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HEADER HYDROLASE 13-FEB-07 2ECF
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL AMINOPEPTIDASE IV FROM
TITLE 2 STENOTROPHOMONAS MALTOPHILIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV;
COMPND 5 EC: 3.4.14.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STENOTROPHOMONAS MALTOPHILIA;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS MALTOPHILIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS PROLYL OLIGOPEPTIDASE FAMILY, PEPTIDASE FAMILY S9,
KEYWDS 2 DIPEPTIDYL PEPTIDASE IV, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKAJIMA,K.ITO,T.YOSHIMOTO
REVDAT 1 26-FEB-08 2ECF 0
JRNL AUTH Y.NAKAJIMA,T.TOSHIMA,K.ITO,T.EGAWA,K.KYONO,
JRNL AUTH 2 F.MATSUBARA,H.OYAMA,T.YOSHIMOTO
JRNL TITL CRYSTAL STRUCTURE OF DIPEPTIDYL AMINOPEPTIDASE IV
JRNL TITL 2 FROM STENOTROPHOMONAS MALTOPHILIA EXHIBITED AN
JRNL TITL 3 ACTIVITY AGAINST SUBSTRATE CONTAING
JRNL TITL 4 4-HYDROXYPROLINE RESIDUE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 23264
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) : 0.185
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1197
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 120
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 : 5445
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.30
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.31
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
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 2ECF COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB026495.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-2003; 03-JUL-2003; 03-
REMARK 200 JUL-2003
REMARK 200 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; N; N
REMARK 200 RADIATION SOURCE : ROTATING ANODE; ROTATING
REMARK 200 ANODE; ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200; RIGAKU RU200;
REMARK 200 RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.5418; 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE; OSMIC MIRROR;
REMARK 200 GRAPHITE
REMARK 200 OPTICS : MONOCHROMETOR; OSMIC MIRROR;
REMARK 200 MONOCHROMETOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE;
REMARK 200 IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV; RIGAKU RAXIS
REMARK 200 IV; RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23396
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.33300
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH;
REMARK 200 SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 0.1M TRIS-HCL, PH 8.0, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.94750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.93850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.93850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 121.42125
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.93850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.93850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.47375
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.93850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.93850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 121.42125
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.93850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.93850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.47375
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 80.94750
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: DIMER
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 105.87700
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 105.87700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 242.84250
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 HIS A 3
REMARK 465 LEU A 4
REMARK 465 PHE A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 LEU A 8
REMARK 465 ALA A 9
REMARK 465 PHE A 10
REMARK 465 MET A 11
REMARK 465 LEU A 12
REMARK 465 ALA A 13
REMARK 465 THR A 14
REMARK 465 SER A 15
REMARK 465 THR A 16
REMARK 465 VAL A 17
REMARK 465 ALA A 18
REMARK 465 HIS A 19
REMARK 465 ALA A 20
REMARK 465 GLU A 21
REMARK 465 PRO A 87
REMARK 465 GLY A 88
REMARK 465 THR A 89
REMARK 465 GLU A 90
REMARK 465 THR A 91
REMARK 465 LEU A 92
REMARK 465 SER A 93
REMARK 465 ASP A 94
REMARK 465 GLU A 95
REMARK 465 GLU A 96
REMARK 465 LYS A 97
REMARK 465 ALA A 98
REMARK 465 ARG A 99
REMARK 465 ARG A 100
REMARK 465 GLU A 101
REMARK 465 ARG A 102
REMARK 465 GLN A 103
REMARK 465 ARG A 104
REMARK 465 ILE A 105
REMARK 465 ALA A 106
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 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 137 CG CD CE NZ
REMARK 470 GLN A 138 CG CD OE1 NE2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 LYS A 370 CG CD CE NZ
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 PRO A 37 176.86 -59.97
REMARK 500 THR A 38 -172.86 -171.89
REMARK 500 ILE A 111 90.37 -67.66
REMARK 500 GLN A 115 146.01 -170.54
REMARK 500 ALA A 120 27.58 43.77
REMARK 500 LYS A 137 -78.64 -43.61
REMARK 500 ASP A 190 21.88 -73.32
REMARK 500 ASP A 220 0.33 94.94
REMARK 500 PRO A 270 49.57 -78.32
REMARK 500 PRO A 297 -2.48 -52.66
REMARK 500 THR A 334 -88.21 -111.79
REMARK 500 SER A 367 -5.93 -56.87
REMARK 500 LYS A 368 -72.04 -102.78
REMARK 500 ASN A 378 46.52 -94.27
REMARK 500 ALA A 386 177.29 177.79
REMARK 500 SER A 406 108.81 -160.88
REMARK 500 ALA A 436 11.76 86.12
REMARK 500 SER A 444 163.33 179.15
REMARK 500 ASN A 446 -9.42 -53.89
REMARK 500 ALA A 463 -176.40 -175.88
REMARK 500 PRO A 476 -8.52 -44.55
REMARK 500 LYS A 498 -29.77 -155.92
REMARK 500 TYR A 524 -66.75 -127.63
REMARK 500 LYS A 577 63.72 -153.30
REMARK 500 THR A 580 -81.23 -128.77
REMARK 500 SER A 610 -115.45 57.02
REMARK 500 ALA A 623 53.89 -159.35
REMARK 500 ALA A 634 62.11 30.08
REMARK 500 ASP A 652 179.38 66.85
REMARK 500 ASN A 657 54.62 -148.05
REMARK 500 MET A 710 106.10 -172.49
REMARK 500 LYS A 716 -145.87 -100.85
REMARK 500 LYS A 740 81.14 53.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ECF A 1 741 UNP P95782 P95782_XANMA 1 741
SEQRES 1 A 741 MET ARG HIS LEU PHE ALA SER LEU ALA PHE MET LEU ALA
SEQRES 2 A 741 THR SER THR VAL ALA HIS ALA GLU LYS LEU THR LEU GLU
SEQRES 3 A 741 ALA ILE THR GLY PRO LEU PRO LEU SER GLY PRO THR LEU
SEQRES 4 A 741 MET LYS PRO LYS VAL ALA PRO ASP GLY SER ARG VAL THR
SEQRES 5 A 741 PHE LEU ARG GLY LYS ASP SER ASP ARG ASN GLN LEU ASP
SEQRES 6 A 741 LEU TRP SER TYR ASP ILE GLY SER GLY GLN THR ARG LEU
SEQRES 7 A 741 LEU VAL ASP SER LYS VAL VAL LEU PRO GLY THR GLU THR
SEQRES 8 A 741 LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG GLN ARG
SEQRES 9 A 741 ILE ALA ALA MET THR GLY ILE VAL ASP TYR GLN TRP SER
SEQRES 10 A 741 PRO ASP ALA GLN ARG LEU LEU PHE PRO LEU GLY GLY GLU
SEQRES 11 A 741 LEU TYR LEU TYR ASP LEU LYS GLN GLU GLY LYS ALA ALA
SEQRES 12 A 741 VAL ARG GLN LEU THR HIS GLY GLU GLY PHE ALA THR ASP
SEQRES 13 A 741 ALA LYS LEU SER PRO LYS GLY GLY PHE VAL SER PHE ILE
SEQRES 14 A 741 ARG GLY ARG ASN LEU TRP VAL ILE ASP LEU ALA SER GLY
SEQRES 15 A 741 ARG GLN MET GLN LEU THR ALA ASP GLY SER THR THR ILE
SEQRES 16 A 741 GLY ASN GLY ILE ALA GLU PHE VAL ALA ASP GLU GLU MET
SEQRES 17 A 741 ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP ASP SER
SEQRES 18 A 741 ALA ILE ALA TYR ALA ARG ILE ASP GLU SER PRO VAL PRO
SEQRES 19 A 741 VAL GLN LYS ARG TYR GLU VAL TYR ALA ASP ARG THR ASP
SEQRES 20 A 741 VAL ILE GLU GLN ARG TYR PRO ALA ALA GLY ASP ALA ASN
SEQRES 21 A 741 VAL GLN VAL LYS LEU GLY VAL ILE SER PRO ALA GLU GLN
SEQRES 22 A 741 ALA GLN THR GLN TRP ILE ASP LEU GLY LYS GLU GLN ASP
SEQRES 23 A 741 ILE TYR LEU ALA ARG VAL ASN TRP ARG ASP PRO GLN HIS
SEQRES 24 A 741 LEU SER PHE GLN ARG GLN SER ARG ASP GLN LYS LYS LEU
SEQRES 25 A 741 ASP LEU VAL GLU VAL THR LEU ALA SER ASN GLN GLN ARG
SEQRES 26 A 741 VAL LEU ALA HIS GLU THR SER PRO THR TRP VAL PRO LEU
SEQRES 27 A 741 HIS ASN SER LEU ARG PHE LEU ASP ASP GLY SER ILE LEU
SEQRES 28 A 741 TRP SER SER GLU ARG THR GLY PHE GLN HIS LEU TYR ARG
SEQRES 29 A 741 ILE ASP SER LYS GLY LYS ALA ALA ALA LEU THR HIS GLY
SEQRES 30 A 741 ASN TRP SER VAL ASP GLU LEU LEU ALA VAL ASP GLU LYS
SEQRES 31 A 741 ALA GLY LEU ALA TYR PHE ARG ALA GLY ILE GLU SER ALA
SEQRES 32 A 741 ARG GLU SER GLN ILE TYR ALA VAL PRO LEU GLN GLY GLY
SEQRES 33 A 741 GLN PRO GLN ARG LEU SER LYS ALA PRO GLY MET HIS SER
SEQRES 34 A 741 ALA SER PHE ALA ARG ASN ALA SER VAL TYR VAL ASP SER
SEQRES 35 A 741 TRP SER ASN ASN SER THR PRO PRO GLN ILE GLU LEU PHE
SEQRES 36 A 741 ARG ALA ASN GLY GLU LYS ILE ALA THR LEU VAL GLU ASN
SEQRES 37 A 741 ASP LEU ALA ASP PRO LYS HIS PRO TYR ALA ARG TYR ARG
SEQRES 38 A 741 GLU ALA GLN ARG PRO VAL GLU PHE GLY THR LEU THR ALA
SEQRES 39 A 741 ALA ASP GLY LYS THR PRO LEU ASN TYR SER VAL ILE LYS
SEQRES 40 A 741 PRO ALA GLY PHE ASP PRO ALA LYS ARG TYR PRO VAL ALA
SEQRES 41 A 741 VAL TYR VAL TYR GLY GLY PRO ALA SER GLN THR VAL THR
SEQRES 42 A 741 ASP SER TRP PRO GLY ARG GLY ASP HIS LEU PHE ASN GLN
SEQRES 43 A 741 TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE SER LEU ASP
SEQRES 44 A 741 ASN ARG GLY THR PRO ARG ARG GLY ARG ASP PHE GLY GLY
SEQRES 45 A 741 ALA LEU TYR GLY LYS GLN GLY THR VAL GLU VAL ALA ASP
SEQRES 46 A 741 GLN LEU ARG GLY VAL ALA TRP LEU LYS GLN GLN PRO TRP
SEQRES 47 A 741 VAL ASP PRO ALA ARG ILE GLY VAL GLN GLY TRP SER ASN
SEQRES 48 A 741 GLY GLY TYR MET THR LEU MET LEU LEU ALA LYS ALA SER
SEQRES 49 A 741 ASP SER TYR ALA CYS GLY VAL ALA GLY ALA PRO VAL THR
SEQRES 50 A 741 ASP TRP GLY LEU TYR ASP SER HIS TYR THR GLU ARG TYR
SEQRES 51 A 741 MET ASP LEU PRO ALA ARG ASN ASP ALA GLY TYR ARG GLU
SEQRES 52 A 741 ALA ARG VAL LEU THR HIS ILE GLU GLY LEU ARG SER PRO
SEQRES 53 A 741 LEU LEU LEU ILE HIS GLY MET ALA ASP ASP ASN VAL LEU
SEQRES 54 A 741 PHE THR ASN SER THR SER LEU MET SER ALA LEU GLN LYS
SEQRES 55 A 741 ARG GLY GLN PRO PHE GLU LEU MET THR TYR PRO GLY ALA
SEQRES 56 A 741 LYS HIS GLY LEU SER GLY ALA ASP ALA LEU HIS ARG TYR
SEQRES 57 A 741 ARG VAL ALA GLU ALA PHE LEU GLY ARG CYS LEU LYS PRO
FORMUL 2 HOH *66(H2 O)
HELIX 1 1 THR A 24 THR A 29 1 6
HELIX 2 2 ASP A 81 VAL A 85 5 5
HELIX 3 3 GLU A 201 MET A 208 1 8
HELIX 4 4 TYR A 477 GLU A 482 1 6
HELIX 5 5 ARG A 539 GLN A 551 1 13
HELIX 6 6 GLY A 567 ALA A 573 1 7
HELIX 7 7 THR A 580 GLN A 595 1 16
HELIX 8 8 SER A 610 ALA A 623 1 14
HELIX 9 9 ASP A 638 TYR A 642 5 5
HELIX 10 10 ASP A 643 ASP A 652 1 10
HELIX 11 11 PRO A 654 ARG A 656 5 3
HELIX 12 12 ASN A 657 ARG A 665 1 9
HELIX 13 13 VAL A 666 LEU A 673 5 8
HELIX 14 14 PHE A 690 ARG A 703 1 14
HELIX 15 15 SER A 720 LYS A 740 1 21
SHEET 1 A 4 MET A 40 VAL A 44 0
SHEET 2 A 4 ARG A 50 ARG A 55 -1 O LEU A 54 N MET A 40
SHEET 3 A 4 GLN A 63 ASP A 70 -1 O ASP A 65 N ARG A 55
SHEET 4 A 4 THR A 76 VAL A 80 -1 O VAL A 80 N LEU A 66
SHEET 1 B 4 MET A 40 VAL A 44 0
SHEET 2 B 4 ARG A 50 ARG A 55 -1 O LEU A 54 N MET A 40
SHEET 3 B 4 GLN A 63 ASP A 70 -1 O ASP A 65 N ARG A 55
SHEET 4 B 4 THR A 109 GLY A 110 1 O THR A 109 N LEU A 64
SHEET 1 C 3 GLN A 115 TRP A 116 0
SHEET 2 C 3 ARG A 122 LEU A 127 -1 O LEU A 124 N GLN A 115
SHEET 3 C 3 GLU A 130 ASP A 135 -1 O TYR A 132 N PHE A 125
SHEET 1 D 4 ALA A 154 LEU A 159 0
SHEET 2 D 4 PHE A 165 ARG A 170 -1 O ILE A 169 N THR A 155
SHEET 3 D 4 ASN A 173 ASP A 178 -1 O TRP A 175 N PHE A 168
SHEET 4 D 4 ARG A 183 GLN A 186 -1 O MET A 185 N VAL A 176
SHEET 1 E 3 ILE A 195 ASN A 197 0
SHEET 2 E 3 ILE A 223 ASP A 229 -1 O ILE A 228 N GLY A 196
SHEET 3 E 3 TYR A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 F 4 ILE A 195 ASN A 197 0
SHEET 2 F 4 ILE A 223 ASP A 229 -1 O ILE A 228 N GLY A 196
SHEET 3 F 4 GLN A 262 ILE A 268 -1 O GLY A 266 N TYR A 225
SHEET 4 F 4 GLN A 277 ILE A 279 -1 O ILE A 279 N LEU A 265
SHEET 1 G 2 VAL A 235 VAL A 241 0
SHEET 2 G 2 THR A 246 ARG A 252 -1 O ILE A 249 N ARG A 238
SHEET 1 H 4 ILE A 287 ASP A 296 0
SHEET 2 H 4 HIS A 299 SER A 306 -1 O SER A 301 N ASN A 293
SHEET 3 H 4 LYS A 311 THR A 318 -1 O ASP A 313 N ARG A 304
SHEET 4 H 4 GLN A 324 THR A 331 -1 O ARG A 325 N GLU A 316
SHEET 1 I 4 ARG A 343 PHE A 344 0
SHEET 2 I 4 ILE A 350 SER A 354 -1 O LEU A 351 N ARG A 343
SHEET 3 I 4 HIS A 361 ILE A 365 -1 O TYR A 363 N TRP A 352
SHEET 4 I 4 ALA A 371 ALA A 373 -1 O ALA A 372 N ARG A 364
SHEET 1 J 4 VAL A 381 ASP A 388 0
SHEET 2 J 4 LEU A 393 ALA A 398 -1 O ARG A 397 N GLU A 383
SHEET 3 J 4 GLN A 407 PRO A 412 -1 O GLN A 407 N ALA A 398
SHEET 4 J 4 GLN A 419 ARG A 420 -1 O GLN A 419 N ALA A 410
SHEET 1 K 4 MET A 427 PHE A 432 0
SHEET 2 K 4 VAL A 438 ASN A 445 -1 O SER A 442 N SER A 429
SHEET 3 K 4 THR A 448 ARG A 456 -1 O GLU A 453 N ASP A 441
SHEET 4 K 4 LYS A 461 ALA A 463 -1 O ILE A 462 N LEU A 454
SHEET 1 L 8 VAL A 487 THR A 493 0
SHEET 2 L 8 PRO A 500 ILE A 506 -1 O LEU A 501 N LEU A 492
SHEET 3 L 8 VAL A 554 LEU A 558 -1 O SER A 557 N SER A 504
SHEET 4 L 8 TYR A 517 TYR A 522 1 N ALA A 520 O VAL A 554
SHEET 5 L 8 VAL A 599 TRP A 609 1 O GLY A 605 N VAL A 519
SHEET 6 L 8 CYS A 629 GLY A 633 1 O GLY A 633 N GLY A 608
SHEET 7 L 8 LEU A 677 GLY A 682 1 O ILE A 680 N ALA A 632
SHEET 8 L 8 GLU A 708 TYR A 712 1 O GLU A 708 N LEU A 679
SSBOND 1 CYS A 629 CYS A 738 1555 1555 2.02
CRYST1 105.877 105.877 161.895 90.00 90.00 90.00 P 43 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 0.009445 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006177 0.00000
TER 5446 PRO A 741
MASTER 348 0 0 15 48 0 0 6 5511 1 2 57
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