HEADER HYDROLASE, METAL BINDING PROTEIN 23-JUN-06 2HF8
TITLE CRYSTAL STRUCTURE OF HYPB FROM METHANOCALDOCOCCUS
TITLE 2 JANNASCHII IN THE TRIPHOSPHATE FORM, IN COMPLEX WITH ZINC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE HYDROGENASE NICKEL INCORPORATION
COMPND 3 PROTEIN HYPB;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 GENE: HYPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS ALPHA AND BETA PROTEIN, P-LOOP CONTAINING NUCLEOSIDE
KEYWDS 2 TRIPHOSPHATE HYDROLASE, HYDROLASE, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.GASPER,A.SCRIMA,A.WITTINGHOFER
REVDAT 3 24-FEB-09 2HF8 1 VERSN
REVDAT 2 10-OCT-06 2HF8 1 JRNL
REVDAT 1 04-JUL-06 2HF8 0
JRNL AUTH R.GASPER,A.SCRIMA,A.WITTINGHOFER
JRNL TITL STRUCTURAL INSIGHTS INTO HYPB, A GTP-BINDING
JRNL TITL 2 PROTEIN THAT REGULATES METAL BINDING.
JRNL REF J.BIOL.CHEM. V. 281 27492 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16807243
JRNL DOI 10.1074/JBC.M600809200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27577
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1410
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1850
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.34000
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): 0.226
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.188
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.124
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.579
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3350 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4518 ; 1.090 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 418 ; 5.330 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;33.660 ;26.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 662 ;13.260 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;13.626 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 536 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2360 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1440 ; 0.185 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2280 ; 0.290 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 200 ; 0.115 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.120 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 33 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.070 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.232 ; 0.200
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): 2160 ; 0.528 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3346 ; 0.835 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1331 ; 1.223 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1172 ; 1.969 ; 4.500
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2HF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB038280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51141
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.760
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.94
REMARK 200 R MERGE FOR SHELL (I) : 0.08400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 175 MM MALEIC ACID DISODIUM SALT,
REMARK 280 52.5 MM HCL, 14% PEG3350, VAPOR DIFFUSION, TEMPERATURE 293K
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 21.56000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.99500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.06500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.99500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.56000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.06500
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 300 REMARK: BIOLOGICAL UNIT IS COMPOSED OF CHAIN A AND B
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: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 GLY A -4
REMARK 465 ALA A -3
REMARK 465 MET A -2
REMARK 465 GLY A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 LEU A 3
REMARK 465 VAL A 4
REMARK 465 GLY A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 ASP A 8
REMARK 465 ILE A 9
REMARK 465 ALA A 10
REMARK 465 GLY B -4
REMARK 465 ALA B -3
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 4
REMARK 465 GLY B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 ASP B 8
REMARK 465 ILE B 9
REMARK 465 ALA B 10
REMARK 465 LYS B 11
REMARK 465 LYS B 221
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 OD2 ASP A 69 O HOH A 467 2.16
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 ASN A 124 122.85 -179.57
REMARK 500 ILE A 126 -75.73 -118.01
REMARK 500 ASN B 124 125.36 -179.66
REMARK 500 ILE B 126 -84.62 -106.72
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GSP A 300 O3G
REMARK 620 2 THR A 47 OG1 176.4
REMARK 620 3 ASP A 75 OD2 96.9 85.1
REMARK 620 4 HOH A 468 O 92.1 85.1 84.8
REMARK 620 5 GLU A 120 OE2 92.0 90.8 95.6 175.8
REMARK 620 6 GSP A 300 O2B 90.0 87.5 167.5 84.6 94.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 95 SG
REMARK 620 2 CYS A 127 SG 102.7
REMARK 620 3 CYS B 95 SG 117.6 107.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 100 NE2
REMARK 620 2 HIS A 104 NE2 109.1
REMARK 620 3 HIS B 104 NE2 100.5 114.0
REMARK 620 4 HIS B 100 NE2 104.5 125.6 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GSP B 300 O3G
REMARK 620 2 THR B 47 OG1 177.7
REMARK 620 3 HOH B 437 O 92.3 87.8
REMARK 620 4 GSP B 300 O2B 90.9 86.9 81.2
REMARK 620 5 GLU B 120 OE2 91.9 87.8 173.9 94.4
REMARK 620 6 ASP B 75 OD2 92.8 89.4 95.6 175.1 88.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 95 SG
REMARK 620 2 HOH B 462 O 91.3
REMARK 620 3 HIS B 96 ND1 128.3 105.0
REMARK 620 4 CYS B 127 SG 113.7 103.6 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 104 NE2
REMARK 620 2 HIS B 100 NE2 98.8
REMARK 620 3 HIS A 104 NE2 96.0 102.4
REMARK 620 4 HIS A 100 NE2 121.5 124.1 109.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 403
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 404
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP A 300
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSP B 300
DBREF 2HF8 A 1 221 UNP Q57884 HYPB_METJA 1 221
DBREF 2HF8 B 1 221 UNP Q57884 HYPB_METJA 1 221
SEQADV 2HF8 GLY A -4 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 ALA A -3 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 MET A -2 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 GLY A -1 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 GLY A 0 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 MSE A 39 UNP Q57884 MET 39 MODIFIED RESIDUE
SEQADV 2HF8 MSE A 79 UNP Q57884 MET 79 MODIFIED RESIDUE
SEQADV 2HF8 MSE A 158 UNP Q57884 MET 158 MODIFIED RESIDUE
SEQADV 2HF8 MSE A 182 UNP Q57884 MET 182 MODIFIED RESIDUE
SEQADV 2HF8 MSE A 203 UNP Q57884 MET 203 MODIFIED RESIDUE
SEQADV 2HF8 GLY B -4 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 ALA B -3 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 MET B -2 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 GLY B -1 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 GLY B 0 UNP Q57884 CLONING ARTIFACT
SEQADV 2HF8 MSE B 39 UNP Q57884 MET 39 MODIFIED RESIDUE
SEQADV 2HF8 MSE B 79 UNP Q57884 MET 79 MODIFIED RESIDUE
SEQADV 2HF8 MSE B 158 UNP Q57884 MET 158 MODIFIED RESIDUE
SEQADV 2HF8 MSE B 182 UNP Q57884 MET 182 MODIFIED RESIDUE
SEQADV 2HF8 MSE B 203 UNP Q57884 MET 203 MODIFIED RESIDUE
SEQRES 1 A 226 GLY ALA MET GLY GLY MET HIS LEU VAL GLY VAL LEU ASP
SEQRES 2 A 226 ILE ALA LYS ASP ILE LEU LYS ALA ASN LYS ARG LEU ALA
SEQRES 3 A 226 ASP LYS ASN ARG LYS LEU LEU ASN LYS HIS GLY VAL VAL
SEQRES 4 A 226 ALA PHE ASP PHE MSE GLY ALA ILE GLY SER GLY LYS THR
SEQRES 5 A 226 LEU LEU ILE GLU LYS LEU ILE ASP ASN LEU LYS ASP LYS
SEQRES 6 A 226 TYR LYS ILE ALA CYS ILE ALA GLY ASP VAL ILE ALA LYS
SEQRES 7 A 226 PHE ASP ALA GLU ARG MSE GLU LYS HIS GLY ALA LYS VAL
SEQRES 8 A 226 VAL PRO LEU ASN THR GLY LYS GLU CYS HIS LEU ASP ALA
SEQRES 9 A 226 HIS LEU VAL GLY HIS ALA LEU GLU ASP LEU ASN LEU ASP
SEQRES 10 A 226 GLU ILE ASP LEU LEU PHE ILE GLU ASN VAL GLY ASN LEU
SEQRES 11 A 226 ILE CYS PRO ALA ASP PHE ASP LEU GLY THR HIS LYS ARG
SEQRES 12 A 226 ILE VAL VAL ILE SER THR THR GLU GLY ASP ASP THR ILE
SEQRES 13 A 226 GLU LYS HIS PRO GLY ILE MSE LYS THR ALA ASP LEU ILE
SEQRES 14 A 226 VAL ILE ASN LYS ILE ASP LEU ALA ASP ALA VAL GLY ALA
SEQRES 15 A 226 ASP ILE LYS LYS MSE GLU ASN ASP ALA LYS ARG ILE ASN
SEQRES 16 A 226 PRO ASP ALA GLU VAL VAL LEU LEU SER LEU LYS THR MSE
SEQRES 17 A 226 GLU GLY PHE ASP LYS VAL LEU GLU PHE ILE GLU LYS SER
SEQRES 18 A 226 VAL LYS GLU VAL LYS
SEQRES 1 B 226 GLY ALA MET GLY GLY MET HIS LEU VAL GLY VAL LEU ASP
SEQRES 2 B 226 ILE ALA LYS ASP ILE LEU LYS ALA ASN LYS ARG LEU ALA
SEQRES 3 B 226 ASP LYS ASN ARG LYS LEU LEU ASN LYS HIS GLY VAL VAL
SEQRES 4 B 226 ALA PHE ASP PHE MSE GLY ALA ILE GLY SER GLY LYS THR
SEQRES 5 B 226 LEU LEU ILE GLU LYS LEU ILE ASP ASN LEU LYS ASP LYS
SEQRES 6 B 226 TYR LYS ILE ALA CYS ILE ALA GLY ASP VAL ILE ALA LYS
SEQRES 7 B 226 PHE ASP ALA GLU ARG MSE GLU LYS HIS GLY ALA LYS VAL
SEQRES 8 B 226 VAL PRO LEU ASN THR GLY LYS GLU CYS HIS LEU ASP ALA
SEQRES 9 B 226 HIS LEU VAL GLY HIS ALA LEU GLU ASP LEU ASN LEU ASP
SEQRES 10 B 226 GLU ILE ASP LEU LEU PHE ILE GLU ASN VAL GLY ASN LEU
SEQRES 11 B 226 ILE CYS PRO ALA ASP PHE ASP LEU GLY THR HIS LYS ARG
SEQRES 12 B 226 ILE VAL VAL ILE SER THR THR GLU GLY ASP ASP THR ILE
SEQRES 13 B 226 GLU LYS HIS PRO GLY ILE MSE LYS THR ALA ASP LEU ILE
SEQRES 14 B 226 VAL ILE ASN LYS ILE ASP LEU ALA ASP ALA VAL GLY ALA
SEQRES 15 B 226 ASP ILE LYS LYS MSE GLU ASN ASP ALA LYS ARG ILE ASN
SEQRES 16 B 226 PRO ASP ALA GLU VAL VAL LEU LEU SER LEU LYS THR MSE
SEQRES 17 B 226 GLU GLY PHE ASP LYS VAL LEU GLU PHE ILE GLU LYS SER
SEQRES 18 B 226 VAL LYS GLU VAL LYS
MODRES 2HF8 MSE A 39 MET SELENOMETHIONINE
MODRES 2HF8 MSE A 79 MET SELENOMETHIONINE
MODRES 2HF8 MSE A 158 MET SELENOMETHIONINE
MODRES 2HF8 MSE A 182 MET SELENOMETHIONINE
MODRES 2HF8 MSE A 203 MET SELENOMETHIONINE
MODRES 2HF8 MSE B 39 MET SELENOMETHIONINE
MODRES 2HF8 MSE B 79 MET SELENOMETHIONINE
MODRES 2HF8 MSE B 158 MET SELENOMETHIONINE
MODRES 2HF8 MSE B 182 MET SELENOMETHIONINE
MODRES 2HF8 MSE B 203 MET SELENOMETHIONINE
HET MSE A 39 8
HET MSE A 79 8
HET MSE A 158 8
HET MSE A 182 8
HET MSE A 203 8
HET MSE B 39 8
HET MSE B 79 8
HET MSE B 158 8
HET MSE B 182 8
HET MSE B 203 8
HET MG A 301 1
HET MG B 301 1
HET ZN A 401 1
HET ZN B 402 1
HET ZN A 403 1
HET ZN B 404 1
HET GSP A 300 32
HET GSP B 300 32
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 3 MG 2(MG 2+)
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 GSP 2(C10 H16 N5 O13 P3 S)
FORMUL 11 HOH *128(H2 O)
HELIX 1 1 ASP A 12 HIS A 31 1 20
HELIX 2 2 GLY A 45 LYS A 58 1 14
HELIX 3 3 ALA A 72 LYS A 81 1 10
HELIX 4 4 ASP A 98 GLU A 107 1 10
HELIX 5 5 ASP A 108 LEU A 109 5 2
HELIX 6 6 ASN A 110 ILE A 114 5 5
HELIX 7 7 ILE A 126 PHE A 131 5 6
HELIX 8 8 THR A 145 GLY A 147 5 3
HELIX 9 9 ASP A 149 HIS A 154 1 6
HELIX 10 10 HIS A 154 LYS A 159 1 6
HELIX 11 11 LYS A 168 ASP A 170 5 3
HELIX 12 12 LEU A 171 GLY A 176 1 6
HELIX 13 13 ASP A 178 ASN A 190 1 13
HELIX 14 14 GLY A 205 VAL A 220 1 16
HELIX 15 15 ASP B 12 HIS B 31 1 20
HELIX 16 16 GLY B 45 LYS B 58 1 14
HELIX 17 17 ALA B 72 LYS B 81 1 10
HELIX 18 18 ASP B 98 ASP B 108 1 11
HELIX 19 19 LEU B 109 ILE B 114 5 6
HELIX 20 20 ILE B 126 PHE B 131 5 6
HELIX 21 21 THR B 145 GLY B 147 5 3
HELIX 22 22 HIS B 154 ALA B 161 1 8
HELIX 23 23 LYS B 168 ASP B 170 5 3
HELIX 24 24 LEU B 171 GLY B 176 1 6
HELIX 25 25 ASP B 178 ASN B 190 1 13
HELIX 26 26 GLY B 205 GLU B 219 1 15
SHEET 1 A 7 LYS A 85 ASN A 90 0
SHEET 2 A 7 ILE A 63 ASP A 69 1 N ALA A 67 O LEU A 89
SHEET 3 A 7 LEU A 116 GLU A 120 1 O GLU A 120 N ILE A 66
SHEET 4 A 7 VAL A 34 GLY A 40 1 N PHE A 38 O ILE A 119
SHEET 5 A 7 LYS A 137 SER A 143 1 O ILE A 139 N MSE A 39
SHEET 6 A 7 LEU A 163 ASN A 167 1 O ASN A 167 N ILE A 142
SHEET 7 A 7 GLU A 194 LEU A 197 1 O GLU A 194 N ILE A 164
SHEET 1 B 7 LYS B 85 ASN B 90 0
SHEET 2 B 7 ILE B 63 ASP B 69 1 N ALA B 67 O LEU B 89
SHEET 3 B 7 LEU B 116 GLU B 120 1 O GLU B 120 N ILE B 66
SHEET 4 B 7 VAL B 34 GLY B 40 1 N PHE B 38 O ILE B 119
SHEET 5 B 7 LYS B 137 SER B 143 1 O ILE B 139 N MSE B 39
SHEET 6 B 7 LEU B 163 ASN B 167 1 O ASN B 167 N ILE B 142
SHEET 7 B 7 GLU B 194 LEU B 197 1 O GLU B 194 N ILE B 164
LINK C PHE A 38 N MSE A 39 1555 1555 1.33
LINK C MSE A 39 N GLY A 40 1555 1555 1.33
LINK C ARG A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N GLU A 80 1555 1555 1.33
LINK C ILE A 157 N MSE A 158 1555 1555 1.33
LINK C MSE A 158 N LYS A 159 1555 1555 1.33
LINK C LYS A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N GLU A 183 1555 1555 1.33
LINK C THR A 202 N MSE A 203 1555 1555 1.33
LINK C MSE A 203 N GLU A 204 1555 1555 1.33
LINK O3G GSP A 300 MG MG A 301 1555 1555 1.93
LINK MG MG A 301 OG1 THR A 47 1555 1555 2.01
LINK MG MG A 301 OD2 ASP A 75 1555 1555 2.00
LINK MG MG A 301 O HOH A 468 1555 1555 2.05
LINK MG MG A 301 OE2 GLU A 120 1555 1555 2.09
LINK MG MG A 301 O2B GSP A 300 1555 1555 2.12
LINK ZN ZN A 401 SG CYS A 95 1555 1555 2.38
LINK ZN ZN A 401 SG CYS A 127 1555 1555 2.19
LINK ZN ZN A 401 SG CYS B 95 1555 1555 2.20
LINK ZN ZN A 403 NE2 HIS A 100 1555 1555 2.34
LINK ZN ZN A 403 NE2 HIS A 104 1555 1555 1.83
LINK C PHE B 38 N MSE B 39 1555 1555 1.33
LINK C MSE B 39 N GLY B 40 1555 1555 1.33
LINK C ARG B 78 N MSE B 79 1555 1555 1.33
LINK C MSE B 79 N GLU B 80 1555 1555 1.33
LINK C ILE B 157 N MSE B 158 1555 1555 1.33
LINK C MSE B 158 N LYS B 159 1555 1555 1.33
LINK C LYS B 181 N MSE B 182 1555 1555 1.33
LINK C MSE B 182 N GLU B 183 1555 1555 1.33
LINK C THR B 202 N MSE B 203 1555 1555 1.34
LINK C MSE B 203 N GLU B 204 1555 1555 1.33
LINK O3G GSP B 300 MG MG B 301 1555 1555 1.97
LINK MG MG B 301 OG1 THR B 47 1555 1555 2.07
LINK MG MG B 301 O HOH B 437 1555 1555 2.23
LINK MG MG B 301 O2B GSP B 300 1555 1555 2.10
LINK MG MG B 301 OE2 GLU B 120 1555 1555 2.14
LINK MG MG B 301 OD2 ASP B 75 1555 1555 2.15
LINK ZN ZN B 402 SG CYS B 95 1555 1555 2.10
LINK ZN ZN B 402 O HOH B 462 1555 1555 2.22
LINK ZN ZN B 402 ND1 HIS B 96 1555 1555 2.20
LINK ZN ZN B 402 SG CYS B 127 1555 1555 2.33
LINK ZN ZN B 404 NE2 HIS B 104 1555 1555 2.05
LINK ZN ZN B 404 NE2 HIS B 100 1555 1555 2.13
LINK ZN ZN A 403 NE2 HIS B 104 1555 4455 2.06
LINK ZN ZN A 403 NE2 HIS B 100 1555 4455 2.09
LINK ZN ZN B 404 NE2 HIS A 104 1555 4555 2.34
LINK ZN ZN B 404 NE2 HIS A 100 1555 4555 1.83
SITE 1 AC1 5 THR A 47 ASP A 75 GLU A 120 GSP A 300
SITE 2 AC1 5 HOH A 468
SITE 1 AC2 5 THR B 47 ASP B 75 GLU B 120 GSP B 300
SITE 2 AC2 5 HOH B 437
SITE 1 AC3 4 CYS A 95 CYS A 127 CYS B 95 ZN B 402
SITE 1 AC4 5 ZN A 401 CYS B 95 HIS B 96 CYS B 127
SITE 2 AC4 5 HOH B 462
SITE 1 AC5 4 HIS A 100 HIS A 104 HIS B 100 HIS B 104
SITE 1 AC6 4 HIS A 100 HIS A 104 HIS B 100 HIS B 104
SITE 1 AC7 25 GLY A 43 SER A 44 GLY A 45 LYS A 46
SITE 2 AC7 25 THR A 47 LEU A 48 ASP A 75 ARG A 78
SITE 3 AC7 25 GLU A 120 ASN A 167 LYS A 168 ASP A 170
SITE 4 AC7 25 SER A 199 LEU A 200 LYS A 201 MG A 301
SITE 5 AC7 25 HOH A 416 HOH A 458 HOH A 464 HOH A 465
SITE 6 AC7 25 HOH A 468 GLU B 146 LYS B 153 ALA B 174
SITE 7 AC7 25 VAL B 175
SITE 1 AC8 26 GLU A 146 LYS A 153 ALA A 174 VAL A 175
SITE 2 AC8 26 ILE B 42 GLY B 43 SER B 44 GLY B 45
SITE 3 AC8 26 LYS B 46 THR B 47 LEU B 48 ASP B 75
SITE 4 AC8 26 ARG B 78 GLU B 120 ASN B 167 LYS B 168
SITE 5 AC8 26 ASP B 170 LEU B 171 SER B 199 LEU B 200
SITE 6 AC8 26 LYS B 201 MG B 301 HOH B 422 HOH B 437
SITE 7 AC8 26 HOH B 453 HOH B 463
CRYST1 43.120 68.130 155.990 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 0.023191 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
