HEADER TRANSFERASE 07-FEB-06 2FY2
TITLE STRUCTURES OF LIGAND BOUND HUMAN CHOLINE ACETYLTRANSFERASE PROVIDE
TITLE 2 INSIGHT INTO REGULATION OF ACETYLCHOLINE SYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 120-733;
COMPND 5 SYNONYM: CHOACTASE, CHOLINE ACETYLASE, CHAT;
COMPND 6 EC: 2.3.1.6;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CHAT;
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: PPROEXHTA
KEYWDS TWO DOMAIN, ALPHA-BETA PROTEIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.KIM,R.J.RYLETT,B.H.SHILTON
REVDAT 5 30-AUG-23 2FY2 1 REMARK
REVDAT 4 20-OCT-21 2FY2 1 SEQADV
REVDAT 3 18-OCT-17 2FY2 1 REMARK
REVDAT 2 24-FEB-09 2FY2 1 VERSN
REVDAT 1 12-DEC-06 2FY2 0
JRNL AUTH A.R.KIM,R.J.RYLETT,B.H.SHILTON
JRNL TITL SUBSTRATE BINDING AND CATALYTIC MECHANISM OF HUMAN CHOLINE
JRNL TITL 2 ACETYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 45 14621 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 17144655
JRNL DOI 10.1021/BI061536L
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.91
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) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 32854
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) : 0.195
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3289
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.35
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3545
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 390
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 : 4583
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 544
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07000
REMARK 3 B22 (A**2) : 2.67000
REMARK 3 B33 (A**2) : -3.73000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.92
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.146
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 50.93
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 2FY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036446.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRADED MULTILAYER (OSMIC)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32962
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.09300
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1Q6X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-13% PEG 3350, 0.1M TRIS-HCL, PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 27.37000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.84500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.84500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.37000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.87500
REMARK 290 SMTRY3 4 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: MONOMERIC
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 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 ALA A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 SER A 7
REMARK 465 ASP A 139
REMARK 465 CYS A 140
REMARK 465 ALA A 141
REMARK 465 LYS A 142
REMARK 465 GLY A 143
REMARK 465 GLN A 144
REMARK 465 LEU A 145
REMARK 465 SER A 146
REMARK 465 ASN A 176
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 ILE A 179
REMARK 465 PRO A 608
REMARK 465 PRO A 609
REMARK 465 THR A 610
REMARK 465 GLU A 611
REMARK 465 SER A 612
REMARK 465 LYS A 613
REMARK 465 PRO A 614
REMARK 465 LEU A 615
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 TYR A 85 -62.31 -128.35
REMARK 500 VAL A 94 -52.88 67.49
REMARK 500 SER A 96 -43.20 -131.15
REMARK 500 PRO A 137 105.51 -50.53
REMARK 500 PRO A 181 160.06 -49.80
REMARK 500 PHE A 203 11.06 50.49
REMARK 500 LEU A 206 129.30 -31.36
REMARK 500 CYS A 268 177.16 178.60
REMARK 500 LEU A 280 35.07 -78.29
REMARK 500 LYS A 297 -111.06 -104.54
REMARK 500 GLU A 446 18.56 54.29
REMARK 500 ARG A 448 -96.00 -103.53
REMARK 500 SER A 540 143.99 -175.72
REMARK 500 LEU A 606 -75.62 -79.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FY3 RELATED DB: PDB
REMARK 900 RELATED ID: 2FY4 RELATED DB: PDB
REMARK 900 RELATED ID: 2FY5 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE ORIGINAL SEQUENCE SSRKLIRADSVSE (RESIDUES 464-476
REMARK 999 IN SWS ENTRY CLAT_HUMAN) WAS MUTATED TO THE SEQUENCE
REMARK 999 PELVRSPMVP (RESIDUES 346-357 IN THE COORDINATES) IN
REMARK 999 ORDER TO MAKE THE PROTEIN CRYSTALLIZE. THE OTHER
REMARK 999 MUTATIONS MENTIONED IN SEQADV WERE MADE FOR THE SAME
REMARK 999 PURPOSE.
DBREF 2FY2 A 2 615 UNP P28329 CLAT_HUMAN 120 733
SEQADV 2FY2 ALA A 1 UNP P28329 CLONING ARTIFACT
SEQADV 2FY2 ALA A 225 UNP P28329 GLU 343 ENGINEERED MUTATION
SEQADV 2FY2 ALA A 226 UNP P28329 ASP 344 ENGINEERED MUTATION
SEQADV 2FY2 ALA A 227 UNP P28329 GLU 345 ENGINEERED MUTATION
SEQADV 2FY2 A UNP P28329 SER 464 SEE REMARK 999
SEQADV 2FY2 A UNP P28329 SER 465 SEE REMARK 999
SEQADV 2FY2 PRO A 346 UNP P28329 ARG 466 SEE REMARK 999
SEQADV 2FY2 GLU A 349 UNP P28329 LYS 467 SEE REMARK 999
SEQADV 2FY2 VAL A 351 UNP P28329 ILE 469 SEE REMARK 999
SEQADV 2FY2 SER A 353 UNP P28329 ALA 471 SEE REMARK 999
SEQADV 2FY2 PRO A 354 UNP P28329 ASP 472 SEE REMARK 999
SEQADV 2FY2 MET A 355 UNP P28329 SER 473 SEE REMARK 999
SEQADV 2FY2 A UNP P28329 SER 475 SEE REMARK 999
SEQADV 2FY2 PRO A 357 UNP P28329 GLU 476 SEE REMARK 999
SEQADV 2FY2 ALA A 518 UNP P28329 LYS 636 ENGINEERED MUTATION
SEQADV 2FY2 ALA A 519 UNP P28329 GLU 637 ENGINEERED MUTATION
SEQADV 2FY2 ALA A 582 UNP P28329 LYS 700 ENGINEERED MUTATION
SEQADV 2FY2 ALA A 583 UNP P28329 GLU 701 ENGINEERED MUTATION
SEQRES 1 A 612 ALA ALA ALA LYS THR PRO SER SER GLU GLU SER GLY LEU
SEQRES 2 A 612 PRO LYS LEU PRO VAL PRO PRO LEU GLN GLN THR LEU ALA
SEQRES 3 A 612 THR TYR LEU GLN CYS MET ARG HIS LEU VAL SER GLU GLU
SEQRES 4 A 612 GLN PHE ARG LYS SER GLN ALA ILE VAL GLN GLN PHE GLY
SEQRES 5 A 612 ALA PRO GLY GLY LEU GLY GLU THR LEU GLN GLN LYS LEU
SEQRES 6 A 612 LEU GLU ARG GLN GLU LYS THR ALA ASN TRP VAL SER GLU
SEQRES 7 A 612 TYR TRP LEU ASN ASP MET TYR LEU ASN ASN ARG LEU ALA
SEQRES 8 A 612 LEU PRO VAL ASN SER SER PRO ALA VAL ILE PHE ALA ARG
SEQRES 9 A 612 GLN HIS PHE PRO GLY THR ASP ASP GLN LEU ARG PHE ALA
SEQRES 10 A 612 ALA SER LEU ILE SER GLY VAL LEU SER TYR LYS ALA LEU
SEQRES 11 A 612 LEU ASP SER HIS SER ILE PRO THR ASP CYS ALA LYS GLY
SEQRES 12 A 612 GLN LEU SER GLY GLN PRO LEU CYS MET LYS GLN TYR TYR
SEQRES 13 A 612 GLY LEU PHE SER SER TYR ARG LEU PRO GLY HIS THR GLN
SEQRES 14 A 612 ASP THR LEU VAL ALA GLN ASN SER SER ILE MET PRO GLU
SEQRES 15 A 612 PRO GLU HIS VAL ILE VAL ALA CYS CYS ASN GLN PHE PHE
SEQRES 16 A 612 VAL LEU ASP VAL VAL ILE ASN PHE ARG ARG LEU SER GLU
SEQRES 17 A 612 GLY ASP LEU PHE THR GLN LEU ARG LYS ILE VAL LYS MET
SEQRES 18 A 612 ALA SER ASN ALA ALA ALA ARG LEU PRO PRO ILE GLY LEU
SEQRES 19 A 612 LEU THR SER ASP GLY ARG SER GLU TRP ALA GLU ALA ARG
SEQRES 20 A 612 THR VAL LEU VAL LYS ASP SER THR ASN ARG ASP SER LEU
SEQRES 21 A 612 ASP MET ILE GLU ARG CYS ILE CYS LEU VAL CYS LEU ASP
SEQRES 22 A 612 ALA PRO GLY GLY VAL GLU LEU SER ASP THR HIS ARG ALA
SEQRES 23 A 612 LEU GLN LEU LEU HIS GLY GLY GLY TYR SER LYS ASN GLY
SEQRES 24 A 612 ALA ASN ARG TRP TYR ASP LYS SER LEU GLN PHE VAL VAL
SEQRES 25 A 612 GLY ARG ASP GLY THR CYS GLY VAL VAL CYS GLU HIS SER
SEQRES 26 A 612 PRO PHE ASP GLY ILE VAL LEU VAL GLN CYS THR GLU HIS
SEQRES 27 A 612 LEU LEU LYS HIS MET THR GLN PRO GLU LEU VAL ARG SER
SEQRES 28 A 612 PRO MET VAL PRO LEU PRO ALA PRO ARG ARG LEU ARG TRP
SEQRES 29 A 612 LYS CYS SER PRO GLU ILE GLN GLY HIS LEU ALA SER SER
SEQRES 30 A 612 ALA GLU LYS LEU GLN ARG ILE VAL LYS ASN LEU ASP PHE
SEQRES 31 A 612 ILE VAL TYR LYS PHE ASP ASN TYR GLY LYS THR PHE ILE
SEQRES 32 A 612 LYS LYS GLN LYS CYS SER PRO ASP ALA PHE ILE GLN VAL
SEQRES 33 A 612 ALA LEU GLN LEU ALA PHE TYR ARG LEU HIS ARG ARG LEU
SEQRES 34 A 612 VAL PRO THR TYR GLU SER ALA SER ILE ARG ARG PHE GLN
SEQRES 35 A 612 GLU GLY ARG VAL ASP ASN ILE ARG SER ALA THR PRO GLU
SEQRES 36 A 612 ALA LEU ALA PHE VAL ARG ALA VAL THR ASP HIS LYS ALA
SEQRES 37 A 612 ALA VAL PRO ALA SER GLU LYS LEU LEU LEU LEU LYS ASP
SEQRES 38 A 612 ALA ILE ARG ALA GLN THR ALA TYR THR VAL MET ALA ILE
SEQRES 39 A 612 THR GLY MET ALA ILE ASP ASN HIS LEU LEU ALA LEU ARG
SEQRES 40 A 612 GLU LEU ALA ARG ALA MET CYS ALA ALA LEU PRO GLU MET
SEQRES 41 A 612 PHE MET ASP GLU THR TYR LEU MET SER ASN ARG PHE VAL
SEQRES 42 A 612 LEU SER THR SER GLN VAL PRO THR THR THR GLU MET PHE
SEQRES 43 A 612 CYS CYS TYR GLY PRO VAL VAL PRO ASN GLY TYR GLY ALA
SEQRES 44 A 612 CYS TYR ASN PRO GLN PRO GLU THR ILE LEU PHE CYS ILE
SEQRES 45 A 612 SER SER PHE HIS SER CYS ALA ALA THR SER SER SER LYS
SEQRES 46 A 612 PHE ALA LYS ALA VAL GLU GLU SER LEU ILE ASP MET ARG
SEQRES 47 A 612 ASP LEU CYS SER LEU LEU PRO PRO THR GLU SER LYS PRO
SEQRES 48 A 612 LEU
FORMUL 2 HOH *544(H2 O)
HELIX 1 1 PRO A 20 ARG A 33 1 14
HELIX 2 2 HIS A 34 VAL A 36 5 3
HELIX 3 3 SER A 37 GLY A 52 1 16
HELIX 4 4 GLY A 56 THR A 72 1 17
HELIX 5 5 VAL A 76 TYR A 85 1 10
HELIX 6 6 ALA A 91 SER A 96 1 6
HELIX 7 7 GLY A 109 SER A 133 1 25
HELIX 8 8 MET A 152 LEU A 158 5 7
HELIX 9 9 SER A 207 SER A 223 1 17
HELIX 10 10 ASN A 224 ARG A 228 5 5
HELIX 11 11 PRO A 231 ASP A 238 5 8
HELIX 12 12 GLY A 239 LYS A 252 1 14
HELIX 13 13 ASP A 253 ARG A 265 1 13
HELIX 14 14 SER A 281 GLY A 292 1 12
HELIX 15 15 ASP A 328 THR A 344 1 17
HELIX 16 16 SER A 370 ASN A 390 1 21
HELIX 17 17 GLY A 402 LYS A 408 1 7
HELIX 18 18 SER A 412 ARG A 430 1 19
HELIX 19 19 THR A 456 ASP A 468 1 13
HELIX 20 20 HIS A 469 ALA A 472 5 4
HELIX 21 21 PRO A 474 THR A 498 1 25
HELIX 22 22 ILE A 502 CYS A 517 1 16
HELIX 23 23 PRO A 521 ASP A 526 1 6
HELIX 24 24 ASP A 526 ASN A 533 1 8
HELIX 25 25 SER A 585 SER A 605 1 21
SHEET 1 A 3 ARG A 204 ARG A 205 0
SHEET 2 A 3 GLN A 193 ILE A 201 -1 N ILE A 201 O ARG A 204
SHEET 3 A 3 ARG A 363 ARG A 364 -1 O ARG A 363 N VAL A 196
SHEET 1 B 8 ARG A 204 ARG A 205 0
SHEET 2 B 8 GLN A 193 ILE A 201 -1 N ILE A 201 O ARG A 204
SHEET 3 B 8 GLU A 184 CYS A 190 -1 N VAL A 188 O PHE A 195
SHEET 4 B 8 LEU A 269 LEU A 272 1 O LEU A 272 N ALA A 189
SHEET 5 B 8 LEU A 308 VAL A 312 1 O PHE A 310 N CYS A 271
SHEET 6 B 8 CYS A 318 CYS A 322 -1 O GLY A 319 N VAL A 311
SHEET 7 B 8 ALA A 99 ILE A 101 -1 N VAL A 100 O VAL A 320
SHEET 8 B 8 PHE A 549 CYS A 551 -1 O PHE A 549 N ILE A 101
SHEET 1 C 2 SER A 161 LEU A 164 0
SHEET 2 C 2 THR A 171 ALA A 174 -1 O VAL A 173 N TYR A 162
SHEET 1 D 6 LEU A 391 PHE A 398 0
SHEET 2 D 6 ILE A 571 PHE A 578 -1 O SER A 577 N ASP A 392
SHEET 3 D 6 TYR A 560 PRO A 566 -1 N CYS A 563 O CYS A 574
SHEET 4 D 6 LEU A 537 GLN A 541 1 N SER A 538 O ALA A 562
SHEET 5 D 6 THR A 435 SER A 440 1 N TYR A 436 O THR A 539
SHEET 6 D 6 VAL A 449 ASN A 451 -1 O ASP A 450 N ALA A 439
CISPEP 1 GLU A 182 PRO A 183 0 -1.51
CISPEP 2 VAL A 356 PRO A 357 0 -0.77
CRYST1 54.740 75.750 165.690 90.00 90.00 90.00 P 21 21 21 4
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 0.018268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006035 0.00000
(ATOM LINES ARE NOT SHOWN.)
END