REMARK 465 ILE A 201
REMARK 465 MET A 202
REMARK 465 THR A 203
REMARK 465 ASP A 204
REMARK 465 GLY A 205
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR A 73 O HOH A 420 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 386 O HOH A 386 7555 1.88
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 ALA A 47 -164.90 -102.17
REMARK 500 ASP A 48 8.14 -65.14
REMARK 500 HIS A 51 129.97 40.84
REMARK 500 ILE A 52 104.56 -164.07
REMARK 500 ASN A 54 -12.24 94.02
REMARK 500 LYS A 59 109.25 176.40
REMARK 500 THR A 60 127.67 -34.23
REMARK 500 SER A 65 -27.94 38.51
REMARK 500 PHE A 66 -71.41 -118.83
REMARK 500 ASN A 87 -162.74 159.17
REMARK 500 LYS A 88 79.14 37.92
REMARK 500 ARG A 99 29.93 -67.26
REMARK 500 ASP A 120 139.10 178.17
REMARK 500 VAL A 131 92.59 55.44
REMARK 500 GLN A 145 -79.26 -50.50
REMARK 500 ARG A 146 108.49 -59.77
REMARK 500 ASP A 147 -82.00 -35.74
REMARK 500 HIS A 171 25.37 -77.59
REMARK 500 ARG A 176 -2.31 72.62
REMARK 500 ASP A 177 45.20 -143.27
REMARK 500 LEU A 189 30.43 72.27
REMARK 500 ASP A 253 122.16 172.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FH9 A 46 319 UNP P06782 SNF1_YEAST 46 319
SEQRES 1 A 274 LEU ALA ASP GLY ALA HIS ILE GLY ASN TYR GLN ILE VAL
SEQRES 2 A 274 LYS THR LEU GLY GLU GLY SER PHE GLY LYS VAL LYS LEU
SEQRES 3 A 274 ALA TYR HIS THR THR THR GLY GLN LYS VAL ALA LEU LYS
SEQRES 4 A 274 ILE ILE ASN LYS LYS VAL LEU ALA LYS SER ASP MET GLN
SEQRES 5 A 274 GLY ARG ILE GLU ARG GLU ILE SER TYR LEU ARG LEU LEU
SEQRES 6 A 274 ARG HIS PRO HIS ILE ILE LYS LEU TYR ASP VAL ILE LYS
SEQRES 7 A 274 SER LYS ASP GLU ILE ILE MET VAL ILE GLU TYR ALA GLY
SEQRES 8 A 274 ASN GLU LEU PHE ASP TYR ILE VAL GLN ARG ASP LYS MET
SEQRES 9 A 274 SER GLU GLN GLU ALA ARG ARG PHE PHE GLN GLN ILE ILE
SEQRES 10 A 274 SER ALA VAL GLU TYR CYS HIS ARG HIS LYS ILE VAL HIS
SEQRES 11 A 274 ARG ASP LEU LYS PRO GLU ASN LEU LEU LEU ASP GLU HIS
SEQRES 12 A 274 LEU ASN VAL LYS ILE ALA ASP PHE GLY LEU SER ASN ILE
SEQRES 13 A 274 MET THR ASP GLY ASN PHE LEU LYS THR SER CYS GLY SER
SEQRES 14 A 274 PRO ASN TYR ALA ALA PRO GLU VAL ILE SER GLY LYS LEU
SEQRES 15 A 274 TYR ALA GLY PRO GLU VAL ASP VAL TRP SER CYS GLY VAL
SEQRES 16 A 274 ILE LEU TYR VAL MET LEU CYS ARG ARG LEU PRO PHE ASP
SEQRES 17 A 274 ASP GLU SER ILE PRO VAL LEU PHE LYS ASN ILE SER ASN
SEQRES 18 A 274 GLY VAL TYR THR LEU PRO LYS PHE LEU SER PRO GLY ALA
SEQRES 19 A 274 ALA GLY LEU ILE LYS ARG MET LEU ILE VAL ASN PRO LEU
SEQRES 20 A 274 ASN ARG ILE SER ILE HIS GLU ILE MET GLN ASP ASP TRP
SEQRES 21 A 274 PHE LYS VAL ASP LEU PRO GLU TYR LEU LEU PRO PRO ASP
SEQRES 22 A 274 LEU
FORMUL 2 HOH *105(H2 O)
HELIX 1 1 ARG A 99 ARG A 108 1 10
HELIX 2 2 LEU A 139 ARG A 146 1 8
HELIX 3 3 SER A 150 HIS A 171 1 22
HELIX 4 4 LYS A 179 GLU A 181 5 3
HELIX 5 5 SER A 214 ALA A 218 5 5
HELIX 6 6 ALA A 219 SER A 224 1 6
HELIX 7 7 PRO A 231 ARG A 248 1 18
HELIX 8 8 SER A 256 ASN A 266 1 11
HELIX 9 9 SER A 276 LEU A 287 1 12
HELIX 10 10 SER A 296 ASP A 303 1 8
HELIX 11 11 ASP A 303 VAL A 308 1 6
HELIX 12 12 PRO A 311 LEU A 315 5 5
SHEET 1 A 4 TYR A 55 GLY A 64 0
SHEET 2 A 4 GLY A 67 HIS A 74 -1 O VAL A 69 N LEU A 61
SHEET 3 A 4 LYS A 80 ILE A 86 -1 O VAL A 81 N ALA A 72
SHEET 4 A 4 ILE A 128 ILE A 129 -1 O ILE A 128 N ILE A 86
SHEET 1 B 4 TYR A 55 GLY A 64 0
SHEET 2 B 4 GLY A 67 HIS A 74 -1 O VAL A 69 N LEU A 61
SHEET 3 B 4 LYS A 80 ILE A 86 -1 O VAL A 81 N ALA A 72
SHEET 4 B 4 ILE A 132 GLU A 133 -1 O ILE A 132 N ALA A 82
SHEET 1 C 3 ASN A 137 GLU A 138 0
SHEET 2 C 3 LEU A 183 LEU A 185 -1 O LEU A 185 N ASN A 137
SHEET 3 C 3 VAL A 191 ILE A 193 -1 O LYS A 192 N LEU A 184
CRYST1 108.677 108.677 61.620 90.00 90.00 90.00 P 4 21 2 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 0.009202 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016228 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
