HEADER HYDROLASE 28-MAY-14 4QHJ
TITLE CRYSTAL STRUCTURE OF METHANOCALDOCOCCUS JANNASCHII SELECASE MUTANT
TITLE 2 I100F+H107F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN MJ1213;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 243232;
SOURCE 4 STRAIN: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
SOURCE 5 GENE: MJ1213;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS MINIGLUZINCIN, PROTEOLYTIC ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LOPEZ-PELEGRIN,N.CERDA-COSTA,A.CINTAS-PEDROLA,F.HERRANZ-TRILLO,
AUTHOR 2 P.BERNADO,J.R.PEINADO,J.L.AROLAS,F.X.GOMIS-RUTH
REVDAT 4 03-APR-24 4QHJ 1 REMARK
REVDAT 3 20-MAR-24 4QHJ 1 REMARK SEQADV LINK
REVDAT 2 22-OCT-14 4QHJ 1 JRNL
REVDAT 1 16-JUL-14 4QHJ 0
JRNL AUTH M.LOPEZ-PELEGRIN,N.CERDA-COSTA,A.CINTAS-PEDROLA,
JRNL AUTH 2 F.HERRANZ-TRILLO,P.BERNADO,J.R.PEINADO,J.L.AROLAS,
JRNL AUTH 3 F.X.GOMIS-RUTH
JRNL TITL MULTIPLE STABLE CONFORMATIONS ACCOUNT FOR REVERSIBLE
JRNL TITL 2 CONCENTRATION-DEPENDENT OLIGOMERIZATION AND AUTOINHIBITION
JRNL TITL 3 OF A METAMORPHIC METALLOPEPTIDASE
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 53 10624 2014
JRNL REFN ISSN 1433-7851
JRNL PMID 25159620
JRNL DOI 10.1002/ANIE.201405727
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 26632
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.810
REMARK 3 FREE R VALUE TEST SET COUNT : 749
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.85
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2806
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2465
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2729
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE : 0.1960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.74
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 749
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 : 1818
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11930
REMARK 3 B22 (A**2) : -2.48830
REMARK 3 B33 (A**2) : 2.60760
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.239
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.112
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1920 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2580 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 955 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 57 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 264 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1920 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 261 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2470 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.52
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.99
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1 - A|108 A|201 - A|201 }
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9164 16.5280 5.6956
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.0515
REMARK 3 T33: 0.0424 T12: 0.0198
REMARK 3 T13: -0.0057 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.6668 L22: 0.3540
REMARK 3 L33: 2.5876 L12: 0.1212
REMARK 3 L13: 1.2085 L23: -0.0595
REMARK 3 S TENSOR
REMARK 3 S11: -0.1206 S12: -0.1158 S13: 0.1673
REMARK 3 S21: 0.0467 S22: 0.0067 S23: 0.0626
REMARK 3 S31: -0.2052 S32: -0.2038 S33: 0.1139
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|1 - B|108 B|201 - B|201 }
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8522 33.5666 19.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0932 T22: -0.0085
REMARK 3 T33: -0.0073 T12: 0.0150
REMARK 3 T13: -0.0669 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.2230 L22: 3.0604
REMARK 3 L33: 0.7248 L12: -0.0901
REMARK 3 L13: 0.3094 L23: 0.4669
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: 0.1089 S13: 0.0600
REMARK 3 S21: -0.4381 S22: -0.0912 S23: 0.2397
REMARK 3 S31: -0.0732 S32: -0.0435 S33: 0.0777
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-14
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 : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26633
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 52.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 52.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.05400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 24.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: DIMERIC SELECASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, 1M SODIUM
REMARK 280 ACETATE TRIHYDRATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 24.69500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.42000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.42000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.69500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.92000
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: 3650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 LYS A 109
REMARK 465 LYS A 110
REMARK 465 LYS B 109
REMARK 465 LYS B 110
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 THR B 44 -29.20 -141.79
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 HIS A 73 NE2 97.8
REMARK 620 3 HIS A 80 NE2 109.0 109.0
REMARK 620 4 ACT A 202 O 103.1 115.3 119.9
REMARK 620 5 ACT A 202 OXT 158.1 91.9 86.1 55.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 69 NE2
REMARK 620 2 HIS B 73 NE2 106.8
REMARK 620 3 HIS B 80 NE2 106.0 104.6
REMARK 620 4 ACT B 202 OXT 101.8 119.9 116.4
REMARK 620 5 ACT B 202 O 157.5 87.1 86.7 55.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JIU RELATED DB: PDB
REMARK 900 PYROCOCCUS ABYSSI ABYLYSIN
REMARK 900 RELATED ID: 4JIX RELATED DB: PDB
REMARK 900 METHANOCALDOCOCCUS JANNASCHII JANNALYSIN
REMARK 900 RELATED ID: 4QHF RELATED DB: PDB
REMARK 900 METHANOCALDOCOCCUS JANNASCHII MONOMERIC SELECASE
REMARK 900 RELATED ID: 4QHG RELATED DB: PDB
REMARK 900 METHANOCALDOCOCCUS JANNASCHII DIMERIC SELECASE
REMARK 900 RELATED ID: 4QHH RELATED DB: PDB
REMARK 900 METHANOCALDOCOCCUS JANNASCHII TETRAMERIC SELECASE
REMARK 900 RELATED ID: 4QHI RELATED DB: PDB
REMARK 900 METHANOCALDOCOCCUS JANNASCHII SELECASE MUTANT R36W
DBREF 4QHJ A 1 110 UNP Q58610 Y1213_METJA 1 110
DBREF 4QHJ B 1 110 UNP Q58610 Y1213_METJA 1 110
SEQADV 4QHJ PHE A 100 UNP Q58610 ILE 100 ENGINEERED MUTATION
SEQADV 4QHJ PHE A 107 UNP Q58610 HIS 107 ENGINEERED MUTATION
SEQADV 4QHJ PHE B 100 UNP Q58610 ILE 100 ENGINEERED MUTATION
SEQADV 4QHJ PHE B 107 UNP Q58610 HIS 107 ENGINEERED MUTATION
SEQRES 1 A 110 MET LYS ASP ARG LYS ILE LEU ASN GLU ILE LEU SER ASN
SEQRES 2 A 110 THR ILE ASN GLU LEU ASN LEU ASN ASP LYS LYS ALA ASN
SEQRES 3 A 110 ILE LYS ILE LYS ILE LYS PRO LEU LYS ARG LYS ILE ALA
SEQRES 4 A 110 SER ILE SER LEU THR ASN LYS THR ILE TYR ILE ASN LYS
SEQRES 5 A 110 ASN ILE LEU PRO TYR LEU SER ASP GLU GLU ILE ARG PHE
SEQRES 6 A 110 ILE LEU ALA HIS GLU LEU LEU HIS LEU LYS TYR GLY LYS
SEQRES 7 A 110 TYR HIS ILE ASN GLU PHE GLU GLU GLU LEU LEU PHE LEU
SEQRES 8 A 110 PHE PRO ASN LYS GLU ALA ILE LEU PHE ASN LEU ILE ASN
SEQRES 9 A 110 LYS LEU PHE GLN LYS LYS
SEQRES 1 B 110 MET LYS ASP ARG LYS ILE LEU ASN GLU ILE LEU SER ASN
SEQRES 2 B 110 THR ILE ASN GLU LEU ASN LEU ASN ASP LYS LYS ALA ASN
SEQRES 3 B 110 ILE LYS ILE LYS ILE LYS PRO LEU LYS ARG LYS ILE ALA
SEQRES 4 B 110 SER ILE SER LEU THR ASN LYS THR ILE TYR ILE ASN LYS
SEQRES 5 B 110 ASN ILE LEU PRO TYR LEU SER ASP GLU GLU ILE ARG PHE
SEQRES 6 B 110 ILE LEU ALA HIS GLU LEU LEU HIS LEU LYS TYR GLY LYS
SEQRES 7 B 110 TYR HIS ILE ASN GLU PHE GLU GLU GLU LEU LEU PHE LEU
SEQRES 8 B 110 PHE PRO ASN LYS GLU ALA ILE LEU PHE ASN LEU ILE ASN
SEQRES 9 B 110 LYS LEU PHE GLN LYS LYS
HET ZN A 201 1
HET ACT A 202 4
HET ACT A 203 4
HET ACT A 204 4
HET ZN B 201 1
HET ACT B 202 4
HET ACT B 203 4
HET GOL B 204 6
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 ACT 5(C2 H3 O2 1-)
FORMUL 10 GOL C3 H8 O3
FORMUL 11 HOH *251(H2 O)
HELIX 1 1 ASP A 3 LEU A 18 1 16
HELIX 2 2 LEU A 20 LYS A 24 5 5
HELIX 3 3 ILE A 54 LEU A 58 5 5
HELIX 4 4 SER A 59 GLY A 77 1 19
HELIX 5 5 ILE A 81 PHE A 92 1 12
HELIX 6 6 ASN A 94 PHE A 107 1 14
HELIX 7 7 ASP B 3 LEU B 18 1 16
HELIX 8 8 LEU B 20 LYS B 24 5 5
HELIX 9 9 ILE B 54 LEU B 58 5 5
HELIX 10 10 SER B 59 GLY B 77 1 19
HELIX 11 11 ILE B 81 PHE B 92 1 12
HELIX 12 12 ASN B 94 GLN B 108 1 15
SHEET 1 A 3 LYS A 28 LYS A 32 0
SHEET 2 A 3 THR A 47 ASN A 51 1 O ILE A 48 N LYS A 28
SHEET 3 A 3 ALA A 39 SER A 42 -1 N SER A 40 O TYR A 49
SHEET 1 B 3 LYS B 28 LYS B 32 0
SHEET 2 B 3 THR B 47 ASN B 51 1 O ILE B 48 N LYS B 28
SHEET 3 B 3 ALA B 39 SER B 42 -1 N SER B 40 O TYR B 49
LINK NE2 HIS A 69 ZN ZN A 201 1555 1555 2.04
LINK NE2 HIS A 73 ZN ZN A 201 1555 1555 2.00
LINK NE2 HIS A 80 ZN ZN A 201 1555 1555 2.00
LINK ZN ZN A 201 O ACT A 202 1555 1555 2.01
LINK ZN ZN A 201 OXT ACT A 202 1555 1555 2.62
LINK NE2 HIS B 69 ZN ZN B 201 1555 1555 2.04
LINK NE2 HIS B 73 ZN ZN B 201 1555 1555 1.93
LINK NE2 HIS B 80 ZN ZN B 201 1555 1555 1.92
LINK ZN ZN B 201 OXT ACT B 202 1555 1555 2.17
LINK ZN ZN B 201 O ACT B 202 1555 1555 2.55
SITE 1 AC1 4 HIS A 69 HIS A 73 HIS A 80 ACT A 202
SITE 1 AC2 8 HIS A 69 HIS A 73 HIS A 80 ZN A 201
SITE 2 AC2 8 HOH A 311 HOH A 342 PHE B 100 ASN B 101
SITE 1 AC3 5 ALA A 39 GLU A 70 HIS A 73 HOH A 356
SITE 2 AC3 5 HOH A 408
SITE 1 AC4 5 GLU A 9 ILE A 10 ARG A 64 HOH A 343
SITE 2 AC4 5 HOH A 345
SITE 1 AC5 4 HIS B 69 HIS B 73 HIS B 80 ACT B 202
SITE 1 AC6 7 PHE A 100 HIS B 69 HIS B 73 HIS B 80
SITE 2 AC6 7 ZN B 201 GOL B 204 HOH B 428
SITE 1 AC7 6 ILE B 6 GLU B 9 ARG B 64 HOH B 319
SITE 2 AC7 6 HOH B 396 HOH B 427
SITE 1 AC8 10 ALA B 39 SER B 40 ILE B 41 HIS B 69
SITE 2 AC8 10 GLU B 70 HIS B 73 ACT B 202 HOH B 340
SITE 3 AC8 10 HOH B 361 HOH B 428
CRYST1 49.390 49.840 104.840 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 0.020247 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020064 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009538 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
