HEADER TRANSFERASE 07-NOV-05 2EX0
TITLE CRYSTAL STRUCTURE OF MULTIFUNCTIONAL SIALYLTRANSFERASE FROM
TITLE 2 PASTEURELLA MULTOCIDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A2,3-SIALYLTRANSFERASE, A2,6-SIALYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.99.4, 2.4.99.6, 2.4.99.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THE PROTEIN HAS FOUR ENZYMATIC ACTIVITIES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PASTEURELLA MULTOCIDA;
SOURCE 3 ORGANISM_TAXID: 747;
SOURCE 4 STRAIN: PM70;
SOURCE 5 GENE: PM0188;
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: PET23A(+)
KEYWDS TWO ROSSMAN FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.NI,M.SUN,X.CHEN,A.J.FISHER
REVDAT 3 14-FEB-24 2EX0 1 REMARK
REVDAT 2 24-FEB-09 2EX0 1 VERSN
REVDAT 1 28-FEB-06 2EX0 0
JRNL AUTH L.NI,M.SUN,H.YU,H.CHOKHAWALA,X.CHEN,A.J.FISHER
JRNL TITL CYTIDINE 5'-MONOPHOSPHATE (CMP)-INDUCED STRUCTURAL CHANGES
JRNL TITL 2 IN A MULTIFUNCTIONAL SIALYLTRANSFERASE FROM PASTEURELLA
JRNL TITL 3 MULTOCIDA
JRNL REF BIOCHEMISTRY V. 45 2139 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16475803
JRNL DOI 10.1021/BI0524013
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1183839.600
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 86251
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) : 0.193
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4349
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12404
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 646
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6371
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 841
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 2.87000
REMARK 3 B33 (A**2) : -2.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.50000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.840
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.950 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 47.85
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 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035196.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MAR325
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 62.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.42300
REMARK 200 R SYM FOR SHELL (I) : 0.30800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.216 MM PROTEIN, 26% PEG3350, 0.1M
REMARK 280 NACL, 0.4% TRITON-X-100, 0.1M HEPES, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 30.64050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 417
REMARK 465 HIS A 418
REMARK 465 HIS A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 GLY B 415
REMARK 465 LEU B 416
REMARK 465 GLU B 417
REMARK 465 HIS B 418
REMARK 465 HIS B 419
REMARK 465 HIS B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
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 GLU A 51 CG CD OE1 OE2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 ARG A 313 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 GLU B 209 CG CD OE1 OE2
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 LYS B 326 CG CD CE NZ
REMARK 470 ASN B 327 CG OD1 ND2
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 ASP A 33 125.07 -172.89
REMARK 500 ALA A 35 -142.20 -98.92
REMARK 500 SER A 36 -52.80 -121.23
REMARK 500 ASN A 154 -14.78 91.70
REMARK 500 LYS A 178 100.11 -170.03
REMARK 500 ALA A 219 -119.97 46.03
REMARK 500 THR A 268 -96.71 -99.21
REMARK 500 ASN A 327 75.48 37.42
REMARK 500 PRO A 332 119.18 -31.06
REMARK 500 ALA A 333 -14.67 -48.98
REMARK 500 SER A 367 -88.64 -94.04
REMARK 500 ASP B 33 125.16 -171.49
REMARK 500 ALA B 35 -143.73 -96.65
REMARK 500 SER B 36 -53.40 -120.11
REMARK 500 LYS B 176 89.32 -69.67
REMARK 500 ALA B 219 -120.78 45.59
REMARK 500 THR B 268 -97.74 -98.60
REMARK 500 GLU B 271 76.88 -65.75
REMARK 500 THR B 274 146.94 -177.65
REMARK 500 SER B 367 -87.66 -94.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EX1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTIFUNCTIONAL SIALYLTRANSFERASE FROM
REMARK 900 PASTEURELLA MULTOCIDA BINDING WITH CMP
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE
REMARK 999 REFERENCE AVAILABLE FOR THIS PROTEIN
DBREF 2EX0 A 26 412 UNP Q15KI8 Q15KI8_PASMU 26 412
DBREF 2EX0 B 26 412 UNP Q15KI8 Q15KI8_PASMU 26 412
SEQRES 1 A 399 MET LYS THR ILE THR LEU TYR LEU ASP PRO ALA SER LEU
SEQRES 2 A 399 PRO ALA LEU ASN GLN LEU MET ASP PHE THR GLN ASN ASN
SEQRES 3 A 399 GLU ASP LYS THR HIS PRO ARG ILE PHE GLY LEU SER ARG
SEQRES 4 A 399 PHE LYS ILE PRO ASP ASN ILE ILE THR GLN TYR GLN ASN
SEQRES 5 A 399 ILE HIS PHE VAL GLU LEU LYS ASP ASN ARG PRO THR GLU
SEQRES 6 A 399 ALA LEU PHE THR ILE LEU ASP GLN TYR PRO GLY ASN ILE
SEQRES 7 A 399 GLU LEU ASN ILE HIS LEU ASN ILE ALA HIS SER VAL GLN
SEQRES 8 A 399 LEU ILE ARG PRO ILE LEU ALA TYR ARG PHE LYS HIS LEU
SEQRES 9 A 399 ASP ARG VAL SER ILE GLN GLN LEU ASN LEU TYR ASP ASP
SEQRES 10 A 399 GLY SER MET GLU TYR VAL ASP LEU GLU LYS GLU GLU ASN
SEQRES 11 A 399 LYS ASP ILE SER ALA GLU ILE LYS GLN ALA GLU LYS GLN
SEQRES 12 A 399 LEU SER HIS TYR LEU LEU THR GLY LYS ILE LYS PHE ASP
SEQRES 13 A 399 ASN PRO THR ILE ALA ARG TYR VAL TRP GLN SER ALA PHE
SEQRES 14 A 399 PRO VAL LYS TYR HIS PHE LEU SER THR ASP TYR PHE GLU
SEQRES 15 A 399 LYS ALA GLU PHE LEU GLN PRO LEU LYS GLU TYR LEU ALA
SEQRES 16 A 399 GLU ASN TYR GLN LYS MET ASP TRP THR ALA TYR GLN GLN
SEQRES 17 A 399 LEU THR PRO GLU GLN GLN ALA PHE TYR LEU THR LEU VAL
SEQRES 18 A 399 GLY PHE ASN ASP GLU VAL LYS GLN SER LEU GLU VAL GLN
SEQRES 19 A 399 GLN ALA LYS PHE ILE PHE THR GLY THR THR THR TRP GLU
SEQRES 20 A 399 GLY ASN THR ASP VAL ARG GLU TYR TYR ALA GLN GLN GLN
SEQRES 21 A 399 LEU ASN LEU LEU ASN HIS PHE THR GLN ALA GLU GLY ASP
SEQRES 22 A 399 LEU PHE ILE GLY ASP HIS TYR LYS ILE TYR PHE LYS GLY
SEQRES 23 A 399 HIS PRO ARG GLY GLY GLU ILE ASN ASP TYR ILE LEU ASN
SEQRES 24 A 399 ASN ALA LYS ASN ILE THR ASN ILE PRO ALA ASN ILE SER
SEQRES 25 A 399 PHE GLU VAL LEU MET MET THR GLY LEU LEU PRO ASP LYS
SEQRES 26 A 399 VAL GLY GLY VAL ALA SER SER LEU TYR PHE SER LEU PRO
SEQRES 27 A 399 LYS GLU LYS ILE SER HIS ILE ILE PHE THR SER ASN LYS
SEQRES 28 A 399 GLN VAL LYS SER LYS GLU ASP ALA LEU ASN ASN PRO TYR
SEQRES 29 A 399 VAL LYS VAL MET ARG ARG LEU GLY ILE ILE ASP GLU SER
SEQRES 30 A 399 GLN VAL ILE PHE TRP ASP SER LEU LYS GLN LEU GLY GLY
SEQRES 31 A 399 GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 399 MET LYS THR ILE THR LEU TYR LEU ASP PRO ALA SER LEU
SEQRES 2 B 399 PRO ALA LEU ASN GLN LEU MET ASP PHE THR GLN ASN ASN
SEQRES 3 B 399 GLU ASP LYS THR HIS PRO ARG ILE PHE GLY LEU SER ARG
SEQRES 4 B 399 PHE LYS ILE PRO ASP ASN ILE ILE THR GLN TYR GLN ASN
SEQRES 5 B 399 ILE HIS PHE VAL GLU LEU LYS ASP ASN ARG PRO THR GLU
SEQRES 6 B 399 ALA LEU PHE THR ILE LEU ASP GLN TYR PRO GLY ASN ILE
SEQRES 7 B 399 GLU LEU ASN ILE HIS LEU ASN ILE ALA HIS SER VAL GLN
SEQRES 8 B 399 LEU ILE ARG PRO ILE LEU ALA TYR ARG PHE LYS HIS LEU
SEQRES 9 B 399 ASP ARG VAL SER ILE GLN GLN LEU ASN LEU TYR ASP ASP
SEQRES 10 B 399 GLY SER MET GLU TYR VAL ASP LEU GLU LYS GLU GLU ASN
SEQRES 11 B 399 LYS ASP ILE SER ALA GLU ILE LYS GLN ALA GLU LYS GLN
SEQRES 12 B 399 LEU SER HIS TYR LEU LEU THR GLY LYS ILE LYS PHE ASP
SEQRES 13 B 399 ASN PRO THR ILE ALA ARG TYR VAL TRP GLN SER ALA PHE
SEQRES 14 B 399 PRO VAL LYS TYR HIS PHE LEU SER THR ASP TYR PHE GLU
SEQRES 15 B 399 LYS ALA GLU PHE LEU GLN PRO LEU LYS GLU TYR LEU ALA
SEQRES 16 B 399 GLU ASN TYR GLN LYS MET ASP TRP THR ALA TYR GLN GLN
SEQRES 17 B 399 LEU THR PRO GLU GLN GLN ALA PHE TYR LEU THR LEU VAL
SEQRES 18 B 399 GLY PHE ASN ASP GLU VAL LYS GLN SER LEU GLU VAL GLN
SEQRES 19 B 399 GLN ALA LYS PHE ILE PHE THR GLY THR THR THR TRP GLU
SEQRES 20 B 399 GLY ASN THR ASP VAL ARG GLU TYR TYR ALA GLN GLN GLN
SEQRES 21 B 399 LEU ASN LEU LEU ASN HIS PHE THR GLN ALA GLU GLY ASP
SEQRES 22 B 399 LEU PHE ILE GLY ASP HIS TYR LYS ILE TYR PHE LYS GLY
SEQRES 23 B 399 HIS PRO ARG GLY GLY GLU ILE ASN ASP TYR ILE LEU ASN
SEQRES 24 B 399 ASN ALA LYS ASN ILE THR ASN ILE PRO ALA ASN ILE SER
SEQRES 25 B 399 PHE GLU VAL LEU MET MET THR GLY LEU LEU PRO ASP LYS
SEQRES 26 B 399 VAL GLY GLY VAL ALA SER SER LEU TYR PHE SER LEU PRO
SEQRES 27 B 399 LYS GLU LYS ILE SER HIS ILE ILE PHE THR SER ASN LYS
SEQRES 28 B 399 GLN VAL LYS SER LYS GLU ASP ALA LEU ASN ASN PRO TYR
SEQRES 29 B 399 VAL LYS VAL MET ARG ARG LEU GLY ILE ILE ASP GLU SER
SEQRES 30 B 399 GLN VAL ILE PHE TRP ASP SER LEU LYS GLN LEU GLY GLY
SEQRES 31 B 399 GLY LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *841(H2 O)
HELIX 1 1 SER A 36 ASN A 49 1 14
HELIX 2 2 PRO A 67 THR A 72 1 6
HELIX 3 3 GLU A 89 ASP A 96 1 8
HELIX 4 4 HIS A 112 HIS A 127 1 16
HELIX 5 5 GLY A 142 LYS A 151 1 10
HELIX 6 6 ASP A 156 GLY A 175 1 20
HELIX 7 7 ASN A 181 ARG A 186 1 6
HELIX 8 8 TYR A 187 ALA A 192 5 6
HELIX 9 9 SER A 201 ALA A 208 1 8
HELIX 10 10 LEU A 211 ALA A 219 1 9
HELIX 11 11 THR A 228 LEU A 233 1 6
HELIX 12 12 THR A 234 GLY A 246 1 13
HELIX 13 13 ASN A 248 LEU A 255 1 8
HELIX 14 14 VAL A 276 GLN A 293 1 18
HELIX 15 15 GLY A 315 ALA A 325 1 11
HELIX 16 16 SER A 336 THR A 343 1 8
HELIX 17 17 SER A 355 LEU A 361 5 7
HELIX 18 18 PRO A 362 GLU A 364 5 3
HELIX 19 19 SER A 379 ASN A 385 1 7
HELIX 20 20 ASN A 386 LEU A 395 1 10
HELIX 21 21 ASP A 399 SER A 401 5 3
HELIX 22 22 ASP A 407 LEU A 409 5 3
HELIX 23 23 SER B 36 ASN B 49 1 14
HELIX 24 24 PRO B 67 THR B 72 1 6
HELIX 25 25 GLU B 89 ASP B 96 1 8
HELIX 26 26 HIS B 112 HIS B 127 1 16
HELIX 27 27 GLY B 142 LYS B 151 1 10
HELIX 28 28 ASP B 156 LEU B 172 1 17
HELIX 29 29 ASN B 181 ARG B 186 1 6
HELIX 30 30 TYR B 187 ALA B 192 5 6
HELIX 31 31 SER B 201 ALA B 208 1 8
HELIX 32 32 LEU B 211 ALA B 219 1 9
HELIX 33 33 THR B 228 LEU B 233 5 6
HELIX 34 34 THR B 234 VAL B 245 1 12
HELIX 35 35 ASN B 248 LEU B 255 1 8
HELIX 36 36 VAL B 276 GLN B 293 1 18
HELIX 37 37 GLY B 315 ASN B 324 1 10
HELIX 38 38 SER B 336 THR B 343 1 8
HELIX 39 39 SER B 355 LEU B 361 5 7
HELIX 40 40 PRO B 362 GLU B 364 5 3
HELIX 41 41 SER B 379 ASN B 385 1 7
HELIX 42 42 ASN B 386 LEU B 395 1 10
HELIX 43 43 ASP B 399 SER B 401 5 3
HELIX 44 44 ASP B 407 LEU B 409 5 3
SHEET 1 A 7 ILE A 77 PHE A 79 0
SHEET 2 A 7 ARG A 57 LEU A 61 1 N PHE A 59 O HIS A 78
SHEET 3 A 7 LYS A 26 ASP A 33 1 N TYR A 31 O GLY A 60
SHEET 4 A 7 ILE A 102 ASN A 109 1 O ASN A 105 N ILE A 28
SHEET 5 A 7 VAL A 131 TYR A 139 1 O ASN A 137 N LEU A 108
SHEET 6 A 7 VAL A 195 PHE A 199 1 O LYS A 196 N LEU A 138
SHEET 7 A 7 TYR A 222 LYS A 224 1 O GLN A 223 N PHE A 199
SHEET 1 B 2 LEU A 82 LYS A 83 0
SHEET 2 B 2 ARG A 86 PRO A 87 -1 O ARG A 86 N LYS A 83
SHEET 1 C 6 THR A 329 ASN A 330 0
SHEET 2 C 6 TYR A 304 LYS A 309 1 N PHE A 308 O THR A 329
SHEET 3 C 6 ALA A 260 THR A 265 1 N PHE A 264 O LYS A 309
SHEET 4 C 6 LYS A 349 VAL A 353 1 O GLY A 351 N THR A 265
SHEET 5 C 6 ILE A 366 PHE A 371 1 O ILE A 370 N GLY A 352
SHEET 6 C 6 VAL A 403 PHE A 405 1 O ILE A 404 N PHE A 371
SHEET 1 D 7 ILE B 77 PHE B 79 0
SHEET 2 D 7 ARG B 57 LEU B 61 1 N PHE B 59 O HIS B 78
SHEET 3 D 7 LYS B 26 ASP B 33 1 N TYR B 31 O GLY B 60
SHEET 4 D 7 ILE B 102 ASN B 109 1 O ASN B 105 N ILE B 28
SHEET 5 D 7 VAL B 131 TYR B 139 1 O ASN B 137 N LEU B 108
SHEET 6 D 7 VAL B 195 PHE B 199 1 O LYS B 196 N LEU B 138
SHEET 7 D 7 TYR B 222 LYS B 224 1 O GLN B 223 N PHE B 199
SHEET 1 E 2 LEU B 82 LYS B 83 0
SHEET 2 E 2 ARG B 86 PRO B 87 -1 O ARG B 86 N LYS B 83
SHEET 1 F 6 THR B 329 ASN B 330 0
SHEET 2 F 6 LYS B 305 LYS B 309 1 N PHE B 308 O THR B 329
SHEET 3 F 6 LYS B 261 THR B 265 1 N PHE B 264 O LYS B 309
SHEET 4 F 6 LYS B 349 VAL B 353 1 O LYS B 349 N ILE B 263
SHEET 5 F 6 ILE B 366 PHE B 371 1 O ILE B 370 N GLY B 352
SHEET 6 F 6 VAL B 403 PHE B 405 1 O ILE B 404 N PHE B 371
CRYST1 63.718 61.281 96.649 90.00 101.56 90.00 P 1 21 1 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 0.015694 0.000000 0.003209 0.00000
SCALE2 0.000000 0.016318 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010561 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
