HEADER HYDROLASE 12-MAR-04 1SNT
TITLE STRUCTURE OF THE HUMAN CYTOSOLIC SIALIDASE NEU2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA- NEURAMINIDASE 2;
COMPND 5 EC: 3.2.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS SIALIDASE, NEURAMINIDASE, GANGLIOSIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.G.CHAVAS,P.FUSI,C.TRINGALI,B.VENERANDO,G.TETTAMANTI,R.KATO,
AUTHOR 2 E.MONTI,S.WAKATSUKI
REVDAT 4 13-JUL-11 1SNT 1 VERSN
REVDAT 3 24-FEB-09 1SNT 1 VERSN
REVDAT 2 18-JAN-05 1SNT 1 JRNL
REVDAT 1 02-NOV-04 1SNT 0
JRNL AUTH L.M.G.CHAVAS,C.TRINGALI,P.FUSI,B.VENERANDO,G.TETTAMANTI,
JRNL AUTH 2 R.KATO,E.MONTI,S.WAKATSUKI
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN CYTOSOLIC SIALIDASE NEU2:
JRNL TITL 2 EVIDENCE FOR THE DYNAMIC NATURE OF SUBSTRATE RECOGNITION
JRNL REF J.BIOL.CHEM. V. 280 469 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15501818
JRNL DOI 10.1074/JBC.M411506200
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 51297
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) : 0.201
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2551
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 : 2768
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 377
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.47
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 : 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:
REMARK 3 ABOUT CD1/CD2 (LEU A 90) AND CG1/CG2 (VAL A 325),
REMARK 3 THERE ARE 3 POSSIBLE POSITIONS FOR THESE ATOMS.
REMARK 3 THERE ARE TWO DIFFERENT CONFORMATIONS FOR EACH ATOM.
REMARK 3 FOR CONVENIENCE, THE AUTHOR ASSIGNED AS A DOUBLE
REMARK 3 CONFORMATION ONLY ONE OF THE ATOMS.(CD2 OF LEU 90
REMARK 3 AND CG1 OF VAL 325)
REMARK 3 THUS THE OCCUPANCIES OF THE ALTERNATE CONFORMATIONS
REMARK 3 ARE GREATER THAN 1.00 AND THERE ARE CHIRALITY ERRORS
REMARK 3 AT THESE ATOMS.
REMARK 4
REMARK 4 1SNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-04.
REMARK 100 THE RCSB ID CODE IS RCSB021858.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9780
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51297
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1EUS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM POTASSIUM PHOSPHATE, SODIUM
REMARK 280 CHLORIDE, PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+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 1.000000 0.000000 0.000000 72.97000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.12925
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.45000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 72.97000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 42.12925
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 21.45000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 72.97000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 42.12925
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.45000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 84.25850
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 42.90000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 84.25850
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 42.90000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 84.25850
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 42.90000
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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 42
REMARK 465 SER A 43
REMARK 465 LYS A 44
REMARK 465 LYS A 45
REMARK 465 ASP A 46
REMARK 465 GLU A 47
REMARK 465 HIS A 48
REMARK 465 GLY A 107
REMARK 465 GLN A 108
REMARK 465 VAL A 109
REMARK 465 THR A 110
REMARK 465 GLU A 111
REMARK 465 GLN A 112
REMARK 465 GLN A 113
REMARK 465 GLN A 114
REMARK 465 LEU A 115
REMARK 465 GLN A 116
REMARK 465 THR A 117
REMARK 465 ARG A 118
REMARK 465 SER A 284
REMARK 465 GLY A 285
REMARK 465 PRO A 286
REMARK 465 GLY A 287
REMARK 465 LEU A 378
REMARK 465 PRO A 379
REMARK 465 GLN A 380
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 ILE A 22 69.39 60.93
REMARK 500 LEU A 184 3.78 -68.31
REMARK 500 PRO A 186 37.69 -75.90
REMARK 500 VAL A 212 -159.70 -94.75
REMARK 500 LEU A 217 -147.78 -119.00
REMARK 500 GLU A 218 117.14 -31.66
REMARK 500 LEU A 240 -163.97 -100.65
REMARK 500 ASP A 306 76.90 58.58
REMARK 500 ALA A 333 -122.50 -127.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 386 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH A 404 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 596 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 637 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A 654 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH A 656 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 678 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH A 716 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 731 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 732 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 749 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 750 DISTANCE = 5.40 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VCU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH SIALIC ACID
REMARK 900 RELATED ID: 1SO7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, SUGAR-INDUCED FORM
DBREF 1SNT A 1 380 UNP Q9Y3R4 NEUR2_HUMAN 1 380
SEQADV 1SNT GLY A -1 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 1SNT SER A 0 UNP Q9Y3R4 CLONING ARTIFACT
SEQRES 1 A 382 GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES 2 A 382 VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES 3 A 382 LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES 4 A 382 ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU
SEQRES 5 A 382 LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES 6 A 382 HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES 7 A 382 ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES 8 A 382 LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES 9 A 382 ILE ALA ILE PRO GLY GLN VAL THR GLU GLN GLN GLN LEU
SEQRES 10 A 382 GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES 11 A 382 SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES 12 A 382 LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES 13 A 382 SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES 14 A 382 ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES 15 A 382 TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES 16 A 382 ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES 17 A 382 ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES 18 A 382 GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES 19 A 382 THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES 20 A 382 ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES 21 A 382 GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES 22 A 382 CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES 23 A 382 GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES 24 A 382 PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES 25 A 382 LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES 26 A 382 PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES 27 A 382 LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES 28 A 382 PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES 29 A 382 VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES 30 A 382 GLU TYR LEU PRO GLN
FORMUL 2 HOH *377(H2 O)
HELIX 1 1 LEU A 142 GLY A 148 1 7
HELIX 2 2 PRO A 149 ARG A 152 5 4
HELIX 3 3 ALA A 317 TRP A 321 5 5
HELIX 4 4 LEU A 369 PHE A 373 1 5
HELIX 5 5 PRO A 374 TYR A 377 5 4
SHEET 1 A 7 GLN A 8 GLN A 14 0
SHEET 2 A 7 GLU A 361 THR A 368 -1 O PHE A 364 N GLU A 10
SHEET 3 A 7 PRO A 348 ALA A 356 -1 N TYR A 354 O VAL A 363
SHEET 4 A 7 VAL A 325 THR A 342 -1 N MET A 340 O LEU A 349
SHEET 5 A 7 ALA A 305 ASN A 312 -1 N LEU A 307 O LEU A 327
SHEET 6 A 7 GLN A 291 PRO A 298 -1 N TYR A 295 O TYR A 310
SHEET 7 A 7 SER A 275 PRO A 280 -1 N PHE A 279 O TRP A 292
SHEET 1 B 4 TYR A 20 LEU A 28 0
SHEET 2 B 4 SER A 33 GLN A 40 -1 O GLU A 39 N ARG A 21
SHEET 3 B 4 LEU A 51 ASP A 60 -1 O GLY A 57 N LEU A 34
SHEET 4 B 4 GLN A 65 TRP A 68 -1 O GLN A 65 N ASP A 60
SHEET 1 C 4 TYR A 20 LEU A 28 0
SHEET 2 C 4 SER A 33 GLN A 40 -1 O GLU A 39 N ARG A 21
SHEET 3 C 4 LEU A 51 ASP A 60 -1 O GLY A 57 N LEU A 34
SHEET 4 C 4 GLU A 72 VAL A 73 -1 O GLU A 72 N LEU A 54
SHEET 1 D 4 ARG A 83 TYR A 91 0
SHEET 2 D 4 LEU A 98 ILE A 105 -1 O PHE A 99 N LEU A 90
SHEET 3 D 4 ARG A 123 SER A 129 -1 O CYS A 125 N PHE A 102
SHEET 4 D 4 ARG A 140 ASP A 141 -1 O ARG A 140 N GLN A 126
SHEET 1 E 3 TRP A 154 VAL A 159 0
SHEET 2 E 3 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 E 3 LEU A 165 GLN A 166 -1 N LEU A 165 O VAL A 175
SHEET 1 F 4 TRP A 154 VAL A 159 0
SHEET 2 F 4 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 F 4 ILE A 191 SER A 199 -1 O SER A 199 N LEU A 174
SHEET 4 F 4 ALA A 207 ARG A 208 -1 O ALA A 207 N LEU A 198
SHEET 1 G 4 THR A 216 THR A 226 0
SHEET 2 G 4 GLN A 229 SER A 238 -1 O THR A 233 N ALA A 222
SHEET 3 G 4 ALA A 242 SER A 248 -1 O VAL A 244 N ALA A 236
SHEET 4 G 4 GLN A 259 VAL A 265 -1 O GLN A 259 N GLN A 245
SSBOND 1 CYS A 88 CYS A 164 1555 1555 2.83
CISPEP 1 GLY A 160 PRO A 161 0 0.43
CISPEP 2 PRO A 268 PRO A 269 0 0.13
CISPEP 3 PRO A 315 PRO A 316 0 -0.12
CRYST1 145.940 145.940 64.350 90.00 90.00 120.00 H 3 9
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 0.006852 0.003956 0.000000 0.00000
SCALE2 0.000000 0.007912 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
