2D5L-pdb | HEADER HYDROLASE 02-NOV-05 2D5L
TITLE CRYSTAL STRUCTURE OF PROLYL TRIPEPTIDYL AMINOPEPTIDASE FROM
TITLE 2 PORPHYROMONAS GINGIVALIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE IV, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 39-732;
COMPND 5 SYNONYM: PROLYL TRIPEPTIDYL AMINOPEPTIDASE;
COMPND 6 EC: 3.4.14.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PORPHYROMONAS GINGIVALIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: W83;
SOURCE 5 GENE: PG1361;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE-30
KEYWDS PEPTIDASE FAMILY S9, SERINE PEPTIDASE, PROLYL
KEYWDS 2 OLIGOPEPTIDASE FAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAKAJIMA,K.ITO,Y.XU,N.YAMADA,Y.ONOHARA,T.YOSHIMOTO
REVDAT 1 19-SEP-06 2D5L 0
JRNL AUTH K.ITO,Y.NAKAJIMA,Y.XU,N.YAMADA,Y.ONOHARA,T.ITO,
JRNL AUTH 2 F.MATSUBARA,T.KABASHIMA,K.NAKAYAMA,T.YOSHIMOTO
JRNL TITL CRYSTAL STRUCTURE AND MECHANISM OF TRIPEPTIDYL
JRNL TITL 2 ACTIVITY OF PROLYL TRIPEPTIDYL AMINOPEPTIDASE FROM
JRNL TITL 3 PORPHYROMONAS GINGIVALIS
JRNL REF J.MOL.BIOL. V. 362 228 2006
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
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) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 61208
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) : 0.203
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3106
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 : 5280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 419
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.60
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.13
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.31
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.74
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: NULL
REMARK 4
REMARK 4 2D5L COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-NOV-2005.
REMARK 100 THE RCSB ID CODE IS RCSB025014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-2004; 27-OCT-2004; 28-
REMARK 200 OCT-2004
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N; N
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; ROTATING
REMARK 200 ANODE; ROTATING ANODE
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU MICROMAX007;
REMARK 200 RIGAKU MICROMAX007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 1.5418; 1.5418
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR; CONFOCAL
REMARK 200 MIRROR; CONFOCAL MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; RIGAKU
REMARK 200 RAXIS IV; RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61466
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.300
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 85.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.80
REMARK 200 R MERGE FOR SHELL (I) : 0.27100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 15.300
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: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M POTASSIUM SODIUM TARTRATE,
REMARK 280 0.2M LITHIUM SULFATE, 0.1M CHES BUFFER, PH 9.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X-Y,X,1/2+Z
REMARK 290 3555 -Y,X-Y,Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 -X+Y,-X,Z
REMARK 290 6555 Y,-X+Y,1/2+Z
REMARK 290 7555 X-Y,-Y,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -X+Y,Y,1/2-Z
REMARK 290 11555 Y,X,-Z
REMARK 290 12555 X,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 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 79.84200
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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.84200
REMARK 290 SMTRY1 5 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.84200
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.84200
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 79.84200
REMARK 290 SMTRY1 11 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 11 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 79.84200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 159.68400
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 MET A 27
REMARK 465 ARG A 28
REMARK 465 GLY A 29
REMARK 465 SER A 30
REMARK 465 HIS A 31
REMARK 465 HIS A 32
REMARK 465 HIS A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 LEU A 39
REMARK 465 MET A 40
REMARK 465 PRO A 41
REMARK 465 GLY A 42
REMARK 465 GLY A 43
REMARK 465 LYS A 44
REMARK 465 TYR A 53
REMARK 465 VAL A 54
REMARK 465 ALA A 77
REMARK 465 ASN A 78
REMARK 465 GLY A 79
REMARK 465 LYS A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLU A 98
REMARK 465 GLY A 99
REMARK 465 CYS A 100
REMARK 465 LYS A 101
REMARK 465 PHE A 102
REMARK 465 GLN A 103
REMARK 465 THR A 104
REMARK 465 THR A 105
REMARK 465 ASP A 106
REMARK 465 ALA A 107
REMARK 465 PHE A 108
REMARK 465 ASN A 471
REMARK 465 PRO A 472
REMARK 465 ASP A 473
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 LYS A 76 CG CD CE NZ
REMARK 470 GLN A 126 CG CD OE1 NE2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 LYS A 470 CG CD CE NZ
REMARK 470 ARG A 531 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 628 CG PRO A 628 CD 0.032
REMARK 500 PRO A 679 CG PRO A 679 CD 0.035
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 72 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU A 142 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 SER A 215 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 225 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ILE A 236 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 SER A 292 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 VAL A 335 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP A 367 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 GLN A 375 N - CA - C ANGL. DEV. =-12.4 DEGREES
REMARK 500 VAL A 383 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 390 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 PRO A 425 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG A 431 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ILE A 442 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASN A 458 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 TYR A 516 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 TYR A 518 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 ALA A 557 N - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 VAL A 629 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 GLY A 675 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 VAL A 681 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 TYR A 699 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 TYR A 705 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 HIS A 731 N - CA - C ANGL. DEV. = 10.1 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 603 -115.17 61.46
DBREF 2D5L A 39 732 GB 34541047 NP_905526 39 732
SEQADV 2D5L MET A 27 GB 34541047 HIS TAG
SEQADV 2D5L ARG A 28 GB 34541047 HIS TAG
SEQADV 2D5L GLY A 29 GB 34541047 HIS TAG
SEQADV 2D5L SER A 30 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 31 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 32 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 33 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 34 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 35 GB 34541047 HIS TAG
SEQADV 2D5L HIS A 36 GB 34541047 HIS TAG
SEQADV 2D5L GLY A 37 GB 34541047 HIS TAG
SEQADV 2D5L SER A 38 GB 34541047 HIS TAG
SEQRES 1 A 706 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER LEU
SEQRES 2 A 706 MET PRO GLY GLY LYS GLU PHE TYR ASN PHE TYR PRO GLU
SEQRES 3 A 706 TYR VAL VAL GLY LEU GLN TRP MET GLY ASP ASN TYR VAL
SEQRES 4 A 706 PHE ILE GLU GLY ASP ASP LEU VAL PHE ASN LYS ALA ASN
SEQRES 5 A 706 GLY LYS SER ALA GLN THR THR ARG PHE SER ALA ALA ASP
SEQRES 6 A 706 LEU ASN ALA LEU MET PRO GLU GLY CYS LYS PHE GLN THR
SEQRES 7 A 706 THR ASP ALA PHE PRO SER PHE ARG THR LEU ASP ALA GLY
SEQRES 8 A 706 ARG GLY LEU VAL VAL LEU PHE THR GLN GLY GLY LEU VAL
SEQRES 9 A 706 GLY PHE ASP MET LEU ALA ARG LYS VAL THR TYR LEU PHE
SEQRES 10 A 706 ASP THR ASN GLU GLU THR ALA SER LEU ASP PHE SER PRO
SEQRES 11 A 706 VAL GLY ASP ARG VAL ALA TYR VAL ARG ASN HIS ASN LEU
SEQRES 12 A 706 TYR ILE ALA ARG GLY GLY LYS LEU GLY GLU GLY MET SER
SEQRES 13 A 706 ARG ALA ILE ALA VAL THR ILE ASP GLY THR GLU THR LEU
SEQRES 14 A 706 VAL TYR GLY GLN ALA VAL HIS GLN ARG GLU PHE GLY ILE
SEQRES 15 A 706 GLU LYS GLY THR PHE TRP SER PRO LYS GLY SER CYS LEU
SEQRES 16 A 706 ALA PHE TYR ARG MET ASP GLN SER MET VAL LYS PRO THR
SEQRES 17 A 706 PRO ILE VAL ASP TYR HIS PRO LEU GLU ALA GLU SER LYS
SEQRES 18 A 706 PRO LEU TYR TYR PRO MET ALA GLY THR PRO SER HIS HIS
SEQRES 19 A 706 VAL THR VAL GLY ILE TYR HIS LEU ALA THR GLY LYS THR
SEQRES 20 A 706 VAL TYR LEU GLN THR GLY GLU PRO LYS GLU LYS PHE LEU
SEQRES 21 A 706 THR ASN LEU SER TRP SER PRO ASP GLU ASN ILE LEU TYR
SEQRES 22 A 706 VAL ALA GLU VAL ASN ARG ALA GLN ASN GLU CYS LYS VAL
SEQRES 23 A 706 ASN ALA TYR ASP ALA GLU THR GLY ARG PHE VAL ARG THR
SEQRES 24 A 706 LEU PHE VAL GLU THR ASP LYS HIS TYR VAL GLU PRO LEU
SEQRES 25 A 706 HIS PRO LEU THR PHE LEU PRO GLY SER ASN ASN GLN PHE
SEQRES 26 A 706 ILE TRP GLN SER ARG ARG ASP GLY TRP ASN HIS LEU TYR
SEQRES 27 A 706 LEU TYR ASP THR THR GLY ARG LEU ILE ARG GLN VAL THR
SEQRES 28 A 706 LYS GLY GLU TRP GLU VAL THR ASN PHE ALA GLY PHE ASP
SEQRES 29 A 706 PRO LYS GLY THR ARG LEU TYR PHE GLU SER THR GLU ALA
SEQRES 30 A 706 SER PRO LEU GLU ARG HIS PHE TYR CYS ILE ASP ILE LYS
SEQRES 31 A 706 GLY GLY LYS THR LYS ASP LEU THR PRO GLU SER GLY MET
SEQRES 32 A 706 HIS ARG THR GLN LEU SER PRO ASP GLY SER ALA ILE ILE
SEQRES 33 A 706 ASP ILE PHE GLN SER PRO THR VAL PRO ARG LYS VAL THR
SEQRES 34 A 706 VAL THR ASN ILE GLY LYS GLY SER HIS THR LEU LEU GLU
SEQRES 35 A 706 ALA LYS ASN PRO ASP THR GLY TYR ALA MET PRO GLU ILE
SEQRES 36 A 706 ARG THR GLY THR ILE MET ALA ALA ASP GLY GLN THR PRO
SEQRES 37 A 706 LEU TYR TYR LYS LEU THR MET PRO LEU HIS PHE ASP PRO
SEQRES 38 A 706 ALA LYS LYS TYR PRO VAL ILE VAL TYR VAL TYR GLY GLY
SEQRES 39 A 706 PRO HIS ALA GLN LEU VAL THR LYS THR TRP ARG SER SER
SEQRES 40 A 706 VAL GLY GLY TRP ASP ILE TYR MET ALA GLN LYS GLY TYR
SEQRES 41 A 706 ALA VAL PHE THR VAL ASP SER ARG GLY SER ALA ASN ARG
SEQRES 42 A 706 GLY ALA ALA PHE GLU GLN VAL ILE HIS ARG ARG LEU GLY
SEQRES 43 A 706 GLN THR GLU MET ALA ASP GLN MET CYS GLY VAL ASP PHE
SEQRES 44 A 706 LEU LYS SER GLN SER TRP VAL ASP ALA ASP ARG ILE GLY
SEQRES 45 A 706 VAL HIS GLY TRP SER TYR GLY GLY PHE MET THR THR ASN
SEQRES 46 A 706 LEU MET LEU THR HIS GLY ASP VAL PHE LYS VAL GLY VAL
SEQRES 47 A 706 ALA GLY GLY PRO VAL ILE ASP TRP ASN ARG TYR GLU ILE
SEQRES 48 A 706 MET TYR GLY GLU ARG TYR PHE ASP ALA PRO GLN GLU ASN
SEQRES 49 A 706 PRO GLU GLY TYR ASP ALA ALA ASN LEU LEU LYS ARG ALA
SEQRES 50 A 706 GLY ASP LEU LYS GLY ARG LEU MET LEU ILE HIS GLY ALA
SEQRES 51 A 706 ILE ASP PRO VAL VAL VAL TRP GLN HIS SER LEU LEU PHE
SEQRES 52 A 706 LEU ASP ALA CYS VAL LYS ALA ARG THR TYR PRO ASP TYR
SEQRES 53 A 706 TYR VAL TYR PRO SER HIS GLU HIS ASN VAL MET GLY PRO
SEQRES 54 A 706 ASP ARG VAL HIS LEU TYR GLU THR ILE THR ARG TYR PHE
SEQRES 55 A 706 THR ASP HIS LEU
HET SO4 999 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S1 2-
FORMUL 3 HOH *419(H2 O1)
HELIX 1 1 SER A 88 ALA A 94 1 7
HELIX 2 2 VAL A 201 GLU A 205 5 5
HELIX 3 3 GLY A 536 GLN A 543 1 8
HELIX 4 4 GLY A 560 VAL A 566 1 7
HELIX 5 5 GLY A 572 SER A 588 1 17
HELIX 6 6 SER A 603 HIS A 616 1 14
HELIX 7 7 ASP A 631 TYR A 635 5 5
HELIX 8 8 GLU A 636 ASP A 645 1 10
HELIX 9 9 ALA A 646 GLU A 649 5 4
HELIX 10 10 ASN A 650 ASN A 658 1 9
HELIX 11 11 LEU A 659 LEU A 666 5 8
HELIX 12 12 TRP A 683 ARG A 697 1 15
HELIX 13 13 PRO A 715 LEU A 732 1 18
SHEET 1 A 3 GLN A 58 MET A 60 0
SHEET 2 A 3 ASN A 63 GLU A 68 -1 O VAL A 65 N GLN A 58
SHEET 3 A 3 ASP A 71 ASN A 75 -1 O VAL A 73 N PHE A 66
SHEET 1 B 4 PHE A 111 ASP A 115 0
SHEET 2 B 4 LEU A 120 THR A 125 -1 O LEU A 120 N LEU A 114
SHEET 3 B 4 GLY A 128 ASP A 133 -1 O VAL A 130 N LEU A 123
SHEET 4 B 4 LYS A 138 PHE A 143 -1 O TYR A 141 N GLY A 131
SHEET 1 C 4 ASP A 153 PHE A 154 0
SHEET 2 C 4 ARG A 160 ARG A 165 -1 O ALA A 162 N ASP A 153
SHEET 3 C 4 ASN A 168 ARG A 173 -1 O ALA A 172 N VAL A 161
SHEET 4 C 4 ILE A 185 ALA A 186 -1 O ILE A 185 N ILE A 171
SHEET 1 D 3 LEU A 195 TYR A 197 0
SHEET 2 D 3 CYS A 220 ASP A 227 -1 O MET A 226 N VAL A 196
SHEET 3 D 3 THR A 212 TRP A 214 -1 N PHE A 213 O ALA A 222
SHEET 1 E 4 LEU A 195 TYR A 197 0
SHEET 2 E 4 CYS A 220 ASP A 227 -1 O MET A 226 N VAL A 196
SHEET 3 E 4 HIS A 260 HIS A 267 -1 O TYR A 266 N LEU A 221
SHEET 4 E 4 LYS A 272 TYR A 275 -1 O LYS A 272 N HIS A 267
SHEET 1 F 2 THR A 234 ASP A 238 0
SHEET 2 F 2 GLU A 245 LEU A 249 -1 O GLU A 245 N ASP A 238
SHEET 1 G 4 PHE A 285 TRP A 291 0
SHEET 2 G 4 ILE A 297 VAL A 303 -1 O TYR A 299 N SER A 290
SHEET 3 G 4 GLU A 309 ASP A 316 -1 O LYS A 311 N GLU A 302
SHEET 4 G 4 PHE A 322 THR A 330 -1 O ARG A 324 N ALA A 314
SHEET 1 H 4 THR A 342 PHE A 343 0
SHEET 2 H 4 GLN A 350 SER A 355 -1 O ILE A 352 N THR A 342
SHEET 3 H 4 HIS A 362 ASP A 367 -1 O TYR A 364 N TRP A 353
SHEET 4 H 4 LEU A 372 GLN A 375 -1 O ARG A 374 N LEU A 365
SHEET 1 I 4 VAL A 383 PHE A 389 0
SHEET 2 I 4 ARG A 395 SER A 400 -1 O TYR A 397 N GLY A 388
SHEET 3 I 4 HIS A 409 ASP A 414 -1 O TYR A 411 N PHE A 398
SHEET 4 I 4 THR A 420 ASP A 422 -1 O LYS A 421 N CYS A 412
SHEET 1 J 4 MET A 429 LEU A 434 0
SHEET 2 J 4 ALA A 440 GLN A 446 -1 O GLN A 446 N MET A 429
SHEET 3 J 4 ARG A 452 ASN A 458 -1 O THR A 455 N ASP A 443
SHEET 4 J 4 SER A 463 ALA A 469 -1 O LEU A 467 N VAL A 454
SHEET 1 K 8 ILE A 481 MET A 487 0
SHEET 2 K 8 PRO A 494 THR A 500 -1 O LEU A 499 N ARG A 482
SHEET 3 K 8 ALA A 547 VAL A 551 -1 O VAL A 548 N THR A 500
SHEET 4 K 8 TYR A 511 TYR A 516 1 N ILE A 514 O ALA A 547
SHEET 5 K 8 VAL A 592 TRP A 602 1 O GLY A 598 N VAL A 513
SHEET 6 K 8 PHE A 620 GLY A 626 1 O GLY A 626 N GLY A 601
SHEET 7 K 8 ARG A 669 GLY A 675 1 O ILE A 673 N ALA A 625
SHEET 8 K 8 ASP A 701 TYR A 705 1 O ASP A 701 N LEU A 670
CISPEP 1 GLU A 280 PRO A 281 0 -0.16
CRYST1 149.394 149.394 159.684 90.00 90.00 120.00 P 63 2 2 12
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 0.006694 0.003865 0.000000 0.00000
SCALE2 0.000000 0.007729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006262 0.00000
TER 5281 LEU A 732
MASTER 378 0 1 13 44 0 0 6 5704 1 5 55
END
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