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HEADER HYDROLASE 09-NOV-12 4HXE
TITLE PYROCOCCUS HORIKOSHII ACYLAMINOACYL PEPTIDASE (UNCOMPLEXED)
CAVEAT 4HXE CHIRALITY ERROR B372
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN PH0594;
COMPND 3 CHAIN: B;
COMPND 4 EC: 3.4.19.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
SOURCE 5 GENE: PH0594;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS SELF-COMPARTMENTALIZATION, BETA-PROPELLER, ALPHA/BETA HYRDOLASE FOLD,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.TICHY-RACS,B.HORNUNG,K.RADI,D.K.MENYHARD,A.KISS-SZEMAN,Z.SZELTNER,
AUTHOR 2 K.DOMOKOS,I.SZAMOSI,G.NARAY-SZABO,L.POLGAR,V.HARMAT
REVDAT 2 15-MAY-13 4HXE 1 JRNL
REVDAT 1 08-MAY-13 4HXE 0
JRNL AUTH D.K.MENYHARD,A.KISS-SZEMAN,E.TICHY-RACS,B.HORNUNG,K.RADI,
JRNL AUTH 2 Z.SZELTNER,K.DOMOKOS,I.SZAMOSI,G.NARAY-SZABO,L.POLGAR,
JRNL AUTH 3 V.HARMAT
JRNL TITL A SELF-COMPARTMENTALIZING HEXAMER SERINE PROTEASE FROM
JRNL TITL 2 PYROCOCCUS HORIKOSHII - SUBSTRATE SELECTION ACHIEVED THROUGH
JRNL TITL 3 MULTIMERIZATION.
JRNL REF J.BIOL.CHEM. 2013
JRNL REFN ESSN 1083-351X
JRNL PMID 23632025
JRNL DOI 10.1074/JBC.M113.451534
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.SZELTNER,A.L.KISS,K.DOMOKOS,V.HARMAT,G.NARAY-SZABO,
REMARK 1 AUTH 2 L.POLGAR
REMARK 1 TITL CHARACTERIZATION OF A NOVEL ACYLAMINOACYL PEPTIDASE WITH
REMARK 1 TITL 2 HEXAMERIC STRUCTURE AND ENDOPEPTIDASE ACTIVITY.
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1794 1204 2009
REMARK 1 REFN ISSN 0006-3002
REMARK 1 PMID 19303951
REMARK 1 DOI 10.1016/J.BBAPAP.2009.03.004
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 64801
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3425
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) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3359
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4959
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 395
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.00000
REMARK 3 B22 (A**2) : -0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.808
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5275 ; 0.018 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7130 ; 1.944 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 641 ; 7.388 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;36.397 ;23.640
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 916 ;15.731 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;19.616 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 731 ; 0.155 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4061 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 346
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9073 -4.7501 43.1027
REMARK 3 T TENSOR
REMARK 3 T11: 0.0195 T22: 0.0424
REMARK 3 T33: 0.0113 T12: 0.0062
REMARK 3 T13: 0.0049 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.3170 L22: 0.2700
REMARK 3 L33: 0.1476 L12: -0.0201
REMARK 3 L13: 0.0438 L23: -0.0060
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: 0.0460 S13: -0.0196
REMARK 3 S21: -0.0341 S22: -0.0068 S23: 0.0089
REMARK 3 S31: 0.0227 S32: -0.0002 S33: -0.0064
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 347 B 618
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2003 14.7802 58.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0105 T22: 0.0052
REMARK 3 T33: 0.0162 T12: -0.0056
REMARK 3 T13: 0.0008 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.3759 L22: 0.3363
REMARK 3 L33: 0.5945 L12: -0.0393
REMARK 3 L13: -0.0055 L23: -0.1069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0125 S13: 0.0477
REMARK 3 S21: -0.0040 S22: -0.0047 S23: -0.0329
REMARK 3 S31: -0.0751 S32: 0.0412 S33: 0.0058
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 4HXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-12.
REMARK 100 THE RCSB ID CODE IS RCSB076039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-05; 23-MAR-06; 03-MAR-06;
REMARK 200 29-JUN-06; 29-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100; 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; N; N; Y; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE; ROTATING ANODE;
REMARK 200 ROTATING ANODE; EMBL/DESY,
REMARK 200 HAMBURG; ESRF
REMARK 200 BEAMLINE : NULL; NULL; NULL; X11; BM14
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200; RIGAKU RU200;
REMARK 200 RIGAKU RU200; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 1.5418; 1.5418; 0.8162;
REMARK 200 1.0715
REMARK 200 MONOCHROMATOR : GRAPHITE; GRAPHITE; GRAPHITE;
REMARK 200 SI(111); SI(111)
REMARK 200 OPTICS : NULL; NULL; NULL; MIRRORS;
REMARK 200 MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE; IMAGE
REMARK 200 PLATE; CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC; RIGAKU RAXIS
REMARK 200 IIC; RIGAKU RAXIS IIC; MAR CCD
REMARK 200 165 MM; MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69738
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 8.320
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.84
REMARK 200 R MERGE FOR SHELL (I) : 0.68600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE
REMARK 200 WAVELENGTH; MAD; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SHELX, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M 1,6-HEXANEDIOL, 0.20 M MGCL2,
REMARK 280 0.1 M TRIS/HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 91.50000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.82755
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 48.21000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 91.50000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 52.82755
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 48.21000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 91.50000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 52.82755
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 48.21000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 91.50000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 52.82755
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 48.21000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 91.50000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 52.82755
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 48.21000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 91.50000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 52.82755
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 48.21000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 105.65510
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 96.42000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 105.65510
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 96.42000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 105.65510
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 96.42000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 105.65510
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 96.42000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 105.65510
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 96.42000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 105.65510
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 96.42000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 39250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 119740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 144.63000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 144.63000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 144.63000
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 B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 ILE B 4
REMARK 465 GLU B 51
REMARK 465 GLU B 80
REMARK 465 GLU B 81
REMARK 465 LYS B 82
REMARK 465 LYS B 83
REMARK 465 LYS B 373
REMARK 465 GLU B 374
REMARK 465 GLY B 375
REMARK 465 GLU B 619
REMARK 465 GLU B 620
REMARK 465 LYS B 621
REMARK 465 LYS B 622
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU B 5 CG CD OE1 OE2
REMARK 470 LYS B 13 NZ
REMARK 470 ARG B 23 CZ NH1 NH2
REMARK 470 LYS B 40 CE NZ
REMARK 470 LYS B 71 CE NZ
REMARK 470 LYS B 93 CG CD CE NZ
REMARK 470 LYS B 99 CE NZ
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LYS B 124 CE NZ
REMARK 470 PRO B 235 CG CD
REMARK 470 LYS B 245 CG CD CE NZ
REMARK 470 ARG B 270 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 271 CG OD1 ND2
REMARK 470 LYS B 273 CE NZ
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 LYS B 298 NZ
REMARK 470 GLU B 331 OE1 OE2
REMARK 470 ARG B 333 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 344 CE NZ
REMARK 470 LYS B 345 CE NZ
REMARK 470 GLU B 371 CG CD OE1 OE2
REMARK 470 GLU B 376 CG CD OE1 OE2
REMARK 470 LYS B 377 CE NZ
REMARK 470 GLU B 446 CG CD OE1 OE2
REMARK 470 ASP B 480 CG OD1 OD2
REMARK 470 LYS B 524 CD CE NZ
REMARK 470 LYS B 535 CE NZ
REMARK 470 LYS B 575 CE NZ
REMARK 470 LYS B 606 CE NZ
REMARK 470 GLU B 614 CG CD OE1 OE2
REMARK 470 LYS B 615 CD CE NZ
REMARK 470 LYS B 618 CG CD CE NZ
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 OD1 ASP B 191 O HOH B 1111 1.89
REMARK 500 O ASN B 25 O ASN B 49 2.02
REMARK 500 OH TYR B 412 O HOH B 994 2.08
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 111 CE2 TRP B 111 CD2 0.077
REMARK 500 TRP B 200 CE2 TRP B 200 CD2 0.073
REMARK 500 TRP B 289 CE2 TRP B 289 CD2 0.077
REMARK 500 HIS B 301 CG HIS B 301 CD2 0.062
REMARK 500 HIS B 385 CG HIS B 385 CD2 0.064
REMARK 500 TRP B 506 CE2 TRP B 506 CD2 0.076
REMARK 500 HIS B 559 CG HIS B 559 CD2 0.063
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 ILE B 372 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 ILE B 372 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASP B 437 CB - CG - OD1 ANGL. DEV. = 6.1 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 LYS B 24 -125.73 42.08
REMARK 500 ALA B 103 78.97 -119.07
REMARK 500 ASN B 105 36.04 70.02
REMARK 500 ASP B 136 -161.73 -120.82
REMARK 500 ASP B 191 -119.94 -106.14
REMARK 500 ASP B 261 58.61 -100.17
REMARK 500 ASP B 309 -105.84 -149.23
REMARK 500 ASP B 337 51.61 -147.63
REMARK 500 ILE B 359 -110.31 60.31
REMARK 500 LYS B 389 40.79 -76.48
REMARK 500 LEU B 435 -101.46 -92.79
REMARK 500 SER B 466 -122.79 75.72
REMARK 500 ALA B 577 -159.80 -92.39
REMARK 500 PHE B 611 76.44 -164.72
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 B 329 GLY B 330 -59.69
REMARK 500 GLU B 371 ILE B 372 42.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU B 37 24.6 L L OUTSIDE RANGE
REMARK 500 ASN B 49 24.6 L L OUTSIDE RANGE
REMARK 500 ILE B 372 6.6 L L EXPECTING SP3
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 B1151 DISTANCE = 5.02 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1037 O
REMARK 620 2 LYS B 99 O 89.1
REMARK 620 3 GLU B 162 OE1 174.1 86.0
REMARK 620 4 HOH B 875 O 94.3 85.6 88.7
REMARK 620 5 HOH B1039 O 89.8 95.9 87.3 175.7
REMARK 620 6 HOH B1038 O 92.0 168.9 93.4 83.3 95.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 911 O
REMARK 620 2 HOH B 858 O 95.7
REMARK 620 3 HOH B1040 O 100.2 87.2
REMARK 620 4 HOH B 937 O 174.5 83.8 85.3
REMARK 620 5 HOH B 904 O 94.4 169.9 90.6 86.2
REMARK 620 6 ASP B 424 OD1 83.5 91.1 176.0 91.0 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 244 OD2
REMARK 620 2 HOH B 834 O 169.0
REMARK 620 3 GLU B 263 OE2 102.8 85.8
REMARK 620 4 HOH B 936 O 81.0 91.6 94.5
REMARK 620 5 HOH B 887 O 101.6 86.0 83.2 176.8
REMARK 620 6 HOH B 902 O 85.9 86.9 167.2 96.1 85.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 709
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HXF RELATED DB: PDB
REMARK 900 RELATED ID: 4HXG RELATED DB: PDB
DBREF 4HXE B 1 622 UNP O58323 O58323_PYRHO 1 622
SEQRES 1 B 622 MET THR SER ILE GLU TRP ASP GLU LYS THR PHE THR LYS
SEQRES 2 B 622 PHE ALA TYR LEU SER ASP PRO ARG THR ARG LYS ASN LEU
SEQRES 3 B 622 VAL ALA TYR VAL LEU THR LYS ALA ASN LEU GLU SER ASN
SEQRES 4 B 622 LYS TYR GLU ASN THR ILE VAL ILE GLU ASN LEU GLU ASP
SEQRES 5 B 622 GLY SER ARG LYS PHE ILE GLU ASP ALA SER MET PRO ARG
SEQRES 6 B 622 ILE SER PRO ASP GLY LYS LYS ILE ALA PHE MET ARG PHE
SEQRES 7 B 622 ASN GLU GLU LYS LYS THR ALA GLN ILE TRP VAL ALA ASP
SEQRES 8 B 622 LEU LYS THR LEU SER ALA LYS LYS VAL LEU GLU ALA LYS
SEQRES 9 B 622 ASN ILE ARG SER ILE GLU TRP ASN GLN ASP SER ARG ARG
SEQRES 10 B 622 LEU LEU ALA VAL GLY PHE LYS ARG ARG GLU ASP GLU ASP
SEQRES 11 B 622 PHE ILE PHE GLU ASP ASP VAL PRO ALA TRP PHE ASP ASN
SEQRES 12 B 622 MET GLY PHE PHE ASP GLY GLU LYS THR THR PHE TRP VAL
SEQRES 13 B 622 ILE ASP THR GLU GLY GLU GLU VAL ILE GLU GLN PHE GLU
SEQRES 14 B 622 LYS PRO ARG PHE SER SER GLY ILE TRP HIS GLY ASP SER
SEQRES 15 B 622 ILE VAL VAL SER VAL PRO HIS ARG ASP VAL ILE PRO ARG
SEQRES 16 B 622 TYR PHE LYS TYR TRP ASP ILE TYR LEU TRP LYS ASP GLY
SEQRES 17 B 622 GLU GLU GLU LYS LEU PHE GLU LYS VAL SER PHE TYR ALA
SEQRES 18 B 622 ILE ASP SER ASP GLY GLU ARG ILE LEU LEU TYR GLY LYS
SEQRES 19 B 622 PRO GLU LYS LYS TYR VAL SER GLU HIS ASP LYS ILE TYR
SEQRES 20 B 622 ILE TYR ASP GLY GLU VAL LYS GLY ILE LEU ASP ASP ILE
SEQRES 21 B 622 ASP ARG GLU VAL ALA GLN ALA LYS ILE ARG ASN GLY LYS
SEQRES 22 B 622 VAL TYR PHE THR LEU PHE GLU GLU GLY SER VAL ASN LEU
SEQRES 23 B 622 TYR LEU TRP ASP GLY GLU VAL ARG GLU ILE ALA LYS GLY
SEQRES 24 B 622 LYS HIS TRP ILE MET GLY PHE ASP ALA ASP GLU ARG LEU
SEQRES 25 B 622 ILE TYR LEU LYS GLU THR ALA THR ARG PRO ALA GLU LEU
SEQRES 26 B 622 TYR LEU TRP ASP GLY GLU GLU ARG GLN LEU THR ASP TYR
SEQRES 27 B 622 ASN GLY LEU ILE PHE LYS LYS LEU LYS THR PHE GLU PRO
SEQRES 28 B 622 ARG HIS PHE ARG PHE LYS SER ILE ASP LEU GLU LEU ASP
SEQRES 29 B 622 GLY TRP TYR ILE LYS PRO GLU ILE LYS GLU GLY GLU LYS
SEQRES 30 B 622 ALA PRO VAL ILE VAL PHE VAL HIS GLY GLY PRO LYS GLY
SEQRES 31 B 622 MET TYR GLY TYR TYR PHE LYS TYR GLU MET GLN LEU MET
SEQRES 32 B 622 ALA SER LYS GLY TYR TYR ILE VAL TYR VAL ASN PRO ARG
SEQRES 33 B 622 GLY SER ASN GLY TYR SER GLU ASP PHE ALA LEU ARG VAL
SEQRES 34 B 622 LEU GLU ARG THR GLY LEU GLU ASP PHE GLN ASP ILE LEU
SEQRES 35 B 622 ASN GLY ILE GLU GLU PHE LEU ARG LEU GLU PRO GLN ALA
SEQRES 36 B 622 ASP ARG GLU ARG ILE GLY ILE THR GLY ILE SER TYR GLY
SEQRES 37 B 622 GLY TYR MET THR ASN TRP ALA LEU THR GLN SER ASP LEU
SEQRES 38 B 622 PHE LYS ALA GLY ILE SER GLU ASN GLY ILE SER TYR TRP
SEQRES 39 B 622 LEU THR SER TYR ALA PHE SER ASP ILE GLY LEU TRP PHE
SEQRES 40 B 622 ASP LYS GLU VAL ILE GLY ASP ASN PRO LEU GLU ASN GLU
SEQRES 41 B 622 ASN TYR ARG LYS LEU SER PRO LEU PHE TYR ALA LYS ASN
SEQRES 42 B 622 VAL LYS ALA PRO LEU LEU LEU ILE HIS SER LEU GLU ASP
SEQRES 43 B 622 TYR ARG CYS PRO LEU ASP GLN SER LEU MET PHE TYR HIS
SEQRES 44 B 622 VAL LEU LYS ASP LEU GLY LYS GLU VAL TYR ILE ALA ILE
SEQRES 45 B 622 PHE LYS LYS GLY ALA HIS GLY HIS SER ILE ARG GLY SER
SEQRES 46 B 622 PRO ARG HIS ARG MET LYS ARG TYR LYS LEU PHE MET GLU
SEQRES 47 B 622 PHE PHE GLU ARG LYS LEU LYS LYS TYR GLU GLU GLY PHE
SEQRES 48 B 622 ASP VAL GLU LYS ILE LEU LYS GLU GLU LYS LYS
HET MG B 701 1
HET MG B 702 1
HET MG B 703 1
HET HEZ B 704 8
HET HEZ B 705 8
HET HEZ B 706 8
HET HEZ B 707 8
HET HEZ B 708 8
HET HEZ B 709 8
HETNAM MG MAGNESIUM ION
HETNAM HEZ HEXANE-1,6-DIOL
FORMUL 2 MG 3(MG 2+)
FORMUL 5 HEZ 6(C6 H14 O2)
FORMUL 11 HOH *395(H2 O)
HELIX 1 1 LYS B 9 PHE B 14 5 6
HELIX 2 2 ASN B 339 LYS B 344 1 6
HELIX 3 3 LYS B 397 LYS B 406 1 10
HELIX 4 4 SER B 422 ARG B 428 1 7
HELIX 5 5 LEU B 435 GLU B 452 1 18
HELIX 6 6 SER B 466 SER B 479 1 14
HELIX 7 7 TYR B 493 SER B 501 1 9
HELIX 8 8 ILE B 503 ILE B 512 1 10
HELIX 9 9 GLU B 520 LEU B 525 1 6
HELIX 10 10 SER B 526 VAL B 534 5 9
HELIX 11 11 LEU B 551 LEU B 564 1 14
HELIX 12 12 GLY B 579 GLY B 584 1 6
HELIX 13 13 SER B 585 LEU B 604 1 20
HELIX 14 14 ASP B 612 LYS B 618 1 7
SHEET 1 A 4 TYR B 16 ARG B 23 0
SHEET 2 A 4 LEU B 26 ASN B 35 -1 O VAL B 30 N SER B 18
SHEET 3 A 4 LYS B 40 GLU B 48 -1 O THR B 44 N LEU B 31
SHEET 4 A 4 ARG B 55 GLU B 59 -1 O ILE B 58 N ILE B 45
SHEET 1 B 4 SER B 62 ILE B 66 0
SHEET 2 B 4 LYS B 72 ARG B 77 -1 O ALA B 74 N ARG B 65
SHEET 3 B 4 GLN B 86 ASP B 91 -1 O ALA B 90 N ILE B 73
SHEET 4 B 4 ALA B 97 GLU B 102 -1 O LEU B 101 N ILE B 87
SHEET 1 C 4 ILE B 106 TRP B 111 0
SHEET 2 C 4 ARG B 117 LYS B 124 -1 O VAL B 121 N ARG B 107
SHEET 3 C 4 LYS B 151 ASP B 158 -1 O ILE B 157 N LEU B 118
SHEET 4 C 4 VAL B 164 LYS B 170 -1 O ILE B 165 N VAL B 156
SHEET 1 D 2 TRP B 140 PHE B 141 0
SHEET 2 D 2 GLY B 145 PHE B 146 -1 O GLY B 145 N PHE B 141
SHEET 1 E 7 SER B 175 HIS B 179 0
SHEET 2 E 7 SER B 182 PRO B 188 -1 O SER B 182 N HIS B 179
SHEET 3 E 7 TRP B 200 LYS B 206 -1 O ASP B 201 N VAL B 187
SHEET 4 E 7 GLU B 209 SER B 224 -1 O LEU B 213 N ILE B 202
SHEET 5 E 7 ILE B 229 LYS B 234 -1 O LEU B 230 N ASP B 223
SHEET 6 E 7 LYS B 245 TYR B 249 -1 O TYR B 247 N LEU B 231
SHEET 7 E 7 VAL B 253 GLY B 255 -1 O LYS B 254 N ILE B 248
SHEET 1 F 4 GLU B 263 ARG B 270 0
SHEET 2 F 4 LYS B 273 GLU B 280 -1 O LYS B 273 N ARG B 270
SHEET 3 F 4 SER B 283 TRP B 289 -1 O TYR B 287 N PHE B 276
SHEET 4 F 4 VAL B 293 ALA B 297 -1 O ARG B 294 N LEU B 288
SHEET 1 G 4 TRP B 302 ALA B 308 0
SHEET 2 G 4 LEU B 312 GLU B 317 -1 O GLU B 317 N TRP B 302
SHEET 3 G 4 GLU B 324 TRP B 328 -1 O GLU B 324 N LYS B 316
SHEET 4 G 4 GLU B 332 GLN B 334 -1 O ARG B 333 N LEU B 327
SHEET 1 H 8 ARG B 352 SER B 358 0
SHEET 2 H 8 LEU B 361 ILE B 368 -1 O TYR B 367 N ARG B 352
SHEET 3 H 8 TYR B 409 VAL B 413 -1 O ILE B 410 N ILE B 368
SHEET 4 H 8 ALA B 378 VAL B 384 1 N ILE B 381 O TYR B 409
SHEET 5 H 8 ALA B 455 ILE B 465 1 O GLY B 461 N VAL B 380
SHEET 6 H 8 ALA B 484 GLU B 488 1 O GLU B 488 N GLY B 464
SHEET 7 H 8 LEU B 538 SER B 543 1 O LEU B 539 N SER B 487
SHEET 8 H 8 VAL B 568 PHE B 573 1 O TYR B 569 N LEU B 540
LINK MG MG B 703 O HOH B1037 1555 1555 2.03
LINK O LYS B 99 MG MG B 703 1555 1555 2.08
LINK OE1 GLU B 162 MG MG B 703 1555 1555 2.08
LINK MG MG B 702 O HOH B 911 1555 1555 2.10
LINK MG MG B 703 O HOH B 875 1555 1555 2.11
LINK MG MG B 702 O HOH B 858 1555 1555 2.11
LINK OD2 ASP B 244 MG MG B 701 1555 1555 2.11
LINK MG MG B 703 O HOH B1039 1555 1555 2.11
LINK MG MG B 702 O HOH B1040 1555 1555 2.12
LINK MG MG B 703 O HOH B1038 1555 1555 2.12
LINK MG MG B 701 O HOH B 834 1555 1555 2.13
LINK MG MG B 702 O HOH B 937 1555 1555 2.14
LINK MG MG B 702 O HOH B 904 1555 1555 2.17
LINK OE2 GLU B 263 MG MG B 701 1555 1555 2.21
LINK MG MG B 701 O HOH B 936 1555 1555 2.21
LINK OD1 ASP B 424 MG MG B 702 1555 1555 2.22
LINK MG MG B 701 O HOH B 887 1555 1555 2.22
LINK MG MG B 701 O HOH B 902 1555 1555 2.30
CISPEP 1 VAL B 137 PRO B 138 0 -9.37
CISPEP 2 GLY B 387 PRO B 388 0 4.55
SITE 1 AC1 6 ASP B 244 GLU B 263 HOH B 834 HOH B 887
SITE 2 AC1 6 HOH B 902 HOH B 936
SITE 1 AC2 6 ASP B 424 HOH B 858 HOH B 904 HOH B 911
SITE 2 AC2 6 HOH B 937 HOH B1040
SITE 1 AC3 6 LYS B 99 GLU B 162 HOH B 875 HOH B1037
SITE 2 AC3 6 HOH B1038 HOH B1039
SITE 1 AC4 7 LYS B 316 ARG B 321 PRO B 322 GLU B 324
SITE 2 AC4 7 TYR B 326 GLN B 334 HEZ B 707
SITE 1 AC5 5 TYR B 239 ASP B 424 GLU B 431 HOH B 882
SITE 2 AC5 5 HOH B 937
SITE 1 AC6 5 TYR B 16 TYR B 41 ILE B 582 ARG B 583
SITE 2 AC6 5 ARG B 589
SITE 1 AC7 3 GLN B 334 LEU B 335 HEZ B 704
SITE 1 AC8 3 LYS B 535 TYR B 607 HOH B1005
SITE 1 AC9 7 GLY B 387 SER B 466 TYR B 467 SER B 497
SITE 2 AC9 7 SER B 501 PHE B 507 ARG B 548
CRYST1 183.000 183.000 144.630 90.00 90.00 120.00 H 3 2 18
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 0.005464 0.003155 0.000000 0.00000
SCALE2 0.000000 0.006310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006914 0.00000
TER 5083 LYS B 618
MASTER 635 0 9 14 37 0 16 6 5405 1 72 48
END |