HEADER HYDROLASE 01-MAR-05 1Z0C
TITLE CRYSTAL STRUCTURE OF A. FULGIDUS LON PROTEOLYTIC DOMAIN D508A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PROTEASE LA HOMOLOG TYPE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEOLYTIC DOMAIN;
COMPND 5 EC: 3.4.21.53;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PRIL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJT12
KEYWDS ATP-DEPENDENT PROTEASE, CATALYTIC SER-LYS DYAD, B-TYPE LON, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.BOTOS,E.E.MELNIKOV,S.CHERRY,S.KOZLOV,O.V.MAKHOVSKAYA,J.E.TROPEA,
AUTHOR 2 A.GUSTCHINA,T.V.ROTANOVA,A.WLODAWER
REVDAT 5 14-FEB-24 1Z0C 1 REMARK
REVDAT 4 20-OCT-21 1Z0C 1 SEQADV
REVDAT 3 11-OCT-17 1Z0C 1 REMARK
REVDAT 2 24-FEB-09 1Z0C 1 VERSN
REVDAT 1 02-AUG-05 1Z0C 0
JRNL AUTH I.BOTOS,E.E.MELNIKOV,S.CHERRY,S.KOZLOV,O.V.MAKHOVSKAYA,
JRNL AUTH 2 J.E.TROPEA,A.GUSTCHINA,T.V.ROTANOVA,A.WLODAWER
JRNL TITL ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF THE PROTEOLYTIC
JRNL TITL 2 DOMAIN OF ARCHAEOGLOBUS FULGIDUS LON REVEALS THE
JRNL TITL 3 CONFORMATIONAL VARIABILITY IN THE ACTIVE SITES OF LON
JRNL TITL 4 PROTEASES
JRNL REF J.MOL.BIOL. V. 351 144 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16002085
JRNL DOI 10.1016/J.JMB.2005.06.008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.DAUTER,I.BOTOS,N.LARONDE-LEBLANC,A.WLODAWER
REMARK 1 TITL PATHOLOGICAL CRYSTALLOGRAPHY: CASE STUDIES OF SEVERAL
REMARK 1 TITL 2 UNUSUAL MACROMOLECULAR CRYSTALS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 61 967 2005
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 15983420
REMARK 1 DOI 10.1107/S0907444905011285
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 23366
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1181
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1600
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1500
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 141
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.22000
REMARK 3 B12 (A**2) : 0.07000
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): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.134
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1520 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2051 ; 1.760 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 198 ; 5.873 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 57 ;40.269 ;25.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 290 ;15.715 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 251 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1086 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 793 ; 0.237 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1066 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 143 ; 0.234 ; 0.200
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): 83 ; 0.247 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.296 ; 0.200
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): 1008 ; 1.481 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1596 ; 2.306 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 552 ; 3.207 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 455 ; 4.795 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 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 1Z0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, CALCIUM ACETATE, SODIUM
REMARK 280 CACODYLATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 27.66667
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 13.83333
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 20.75000
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 6.91667
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 34.58333
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 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 34.58333
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 27.66667
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 20.75000
REMARK 350 BIOMT1 5 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 13.83333
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 6.91667
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 ASP A 415
REMARK 465 SER A 454
REMARK 465 LYS A 455
REMARK 465 SER A 456
REMARK 465 ALA A 619
REMARK 465 ALA A 620
REMARK 465 VAL A 621
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 GLU A 542 O HOH A 110 1.23
REMARK 500 CD GLU A 542 O HOH A 110 2.12
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 SER A 438 10.38 -156.92
REMARK 500 LEU A 575 73.89 -102.50
REMARK 500 ASP A 577 -165.02 144.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z0B RELATED DB: PDB
REMARK 900 SAME PROTEIN E506A MUTANT
REMARK 900 RELATED ID: 1Z0E RELATED DB: PDB
REMARK 900 SAME PROTEIN MONOCLINIC FORM HEXAMER
REMARK 900 RELATED ID: 1Z0G RELATED DB: PDB
REMARK 900 SAME PROTEIN HEXAMER
REMARK 900 RELATED ID: 1Z0V RELATED DB: PDB
REMARK 900 SAME PROTEIN MONOCLINIC FORM DUAL LATTICE
REMARK 900 RELATED ID: 1Z0T RELATED DB: PDB
REMARK 900 SAME PROTEIN ORTHORHOMBIC FORM DUAL LATTICE
REMARK 900 RELATED ID: 1Z0W RELATED DB: PDB
REMARK 900 SAME PROTEIN
DBREF 1Z0C A 415 621 UNP O29883 LONH_ARCFU 415 621
SEQADV 1Z0C ALA A 508 UNP O29883 ASP 508 ENGINEERED MUTATION
SEQRES 1 A 207 ASP TYR LYS LEU PHE ILE THR GLU GLY TYR GLU VAL GLY
SEQRES 2 A 207 ARG VAL ASN GLY LEU ALA VAL ILE GLY GLU SER ALA GLY
SEQRES 3 A 207 ILE VAL LEU PRO ILE ILE ALA GLU VAL THR PRO SER MET
SEQRES 4 A 207 SER LYS SER GLU GLY ARG VAL ILE ALA THR GLY ARG LEU
SEQRES 5 A 207 GLN GLU ILE ALA ARG GLU ALA VAL MET ASN VAL SER ALA
SEQRES 6 A 207 ILE ILE LYS LYS TYR THR GLY ARG ASP ILE SER ASN MET
SEQRES 7 A 207 ASP VAL HIS ILE GLN PHE VAL GLY THR TYR GLU GLY VAL
SEQRES 8 A 207 GLU GLY ALA SER ALA SER ILE SER ILE ALA THR ALA VAL
SEQRES 9 A 207 ILE SER ALA ILE GLU GLY ILE PRO VAL ASP GLN SER VAL
SEQRES 10 A 207 ALA MET THR GLY SER LEU SER VAL LYS GLY GLU VAL LEU
SEQRES 11 A 207 PRO VAL GLY GLY VAL THR GLN LYS ILE GLU ALA ALA ILE
SEQRES 12 A 207 GLN ALA GLY LEU LYS LYS VAL ILE ILE PRO LYS ASP ASN
SEQRES 13 A 207 ILE ASP ASP VAL LEU LEU ASP ALA GLU HIS GLU GLY LYS
SEQRES 14 A 207 ILE GLU VAL ILE PRO VAL SER ARG ILE ASN GLU VAL LEU
SEQRES 15 A 207 GLU HIS VAL LEU GLU ASP GLY LYS LYS LYS ASN ARG LEU
SEQRES 16 A 207 MET SER LYS PHE LYS GLU LEU GLU LEU ALA ALA VAL
FORMUL 2 HOH *141(H2 O)
HELIX 1 1 LEU A 466 GLY A 486 1 21
HELIX 2 2 ASP A 488 SER A 490 5 3
HELIX 3 3 SER A 511 GLY A 524 1 14
HELIX 4 4 GLY A 548 ALA A 559 1 12
HELIX 5 5 ASP A 569 VAL A 574 5 6
HELIX 6 6 ARG A 591 LEU A 600 1 10
HELIX 7 7 GLY A 603 PHE A 613 1 11
HELIX 8 8 PHE A 613 LEU A 618 1 6
SHEET 1 A 2 TYR A 424 GLU A 425 0
SHEET 2 A 2 VAL A 527 ASP A 528 -1 O VAL A 527 N GLU A 425
SHEET 1 B 5 VAL A 460 ILE A 461 0
SHEET 2 B 5 MET A 492 PHE A 498 1 O VAL A 494 N ILE A 461
SHEET 3 B 5 ALA A 439 PRO A 451 -1 N THR A 450 O ASP A 493
SHEET 4 B 5 ARG A 428 ILE A 435 -1 N VAL A 429 O ILE A 445
SHEET 5 B 5 VAL A 505 GLU A 506 -1 O GLU A 506 N VAL A 434
SHEET 1 C 7 VAL A 460 ILE A 461 0
SHEET 2 C 7 MET A 492 PHE A 498 1 O VAL A 494 N ILE A 461
SHEET 3 C 7 ALA A 439 PRO A 451 -1 N THR A 450 O ASP A 493
SHEET 4 C 7 ARG A 428 ILE A 435 -1 N VAL A 429 O ILE A 445
SHEET 5 C 7 VAL A 531 MET A 533 1 O MET A 533 N ASN A 430
SHEET 6 C 7 LYS A 563 PRO A 567 1 O ILE A 565 N ALA A 532
SHEET 7 C 7 GLU A 585 VAL A 589 1 O ILE A 587 N VAL A 564
SHEET 1 D 2 SER A 536 LEU A 537 0
SHEET 2 D 2 VAL A 543 LEU A 544 -1 O LEU A 544 N SER A 536
CISPEP 1 GLU A 581 GLY A 582 0 -1.19
CRYST1 81.960 81.960 41.500 90.00 90.00 120.00 P 65 6
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 0.012201 0.007044 0.000000 0.00000
SCALE2 0.000000 0.014089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
