| content |
HEADER HYDROLASE 01-NOV-17 5YP2
TITLE CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP IV) WITH DPP4
TITLE 2 INHIBITOR FROM PSEUDOXANTHOMONAS MEXICANA WO24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV,DAP IV;
COMPND 5 EC: 3.4.14.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOXANTHOMONAS MEXICANA;
SOURCE 3 ORGANISM_COMMON: PSEUDOMONAS SP. WO24;
SOURCE 4 ORGANISM_TAXID: 128785;
SOURCE 5 STRAIN: WO24;
SOURCE 6 GENE: DAP4;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS DAP IV, CLAN SC S9, PEPTIDASE, DPP4, DPP8, DPP9, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUIMOTO,S.MORISAWA,I.IIZUKA,
AUTHOR 2 A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,Y.SAKAMOTO,T.NONAKA
REVDAT 1 21-FEB-18 5YP2 0
JRNL AUTH S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUJIMOTO,S.MORISAWA,
JRNL AUTH 2 I.IIZUKA,A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,
JRNL AUTH 3 Y.SAKAMOTO,T.NONAKA
JRNL TITL CRYSTAL STRUCTURES OF A BACTERIAL DIPEPTIDYL PEPTIDASE IV
JRNL TITL 2 REVEAL A NOVEL SUBSTRATE RECOGNITION MECHANISM DISTINCT FROM
JRNL TITL 3 THAT OF MAMMALIAN ORTHOLOGUES.
JRNL REF SCI REP V. 8 2714 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29426867
JRNL DOI 10.1038/S41598-018-21056-Y
REMARK 2
REMARK 2 RESOLUTION. 2.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 89236
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 + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4652
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.13
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6117
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 305
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11320
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.76000
REMARK 3 B22 (A**2) : -0.81000
REMARK 3 B33 (A**2) : 0.06000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.210
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.468
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11657 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10660 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15853 ; 1.864 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24632 ; 1.052 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1446 ; 7.321 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 544 ;31.277 ;23.051
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1832 ;15.063 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 102 ;19.460 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1721 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13142 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2528 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5790 ; 2.517 ; 3.053
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5789 ; 2.516 ; 3.052
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7234 ; 3.592 ; 4.571
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7235 ; 3.592 ; 4.572
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5867 ; 3.148 ; 3.358
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5867 ; 3.148 ; 3.358
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8620 ; 4.744 ; 4.903
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13024 ; 6.256 ;35.739
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12929 ; 6.232 ;35.668
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005660.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.5.170
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93976
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.130
REMARK 200 RESOLUTION RANGE LOW (A) : 44.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.87600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 5YP1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 20000, 100MM MES PH6.5, 20%
REMARK 280 GLYCEROL, 1.5MM INHIBITOR 1C, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
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 29.94000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.94500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.11000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.94500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.94000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.11000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 ARG A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 PHE A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 PHE A 9
REMARK 465 ALA A 10
REMARK 465 LEU A 11
REMARK 465 ILE A 12
REMARK 465 THR A 13
REMARK 465 VAL A 14
REMARK 465 ALA A 15
REMARK 465 THR A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 HIS A 21
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LEU B 3
REMARK 465 ALA B 4
REMARK 465 LEU B 5
REMARK 465 PHE B 6
REMARK 465 ALA B 7
REMARK 465 LEU B 8
REMARK 465 PHE B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 ILE B 12
REMARK 465 THR B 13
REMARK 465 VAL B 14
REMARK 465 ALA B 15
REMARK 465 THR B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 HIS B 21
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLN A 379 O HOH A 901 1.92
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 192 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 297 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 297 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 403 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 537 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 542 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 542 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG B 568 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 606 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG B 606 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP B 641 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 36 -58.90 -121.65
REMARK 500 LEU A 129 126.49 -171.74
REMARK 500 SER A 162 146.83 -39.55
REMARK 500 PRO A 272 44.63 -76.90
REMARK 500 THR A 336 -93.90 -98.38
REMARK 500 THR A 501 -42.91 -134.25
REMARK 500 TYR A 527 -71.15 -118.41
REMARK 500 ARG A 542 32.48 -77.05
REMARK 500 SER A 543 -117.19 -112.81
REMARK 500 LYS A 580 54.46 -147.16
REMARK 500 THR A 583 -71.58 -113.69
REMARK 500 SER A 613 -105.34 63.01
REMARK 500 HIS A 626 49.75 -141.52
REMARK 500 ALA A 637 58.79 29.16
REMARK 500 ASP A 655 176.82 67.49
REMARK 500 ASN A 660 59.97 -144.62
REMARK 500 ASN A 691 -75.04 -117.37
REMARK 500 LYS A 720 -142.27 -102.05
REMARK 500 LYS A 744 61.74 62.59
REMARK 500 LEU B 36 -66.45 -135.03
REMARK 500 THR B 336 -88.63 -106.34
REMARK 500 GLU B 381 58.72 -90.14
REMARK 500 THR B 501 -37.09 -138.91
REMARK 500 TYR B 527 -64.06 -120.16
REMARK 500 SER B 543 -138.55 -152.83
REMARK 500 LYS B 580 41.14 -145.94
REMARK 500 THR B 583 -84.23 -120.13
REMARK 500 SER B 613 -110.42 69.24
REMARK 500 HIS B 626 51.87 -141.38
REMARK 500 ALA B 637 56.61 36.13
REMARK 500 ASP B 655 176.92 67.20
REMARK 500 ASN B 660 58.13 -147.82
REMARK 500 ASN B 691 -74.33 -120.04
REMARK 500 LYS B 720 -140.19 -109.21
REMARK 500 LYS B 744 71.61 43.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 144 ALA A 145 147.24
REMARK 500 PRO A 638 VAL A 639 149.85
REMARK 500 GLY A 718 ALA A 719 -148.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8YC A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 8YC B 801 and SER B
REMARK 800 613
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YP1 RELATED DB: PDB
REMARK 900 5YP1 IS THE SAME PROTEIN APO FORM.
REMARK 900 RELATED ID: 5YP3 RELATED DB: PDB
REMARK 900 5YP3 IS THE SAME PROTEIN COMPLEXED WITH ILE-PRO.
REMARK 900 RELATED ID: 5YP4 RELATED DB: PDB
REMARK 900 5YP4 IS THE SAME PROTEIN COMPLEXED WITH LYS-PRO.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE M12I IS MUTAGENESIS ACCORDING TO SEQUENCE DATABASE
REMARK 999 UNIPORTKB Q6F3I7 (DAP4_PSEMX).
DBREF 5YP2 A 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
DBREF 5YP2 B 1 745 UNP Q6F3I7 DAP4_PSEMX 1 745
SEQADV 5YP2 ILE A 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQADV 5YP2 ILE B 12 UNP Q6F3I7 MET 12 SEE SEQUENCE DETAILS
SEQRES 1 A 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 A 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 A 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 A 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 A 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 A 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 A 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 A 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 A 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 A 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 A 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 A 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 A 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 A 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 A 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 A 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 A 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 A 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 A 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 A 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 A 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 A 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 A 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 A 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 A 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 A 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 A 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 A 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 A 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 A 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 A 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 A 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 A 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 A 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 A 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 A 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 A 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 A 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 A 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 A 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 A 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 A 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 A 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 A 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 A 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 A 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 A 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 A 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 A 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 A 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 A 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 A 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 A 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 A 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 A 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 A 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 A 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 A 745 CYS LEU LYS PRO
SEQRES 1 B 745 MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR
SEQRES 2 B 745 VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR
SEQRES 3 B 745 LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO
SEQRES 4 B 745 THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG
SEQRES 5 B 745 VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG
SEQRES 6 B 745 LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR
SEQRES 7 B 745 ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU
SEQRES 8 B 745 GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG
SEQRES 9 B 745 GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN
SEQRES 10 B 745 TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY
SEQRES 11 B 745 GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG
SEQRES 12 B 745 ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA
SEQRES 13 B 745 THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER
SEQRES 14 B 745 PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA
SEQRES 15 B 745 SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP
SEQRES 16 B 745 THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU
SEQRES 17 B 745 GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP
SEQRES 18 B 745 ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO
SEQRES 19 B 745 VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG
SEQRES 20 B 745 THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP
SEQRES 21 B 745 HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS
SEQRES 22 B 745 THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP
SEQRES 23 B 745 PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO
SEQRES 24 B 745 GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS
SEQRES 25 B 745 LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR
SEQRES 26 B 745 GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL
SEQRES 27 B 745 PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG
SEQRES 28 B 745 PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU
SEQRES 29 B 745 TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU
SEQRES 30 B 745 THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE
SEQRES 31 B 745 ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG
SEQRES 32 B 745 ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU
SEQRES 33 B 745 SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY
SEQRES 34 B 745 MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE
SEQRES 35 B 745 VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE
SEQRES 36 B 745 GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU
SEQRES 37 B 745 LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA
SEQRES 38 B 745 LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR
SEQRES 39 B 745 LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER
SEQRES 40 B 745 LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR
SEQRES 41 B 745 PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN
SEQRES 42 B 745 THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE
SEQRES 43 B 745 PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE
SEQRES 44 B 745 THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA
SEQRES 45 B 745 PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU
SEQRES 46 B 745 VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER
SEQRES 47 B 745 GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY
SEQRES 48 B 745 TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA
SEQRES 49 B 745 LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA
SEQRES 50 B 745 PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR
SEQRES 51 B 745 GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY
SEQRES 52 B 745 TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE
SEQRES 53 B 745 GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP
SEQRES 54 B 745 ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER
SEQRES 55 B 745 GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR
SEQRES 56 B 745 TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU
SEQRES 57 B 745 LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG
SEQRES 58 B 745 CYS LEU LYS PRO
HET 8YC A 801 20
HET GOL A 802 6
HET GOL A 803 6
HET 8YC B 801 20
HET GOL B 802 6
HETNAM 8YC (2S,5R)-1-[2-[[1-(HYDROXYMETHYL)
HETNAM 2 8YC CYCLOPENTYL]AMINO]ETHANOYL]PYRROLIDINE-2,5-
HETNAM 3 8YC DICARBONITRILE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 8YC 2(C14 H20 N4 O2)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 8 HOH *700(H2 O)
HELIX 1 AA1 THR A 26 GLY A 32 1 7
HELIX 2 AA2 ASP A 83 LEU A 88 1 6
HELIX 3 AA3 SER A 95 GLN A 105 1 11
HELIX 4 AA4 SER A 141 ASP A 144 5 4
HELIX 5 AA5 GLU A 203 MET A 210 1 8
HELIX 6 AA6 TYR A 480 ALA A 485 1 6
HELIX 7 AA7 SER A 543 GLN A 554 1 12
HELIX 8 AA8 GLY A 570 ALA A 576 1 7
HELIX 9 AA9 THR A 583 SER A 598 1 16
HELIX 10 AB1 SER A 613 HIS A 626 1 14
HELIX 11 AB2 ASP A 641 TYR A 645 5 5
HELIX 12 AB3 ASP A 646 ASP A 655 1 10
HELIX 13 AB4 ASN A 660 SER A 668 1 9
HELIX 14 AB5 SER A 668 VAL A 673 1 6
HELIX 15 AB6 ASP A 674 ILE A 676 5 3
HELIX 16 AB7 PHE A 694 GLY A 708 1 15
HELIX 17 AB8 GLY A 725 LYS A 744 1 20
HELIX 18 AB9 THR B 26 GLY B 32 1 7
HELIX 19 AC1 ASP B 83 LEU B 88 1 6
HELIX 20 AC2 SER B 95 GLN B 105 1 11
HELIX 21 AC3 SER B 141 ASP B 144 5 4
HELIX 22 AC4 GLU B 203 MET B 210 1 8
HELIX 23 AC5 TYR B 480 ARG B 484 5 5
HELIX 24 AC6 SER B 543 GLN B 554 1 12
HELIX 25 AC7 GLY B 570 ALA B 576 1 7
HELIX 26 AC8 THR B 583 SER B 598 1 16
HELIX 27 AC9 SER B 613 HIS B 626 1 14
HELIX 28 AD1 ASP B 641 TYR B 645 5 5
HELIX 29 AD2 ASP B 646 ASP B 655 1 10
HELIX 30 AD3 LEU B 656 ALA B 659 5 4
HELIX 31 AD4 ASN B 660 SER B 668 1 9
HELIX 32 AD5 VAL B 669 ILE B 676 5 8
HELIX 33 AD6 PHE B 694 GLY B 708 1 15
HELIX 34 AD7 ARG B 724 LYS B 744 1 21
SHEET 1 AA1 4 LEU A 41 ILE A 46 0
SHEET 2 AA1 4 ARG A 52 GLY A 58 -1 O LEU A 56 N THR A 42
SHEET 3 AA1 4 ARG A 65 ASP A 72 -1 O TRP A 69 N PHE A 55
SHEET 4 AA1 4 THR A 78 VAL A 82 -1 O LEU A 81 N LEU A 68
SHEET 1 AA2 4 LEU A 41 ILE A 46 0
SHEET 2 AA2 4 ARG A 52 GLY A 58 -1 O LEU A 56 N THR A 42
SHEET 3 AA2 4 ARG A 65 ASP A 72 -1 O TRP A 69 N PHE A 55
SHEET 4 AA2 4 SER A 111 GLY A 112 1 O SER A 111 N LEU A 66
SHEET 1 AA3 4 GLN A 117 TRP A 118 0
SHEET 2 AA3 4 ALA A 124 LEU A 129 -1 O LEU A 126 N GLN A 117
SHEET 3 AA3 4 GLU A 132 ASP A 137 -1 O GLU A 132 N LEU A 129
SHEET 4 AA3 4 VAL A 146 LYS A 148 -1 O ARG A 147 N PHE A 135
SHEET 1 AA4 4 THR A 157 ILE A 161 0
SHEET 2 AA4 4 PHE A 167 ARG A 172 -1 O SER A 169 N LYS A 160
SHEET 3 AA4 4 ASN A 175 ASP A 180 -1 O ILE A 179 N VAL A 168
SHEET 4 AA4 4 LYS A 185 GLN A 188 -1 O VAL A 187 N ALA A 178
SHEET 1 AA5 3 ILE A 197 ASN A 199 0
SHEET 2 AA5 3 ILE A 225 ASP A 231 -1 O ILE A 230 N GLY A 198
SHEET 3 AA5 3 TYR A 216 TRP A 218 -1 N TRP A 217 O ALA A 226
SHEET 1 AA6 4 ILE A 197 ASN A 199 0
SHEET 2 AA6 4 ILE A 225 ASP A 231 -1 O ILE A 230 N GLY A 198
SHEET 3 AA6 4 ARG A 264 ILE A 270 -1 O GLY A 268 N PHE A 227
SHEET 4 AA6 4 ARG A 279 TRP A 280 -1 O ARG A 279 N VAL A 269
SHEET 1 AA7 2 VAL A 237 VAL A 243 0
SHEET 2 AA7 2 THR A 248 ARG A 254 -1 O VAL A 251 N ARG A 240
SHEET 1 AA8 4 ILE A 289 ASP A 298 0
SHEET 2 AA8 4 ARG A 301 SER A 308 -1 O THR A 303 N ASP A 295
SHEET 3 AA8 4 LYS A 313 THR A 320 -1 O ILE A 317 N PHE A 304
SHEET 4 AA8 4 GLN A 326 THR A 333 -1 O GLU A 332 N ILE A 314
SHEET 1 AA9 4 ARG A 345 PHE A 346 0
SHEET 2 AA9 4 PHE A 352 SER A 356 -1 O LEU A 353 N ARG A 345
SHEET 3 AA9 4 HIS A 363 ALA A 367 -1 O TYR A 365 N TRP A 354
SHEET 4 AA9 4 LEU A 374 ALA A 376 -1 O THR A 375 N VAL A 366
SHEET 1 AB1 4 VAL A 384 ASP A 391 0
SHEET 2 AB1 4 LEU A 396 GLY A 401 -1 O LEU A 396 N ASP A 391
SHEET 3 AB1 4 HIS A 410 PRO A 415 -1 O VAL A 414 N ALA A 397
SHEET 4 AB1 4 ARG A 422 ARG A 423 -1 O ARG A 422 N ALA A 413
SHEET 1 AB2 4 MET A 430 PHE A 435 0
SHEET 2 AB2 4 VAL A 441 SER A 448 -1 O VAL A 443 N THR A 434
SHEET 3 AB2 4 THR A 451 LYS A 459 -1 O GLN A 454 N TRP A 446
SHEET 4 AB2 4 LYS A 464 THR A 467 -1 O ALA A 466 N LEU A 457
SHEET 1 AB3 8 ALA A 491 THR A 496 0
SHEET 2 AB3 8 PRO A 503 ILE A 509 -1 O LEU A 504 N LEU A 495
SHEET 3 AB3 8 VAL A 557 LEU A 561 -1 O VAL A 558 N ILE A 509
SHEET 4 AB3 8 TYR A 520 PHE A 525 1 N PRO A 521 O VAL A 557
SHEET 5 AB3 8 VAL A 602 TRP A 612 1 O GLY A 608 N VAL A 522
SHEET 6 AB3 8 CYS A 632 GLY A 636 1 O GLY A 636 N GLY A 611
SHEET 7 AB3 8 LEU A 681 GLY A 686 1 O LEU A 682 N GLY A 633
SHEET 8 AB3 8 GLU A 712 TYR A 716 1 O GLU A 712 N LEU A 681
SHEET 1 AB4 4 LEU B 41 ILE B 46 0
SHEET 2 AB4 4 ARG B 52 GLY B 58 -1 O LEU B 56 N THR B 42
SHEET 3 AB4 4 ARG B 65 ASP B 72 -1 O TRP B 69 N PHE B 55
SHEET 4 AB4 4 THR B 78 VAL B 82 -1 O LEU B 81 N LEU B 68
SHEET 1 AB5 4 LEU B 41 ILE B 46 0
SHEET 2 AB5 4 ARG B 52 GLY B 58 -1 O LEU B 56 N THR B 42
SHEET 3 AB5 4 ARG B 65 ASP B 72 -1 O TRP B 69 N PHE B 55
SHEET 4 AB5 4 SER B 111 GLY B 112 1 O SER B 111 N LEU B 66
SHEET 1 AB6 4 GLN B 117 TRP B 118 0
SHEET 2 AB6 4 ALA B 124 LEU B 129 -1 O LEU B 126 N GLN B 117
SHEET 3 AB6 4 GLU B 132 ASP B 137 -1 O TYR B 134 N PHE B 127
SHEET 4 AB6 4 VAL B 146 LYS B 148 -1 O ARG B 147 N PHE B 135
SHEET 1 AB7 4 THR B 157 ILE B 161 0
SHEET 2 AB7 4 PHE B 167 ARG B 172 -1 O ILE B 171 N THR B 157
SHEET 3 AB7 4 ASN B 175 ASP B 180 -1 O ILE B 179 N VAL B 168
SHEET 4 AB7 4 GLU B 186 GLN B 188 -1 O VAL B 187 N ALA B 178
SHEET 1 AB8 3 ILE B 197 ASN B 199 0
SHEET 2 AB8 3 ILE B 225 ASP B 231 -1 O ILE B 230 N GLY B 198
SHEET 3 AB8 3 TYR B 216 TRP B 218 -1 N TRP B 217 O ALA B 226
SHEET 1 AB9 4 ILE B 197 ASN B 199 0
SHEET 2 AB9 4 ILE B 225 ASP B 231 -1 O ILE B 230 N GLY B 198
SHEET 3 AB9 4 ARG B 264 ILE B 270 -1 O GLY B 268 N PHE B 227
SHEET 4 AB9 4 ARG B 279 ILE B 281 -1 O ILE B 281 N LEU B 267
SHEET 1 AC1 2 VAL B 237 VAL B 243 0
SHEET 2 AC1 2 THR B 248 ARG B 254 -1 O VAL B 251 N ARG B 240
SHEET 1 AC2 4 ILE B 289 ASP B 298 0
SHEET 2 AC2 4 ARG B 301 SER B 308 -1 O GLN B 307 N TYR B 290
SHEET 3 AC2 4 LYS B 313 THR B 320 -1 O THR B 319 N LEU B 302
SHEET 4 AC2 4 THR B 325 THR B 333 -1 O GLU B 332 N ILE B 314
SHEET 1 AC3 4 ARG B 345 PHE B 346 0
SHEET 2 AC3 4 PHE B 352 SER B 356 -1 O LEU B 353 N ARG B 345
SHEET 3 AC3 4 HIS B 363 ALA B 367 -1 O ALA B 367 N PHE B 352
SHEET 4 AC3 4 LEU B 374 ALA B 376 -1 O THR B 375 N VAL B 366
SHEET 1 AC4 4 VAL B 384 ASP B 391 0
SHEET 2 AC4 4 LEU B 396 GLY B 401 -1 O LEU B 396 N ASP B 391
SHEET 3 AC4 4 HIS B 410 PRO B 415 -1 O TYR B 412 N VAL B 399
SHEET 4 AC4 4 ARG B 422 ARG B 423 -1 O ARG B 422 N ALA B 413
SHEET 1 AC5 4 MET B 430 PHE B 435 0
SHEET 2 AC5 4 VAL B 441 SER B 448 -1 O VAL B 443 N THR B 434
SHEET 3 AC5 4 THR B 451 LYS B 459 -1 O PHE B 458 N PHE B 442
SHEET 4 AC5 4 LYS B 464 THR B 467 -1 O LEU B 465 N LEU B 457
SHEET 1 AC6 8 THR B 490 THR B 496 0
SHEET 2 AC6 8 PRO B 503 ILE B 509 -1 O LEU B 508 N ALA B 491
SHEET 3 AC6 8 VAL B 557 LEU B 561 -1 O VAL B 558 N ILE B 509
SHEET 4 AC6 8 TYR B 520 PHE B 525 1 N PRO B 521 O VAL B 557
SHEET 5 AC6 8 VAL B 602 TRP B 612 1 O GLY B 608 N VAL B 522
SHEET 6 AC6 8 CYS B 632 GLY B 636 1 O GLY B 636 N GLY B 611
SHEET 7 AC6 8 LEU B 681 GLY B 686 1 O ILE B 684 N ALA B 635
SHEET 8 AC6 8 GLU B 712 TYR B 716 1 O GLU B 712 N LEU B 681
LINK OG SER A 613 C7 8YC A 801 1555 1555 1.43
LINK OG SER B 613 C7 8YC B 801 1555 1555 1.41
SITE 1 AC1 12 ARG A 106 GLU A 208 GLU A 209 TYR A 527
SITE 2 AC1 12 SER A 613 ASN A 614 VAL A 639 TYR A 645
SITE 3 AC1 12 TYR A 649 ASN A 691 VAL A 692 HOH A 979
SITE 1 AC2 6 ARG A 106 ILE A 107 ALA A 108 ALA A 109
SITE 2 AC2 6 ARG A 724 HOH A 963
SITE 1 AC3 6 SER A 543 ASP A 544 TRP A 612 GLY A 722
SITE 2 AC3 6 LEU A 723 ARG A 731
SITE 1 AC4 6 ARG B 106 ILE B 107 ALA B 108 ALA B 109
SITE 2 AC4 6 HOH B 906 HOH B1006
SITE 1 AC5 19 ARG B 106 GLU B 208 GLU B 209 TYR B 527
SITE 2 AC5 19 ALA B 531 TRP B 612 ASN B 614 GLY B 615
SITE 3 AC5 19 GLY B 616 TYR B 617 GLY B 636 ALA B 637
SITE 4 AC5 19 VAL B 639 TYR B 645 TYR B 649 ASN B 691
SITE 5 AC5 19 VAL B 692 HIS B 721 HOH B1012
CRYST1 59.880 120.220 231.890 90.00 90.00 90.00 P 21 21 21 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 0.016700 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008318 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004312 0.00000
TER 5661 PRO A 745
TER 11322 PRO B 745
MASTER 427 0 5 34 98 0 14 612078 2 60 116
END |