HEADER HYDROLASE 11-JAN-07 2OIK
TITLE CRYSTAL STRUCTURE OF A HISTIDINE TRIAD (HIT) PROTEIN (MFLA_2506) FROM
TITLE 2 METHYLOBACILLUS FLAGELLATUS KT AT 1.65 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTIDINE TRIAD (HIT) PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOBACILLUS FLAGELLATUS;
SOURCE 3 ORGANISM_TAXID: 265072;
SOURCE 4 STRAIN: KT;
SOURCE 5 ATCC: 51484;
SOURCE 6 COLLECTION: DSM 6875;
SOURCE 7 GENE: YP_546612.1, MFLA_2506;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS HIT-LIKE FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 7 25-JAN-23 2OIK 1 REMARK SEQADV LINK
REVDAT 6 25-OCT-17 2OIK 1 REMARK
REVDAT 5 18-OCT-17 2OIK 1 REMARK
REVDAT 4 13-JUL-11 2OIK 1 VERSN
REVDAT 3 23-MAR-11 2OIK 1 HEADER TITLE KEYWDS
REVDAT 2 24-FEB-09 2OIK 1 VERSN
REVDAT 1 30-JAN-07 2OIK 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF HISTIDINE TRIAD (HIT) PROTEIN
JRNL TITL 2 (YP_546612.1) FROM METHYLOBACILLUS FLAGELLATUS KT AT 1.65 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 62091
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3135
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3117
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 165
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 461
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 24.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.83000
REMARK 3 B22 (A**2) : -0.57000
REMARK 3 B33 (A**2) : 0.42000
REMARK 3 B12 (A**2) : -0.70000
REMARK 3 B13 (A**2) : -0.57000
REMARK 3 B23 (A**2) : -1.30000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.580
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4575 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4222 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6204 ; 1.565 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9739 ; 0.863 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 572 ; 6.064 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;28.521 ;22.330
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 765 ;12.753 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;16.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 691 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5050 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 955 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 797 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4265 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2129 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2685 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 360 ; 0.175 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.075 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.235 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 63 ; 0.352 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.130 ; 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): 2867 ; 1.913 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1129 ; 0.697 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4551 ; 2.607 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1891 ; 4.056 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1644 ; 5.521 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 144 4
REMARK 3 1 B 6 B 144 4
REMARK 3 1 C 6 C 144 4
REMARK 3 1 D 6 D 144 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2050 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2050 ; 0.34 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2050 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2050 ; 0.35 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2050 ; 0.97 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2050 ; 1.02 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2050 ; 0.94 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2050 ; 0.90 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 : A 6 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2059 26.9301 34.6446
REMARK 3 T TENSOR
REMARK 3 T11: -0.0389 T22: -0.0717
REMARK 3 T33: -0.0403 T12: 0.0056
REMARK 3 T13: -0.0002 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 2.1833 L22: 1.0850
REMARK 3 L33: 1.9243 L12: -0.0761
REMARK 3 L13: 0.9265 L23: 0.5168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: -0.1043 S13: 0.2065
REMARK 3 S21: -0.0815 S22: -0.0622 S23: 0.0352
REMARK 3 S31: -0.1134 S32: -0.2139 S33: 0.1282
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 6 B 144
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4708 10.5871 41.6943
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: -0.0912
REMARK 3 T33: -0.0590 T12: -0.0047
REMARK 3 T13: -0.0160 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.6153 L22: 1.1912
REMARK 3 L33: 1.6692 L12: 0.5677
REMARK 3 L13: 0.6021 L23: 0.0252
REMARK 3 S TENSOR
REMARK 3 S11: 0.1484 S12: -0.1673 S13: -0.0885
REMARK 3 S21: 0.0938 S22: 0.0086 S23: -0.0219
REMARK 3 S31: 0.3052 S32: -0.0207 S33: -0.1571
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 144
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6302 39.0928 69.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.0082 T22: -0.0420
REMARK 3 T33: -0.0421 T12: -0.0038
REMARK 3 T13: 0.0229 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 1.9915 L22: 1.2636
REMARK 3 L33: 1.3942 L12: 0.1949
REMARK 3 L13: 0.3179 L23: 0.3893
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: 0.2883 S13: 0.1817
REMARK 3 S21: -0.1080 S22: 0.0207 S23: 0.0575
REMARK 3 S31: -0.2394 S32: 0.0338 S33: 0.0107
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 6 D 144
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6776 22.5618 76.4540
REMARK 3 T TENSOR
REMARK 3 T11: -0.0453 T22: -0.0807
REMARK 3 T33: -0.0392 T12: 0.0010
REMARK 3 T13: 0.0109 T23: 0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 2.8384 L22: 1.0671
REMARK 3 L33: 1.2898 L12: -0.0151
REMARK 3 L13: -0.3251 L23: 0.5486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0482 S12: 0.0770 S13: -0.2742
REMARK 3 S21: 0.0962 S22: -0.0650 S23: 0.0300
REMARK 3 S31: 0.0743 S32: -0.1218 S33: 0.0168
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE
REMARK 3 ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED
REMARK 3 SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. EACH
REMARK 3 MONOMER CONTAINS ONE METAL WHICH IS ASSIGNED AS ZINC. THE
REMARK 3 ASSIGNMENT OF ZINC IS SUPPORTED BY BOTH X-RAY FLUORESCENCE
REMARK 3 EXCITATION SCAN AND ANOMALOUS DIFFERENCE FOURIER MAPS.
REMARK 4
REMARK 4 2OIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97913
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 45.549
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 3.940
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.71
REMARK 200 R MERGE FOR SHELL (I) : 0.82800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.1M NACL, 30.0% PEG MME
REMARK 280 -550, 0.1M BICINE PH 9.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K, PH 9.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1,2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A
REMARK 300 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
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: 4340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 MSE A 5
REMARK 465 GLN A 145
REMARK 465 GLY A 146
REMARK 465 GLU A 147
REMARK 465 PRO A 148
REMARK 465 VAL A 149
REMARK 465 PHE A 150
REMARK 465 MSE A 151
REMARK 465 GLY A 152
REMARK 465 MSE A 153
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 ARG B 3
REMARK 465 THR B 4
REMARK 465 MSE B 5
REMARK 465 GLN B 145
REMARK 465 GLY B 146
REMARK 465 GLU B 147
REMARK 465 PRO B 148
REMARK 465 VAL B 149
REMARK 465 PHE B 150
REMARK 465 MSE B 151
REMARK 465 GLY B 152
REMARK 465 MSE B 153
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 ARG C 3
REMARK 465 THR C 4
REMARK 465 GLY C 146
REMARK 465 GLU C 147
REMARK 465 PRO C 148
REMARK 465 VAL C 149
REMARK 465 PHE C 150
REMARK 465 MSE C 151
REMARK 465 GLY C 152
REMARK 465 MSE C 153
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 THR D 2
REMARK 465 ARG D 3
REMARK 465 THR D 4
REMARK 465 MSE D 5
REMARK 465 GLN D 145
REMARK 465 GLY D 146
REMARK 465 GLU D 147
REMARK 465 PRO D 148
REMARK 465 VAL D 149
REMARK 465 PHE D 150
REMARK 465 MSE D 151
REMARK 465 GLY D 152
REMARK 465 MSE D 153
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 SER A 6 CB OG
REMARK 470 HIS A 8 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 GLU A 12 CD OE1 OE2
REMARK 470 GLN A 36 CD OE1 NE2
REMARK 470 ARG A 80 NE CZ NH1 NH2
REMARK 470 GLU A 121 OE1 OE2
REMARK 470 LEU A 123 CG CD1 CD2
REMARK 470 GLN A 125 CG CD OE1 NE2
REMARK 470 GLN A 129 CG CD OE1 NE2
REMARK 470 SER B 6 CB OG
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 ASN B 10 CG OD1 ND2
REMARK 470 GLU B 12 OE1 OE2
REMARK 470 LEU B 123 CG CD1 CD2
REMARK 470 GLN B 125 CG CD OE1 NE2
REMARK 470 ASP B 128 CG OD1 OD2
REMARK 470 GLN B 129 CG CD OE1 NE2
REMARK 470 SER C 6 OG
REMARK 470 ASN C 10 CG OD1 ND2
REMARK 470 GLN C 36 CD OE1 NE2
REMARK 470 ARG C 57 CD NE CZ NH1 NH2
REMARK 470 LEU C 123 CG CD1 CD2
REMARK 470 GLN C 125 CG CD OE1 NE2
REMARK 470 GLN C 129 CG CD OE1 NE2
REMARK 470 LYS C 137 CG CD CE NZ
REMARK 470 GLN C 145 CG CD OE1 NE2
REMARK 470 SER D 6 CB OG
REMARK 470 LYS D 9 CG CD CE NZ
REMARK 470 GLU D 12 CG CD OE1 OE2
REMARK 470 ARG D 80 NE CZ NH1 NH2
REMARK 470 GLU D 121 CG CD OE1 OE2
REMARK 470 LEU D 123 CG CD1 CD2
REMARK 470 GLN D 125 CG CD OE1 NE2
REMARK 470 ASP D 128 OD1 OD2
REMARK 470 GLN D 129 CG CD OE1 NE2
REMARK 470 LYS D 137 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 O HOH D 278 O HOH D 296 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP B 107 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 89 -75.87 -106.19
REMARK 500 LEU B 123 75.51 -113.99
REMARK 500 LEU D 89 -72.84 -110.97
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 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 118.9
REMARK 620 3 HIS A 49 ND1 109.8 102.2
REMARK 620 4 HIS A 95 ND1 110.2 107.1 108.0
REMARK 620 N 1 2 3
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 CYS B 11 SG
REMARK 620 2 CYS B 14 SG 118.8
REMARK 620 3 HIS B 49 ND1 107.0 111.3
REMARK 620 4 HIS B 95 ND1 107.5 109.1 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 11 SG
REMARK 620 2 CYS C 14 SG 120.7
REMARK 620 3 HIS C 49 ND1 104.3 109.7
REMARK 620 4 HIS C 95 ND1 112.3 108.0 99.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 11 SG
REMARK 620 2 CYS D 14 SG 117.5
REMARK 620 3 HIS D 49 ND1 110.4 105.0
REMARK 620 4 HIS D 95 ND1 110.8 110.6 101.1
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 ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 205
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 371704 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE, FOLLOWED BY THE
REMARK 999 TARGET SEQUENCE.
DBREF 2OIK A 1 153 UNP Q1GYB6 Q1GYB6_METFK 1 153
DBREF 2OIK B 1 153 UNP Q1GYB6 Q1GYB6_METFK 1 153
DBREF 2OIK C 1 153 UNP Q1GYB6 Q1GYB6_METFK 1 153
DBREF 2OIK D 1 153 UNP Q1GYB6 Q1GYB6_METFK 1 153
SEQADV 2OIK GLY A 0 UNP Q1GYB6 EXPRESSION TAG
SEQADV 2OIK MSE A 1 UNP Q1GYB6 MET 1 MODIFIED RESIDUE
SEQADV 2OIK MSE A 5 UNP Q1GYB6 MET 5 MODIFIED RESIDUE
SEQADV 2OIK MSE A 53 UNP Q1GYB6 MET 53 MODIFIED RESIDUE
SEQADV 2OIK MSE A 65 UNP Q1GYB6 MET 65 MODIFIED RESIDUE
SEQADV 2OIK MSE A 79 UNP Q1GYB6 MET 79 MODIFIED RESIDUE
SEQADV 2OIK MSE A 92 UNP Q1GYB6 MET 92 MODIFIED RESIDUE
SEQADV 2OIK MSE A 151 UNP Q1GYB6 MET 151 MODIFIED RESIDUE
SEQADV 2OIK MSE A 153 UNP Q1GYB6 MET 153 MODIFIED RESIDUE
SEQADV 2OIK GLY B 0 UNP Q1GYB6 EXPRESSION TAG
SEQADV 2OIK MSE B 1 UNP Q1GYB6 MET 1 MODIFIED RESIDUE
SEQADV 2OIK MSE B 5 UNP Q1GYB6 MET 5 MODIFIED RESIDUE
SEQADV 2OIK MSE B 53 UNP Q1GYB6 MET 53 MODIFIED RESIDUE
SEQADV 2OIK MSE B 65 UNP Q1GYB6 MET 65 MODIFIED RESIDUE
SEQADV 2OIK MSE B 79 UNP Q1GYB6 MET 79 MODIFIED RESIDUE
SEQADV 2OIK MSE B 92 UNP Q1GYB6 MET 92 MODIFIED RESIDUE
SEQADV 2OIK MSE B 151 UNP Q1GYB6 MET 151 MODIFIED RESIDUE
SEQADV 2OIK MSE B 153 UNP Q1GYB6 MET 153 MODIFIED RESIDUE
SEQADV 2OIK GLY C 0 UNP Q1GYB6 EXPRESSION TAG
SEQADV 2OIK MSE C 1 UNP Q1GYB6 MET 1 MODIFIED RESIDUE
SEQADV 2OIK MSE C 5 UNP Q1GYB6 MET 5 MODIFIED RESIDUE
SEQADV 2OIK MSE C 53 UNP Q1GYB6 MET 53 MODIFIED RESIDUE
SEQADV 2OIK MSE C 65 UNP Q1GYB6 MET 65 MODIFIED RESIDUE
SEQADV 2OIK MSE C 79 UNP Q1GYB6 MET 79 MODIFIED RESIDUE
SEQADV 2OIK MSE C 92 UNP Q1GYB6 MET 92 MODIFIED RESIDUE
SEQADV 2OIK MSE C 151 UNP Q1GYB6 MET 151 MODIFIED RESIDUE
SEQADV 2OIK MSE C 153 UNP Q1GYB6 MET 153 MODIFIED RESIDUE
SEQADV 2OIK GLY D 0 UNP Q1GYB6 EXPRESSION TAG
SEQADV 2OIK MSE D 1 UNP Q1GYB6 MET 1 MODIFIED RESIDUE
SEQADV 2OIK MSE D 5 UNP Q1GYB6 MET 5 MODIFIED RESIDUE
SEQADV 2OIK MSE D 53 UNP Q1GYB6 MET 53 MODIFIED RESIDUE
SEQADV 2OIK MSE D 65 UNP Q1GYB6 MET 65 MODIFIED RESIDUE
SEQADV 2OIK MSE D 79 UNP Q1GYB6 MET 79 MODIFIED RESIDUE
SEQADV 2OIK MSE D 92 UNP Q1GYB6 MET 92 MODIFIED RESIDUE
SEQADV 2OIK MSE D 151 UNP Q1GYB6 MET 151 MODIFIED RESIDUE
SEQADV 2OIK MSE D 153 UNP Q1GYB6 MET 153 MODIFIED RESIDUE
SEQRES 1 A 154 GLY MSE THR ARG THR MSE SER PHE HIS LYS ASN CYS GLU
SEQRES 2 A 154 LEU CYS THR THR ALA GLY GLY GLU ILE LEU TRP GLN ASP
SEQRES 3 A 154 ALA LEU CYS ARG VAL VAL HIS VAL GLU ASN GLN ASP TYR
SEQRES 4 A 154 PRO GLY PHE CYS ARG VAL ILE LEU ASN ARG HIS VAL LYS
SEQRES 5 A 154 GLU MSE SER ASP LEU ARG PRO ALA GLU ARG ASP HIS LEU
SEQRES 6 A 154 MSE LEU VAL VAL PHE ALA VAL GLU GLU ALA VAL ARG GLU
SEQRES 7 A 154 VAL MSE ARG PRO ASP LYS ILE ASN LEU ALA SER LEU GLY
SEQRES 8 A 154 ASN MSE THR PRO HIS VAL HIS TRP HIS VAL ILE PRO ARG
SEQRES 9 A 154 PHE LYS ARG ASP ARG HIS PHE PRO ASN SER VAL TRP GLY
SEQRES 10 A 154 GLU THR LYS ARG GLU SER LEU PRO GLN ALA LEU ASP GLN
SEQRES 11 A 154 GLY SER THR THR ALA LEU LYS LYS ALA ILE SER VAL ARG
SEQRES 12 A 154 LEU ASP GLN GLY GLU PRO VAL PHE MSE GLY MSE
SEQRES 1 B 154 GLY MSE THR ARG THR MSE SER PHE HIS LYS ASN CYS GLU
SEQRES 2 B 154 LEU CYS THR THR ALA GLY GLY GLU ILE LEU TRP GLN ASP
SEQRES 3 B 154 ALA LEU CYS ARG VAL VAL HIS VAL GLU ASN GLN ASP TYR
SEQRES 4 B 154 PRO GLY PHE CYS ARG VAL ILE LEU ASN ARG HIS VAL LYS
SEQRES 5 B 154 GLU MSE SER ASP LEU ARG PRO ALA GLU ARG ASP HIS LEU
SEQRES 6 B 154 MSE LEU VAL VAL PHE ALA VAL GLU GLU ALA VAL ARG GLU
SEQRES 7 B 154 VAL MSE ARG PRO ASP LYS ILE ASN LEU ALA SER LEU GLY
SEQRES 8 B 154 ASN MSE THR PRO HIS VAL HIS TRP HIS VAL ILE PRO ARG
SEQRES 9 B 154 PHE LYS ARG ASP ARG HIS PHE PRO ASN SER VAL TRP GLY
SEQRES 10 B 154 GLU THR LYS ARG GLU SER LEU PRO GLN ALA LEU ASP GLN
SEQRES 11 B 154 GLY SER THR THR ALA LEU LYS LYS ALA ILE SER VAL ARG
SEQRES 12 B 154 LEU ASP GLN GLY GLU PRO VAL PHE MSE GLY MSE
SEQRES 1 C 154 GLY MSE THR ARG THR MSE SER PHE HIS LYS ASN CYS GLU
SEQRES 2 C 154 LEU CYS THR THR ALA GLY GLY GLU ILE LEU TRP GLN ASP
SEQRES 3 C 154 ALA LEU CYS ARG VAL VAL HIS VAL GLU ASN GLN ASP TYR
SEQRES 4 C 154 PRO GLY PHE CYS ARG VAL ILE LEU ASN ARG HIS VAL LYS
SEQRES 5 C 154 GLU MSE SER ASP LEU ARG PRO ALA GLU ARG ASP HIS LEU
SEQRES 6 C 154 MSE LEU VAL VAL PHE ALA VAL GLU GLU ALA VAL ARG GLU
SEQRES 7 C 154 VAL MSE ARG PRO ASP LYS ILE ASN LEU ALA SER LEU GLY
SEQRES 8 C 154 ASN MSE THR PRO HIS VAL HIS TRP HIS VAL ILE PRO ARG
SEQRES 9 C 154 PHE LYS ARG ASP ARG HIS PHE PRO ASN SER VAL TRP GLY
SEQRES 10 C 154 GLU THR LYS ARG GLU SER LEU PRO GLN ALA LEU ASP GLN
SEQRES 11 C 154 GLY SER THR THR ALA LEU LYS LYS ALA ILE SER VAL ARG
SEQRES 12 C 154 LEU ASP GLN GLY GLU PRO VAL PHE MSE GLY MSE
SEQRES 1 D 154 GLY MSE THR ARG THR MSE SER PHE HIS LYS ASN CYS GLU
SEQRES 2 D 154 LEU CYS THR THR ALA GLY GLY GLU ILE LEU TRP GLN ASP
SEQRES 3 D 154 ALA LEU CYS ARG VAL VAL HIS VAL GLU ASN GLN ASP TYR
SEQRES 4 D 154 PRO GLY PHE CYS ARG VAL ILE LEU ASN ARG HIS VAL LYS
SEQRES 5 D 154 GLU MSE SER ASP LEU ARG PRO ALA GLU ARG ASP HIS LEU
SEQRES 6 D 154 MSE LEU VAL VAL PHE ALA VAL GLU GLU ALA VAL ARG GLU
SEQRES 7 D 154 VAL MSE ARG PRO ASP LYS ILE ASN LEU ALA SER LEU GLY
SEQRES 8 D 154 ASN MSE THR PRO HIS VAL HIS TRP HIS VAL ILE PRO ARG
SEQRES 9 D 154 PHE LYS ARG ASP ARG HIS PHE PRO ASN SER VAL TRP GLY
SEQRES 10 D 154 GLU THR LYS ARG GLU SER LEU PRO GLN ALA LEU ASP GLN
SEQRES 11 D 154 GLY SER THR THR ALA LEU LYS LYS ALA ILE SER VAL ARG
SEQRES 12 D 154 LEU ASP GLN GLY GLU PRO VAL PHE MSE GLY MSE
MODRES 2OIK MSE A 53 MET SELENOMETHIONINE
MODRES 2OIK MSE A 65 MET SELENOMETHIONINE
MODRES 2OIK MSE A 79 MET SELENOMETHIONINE
MODRES 2OIK MSE A 92 MET SELENOMETHIONINE
MODRES 2OIK MSE B 53 MET SELENOMETHIONINE
MODRES 2OIK MSE B 65 MET SELENOMETHIONINE
MODRES 2OIK MSE B 79 MET SELENOMETHIONINE
MODRES 2OIK MSE B 92 MET SELENOMETHIONINE
MODRES 2OIK MSE C 5 MET SELENOMETHIONINE
MODRES 2OIK MSE C 53 MET SELENOMETHIONINE
MODRES 2OIK MSE C 65 MET SELENOMETHIONINE
MODRES 2OIK MSE C 79 MET SELENOMETHIONINE
MODRES 2OIK MSE C 92 MET SELENOMETHIONINE
MODRES 2OIK MSE D 53 MET SELENOMETHIONINE
MODRES 2OIK MSE D 65 MET SELENOMETHIONINE
MODRES 2OIK MSE D 79 MET SELENOMETHIONINE
MODRES 2OIK MSE D 92 MET SELENOMETHIONINE
HET MSE A 53 8
HET MSE A 65 8
HET MSE A 79 8
HET MSE A 92 13
HET MSE B 53 8
HET MSE B 65 8
HET MSE B 79 8
HET MSE B 92 13
HET MSE C 5 8
HET MSE C 53 8
HET MSE C 65 8
HET MSE C 79 8
HET MSE C 92 13
HET MSE D 53 8
HET MSE D 65 8
HET MSE D 79 8
HET MSE D 92 13
HET ZN A 201 1
HET CL A 202 1
HET GOL A 203 6
HET GOL A 204 6
HET GOL A 205 6
HET ZN B 201 1
HET CL B 202 1
HET GOL B 203 6
HET GOL B 204 6
HET ZN C 201 1
HET CL C 202 1
HET GOL C 203 6
HET GOL C 204 6
HET ZN D 201 1
HET CL D 202 1
HET CL D 203 1
HET GOL D 204 6
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 17(C5 H11 N O2 SE)
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 CL 5(CL 1-)
FORMUL 7 GOL 8(C3 H8 O3)
FORMUL 22 HOH *461(H2 O)
HELIX 1 1 CYS A 11 THR A 16 1 6
HELIX 2 2 GLU A 52 LEU A 56 5 5
HELIX 3 3 ARG A 57 ARG A 80 1 24
HELIX 4 4 ASP A 128 ASP A 144 1 17
HELIX 5 5 CYS B 11 THR B 16 1 6
HELIX 6 6 GLU B 52 LEU B 56 5 5
HELIX 7 7 ARG B 57 ARG B 80 1 24
HELIX 8 8 ASP B 128 ASP B 144 1 17
HELIX 9 9 CYS C 11 THR C 16 1 6
HELIX 10 10 GLU C 52 LEU C 56 5 5
HELIX 11 11 ARG C 57 ARG C 80 1 24
HELIX 12 12 ASP C 128 ASP C 144 1 17
HELIX 13 13 CYS D 11 THR D 16 1 6
HELIX 14 14 GLU D 52 LEU D 56 5 5
HELIX 15 15 ARG D 57 ARG D 80 1 24
HELIX 16 16 ASP D 128 ASP D 144 1 17
SHEET 1 A10 GLU A 20 GLN A 24 0
SHEET 2 A10 CYS A 28 HIS A 32 -1 O VAL A 30 N LEU A 22
SHEET 3 A10 CYS A 42 LEU A 46 -1 O ILE A 45 N ARG A 29
SHEET 4 A10 HIS A 97 ARG A 103 -1 O VAL A 100 N CYS A 42
SHEET 5 A10 LYS A 83 SER A 88 -1 N LYS A 83 O ARG A 103
SHEET 6 A10 LYS B 83 SER B 88 -1 O LEU B 86 N SER A 88
SHEET 7 A10 HIS B 97 ARG B 103 -1 O ARG B 103 N LYS B 83
SHEET 8 A10 CYS B 42 LEU B 46 -1 N CYS B 42 O VAL B 100
SHEET 9 A10 CYS B 28 HIS B 32 -1 N ARG B 29 O ILE B 45
SHEET 10 A10 GLU B 20 GLN B 24 -1 N TRP B 23 O VAL B 30
SHEET 1 B10 GLU C 20 GLN C 24 0
SHEET 2 B10 CYS C 28 HIS C 32 -1 O VAL C 30 N TRP C 23
SHEET 3 B10 CYS C 42 LEU C 46 -1 O ILE C 45 N ARG C 29
SHEET 4 B10 HIS C 97 ARG C 103 -1 O VAL C 100 N CYS C 42
SHEET 5 B10 LYS C 83 SER C 88 -1 N LYS C 83 O ARG C 103
SHEET 6 B10 LYS D 83 SER D 88 -1 O SER D 88 N LEU C 86
SHEET 7 B10 HIS D 97 ARG D 103 -1 O ARG D 103 N LYS D 83
SHEET 8 B10 CYS D 42 LEU D 46 -1 N CYS D 42 O VAL D 100
SHEET 9 B10 CYS D 28 HIS D 32 -1 N ARG D 29 O ILE D 45
SHEET 10 B10 GLU D 20 GLN D 24 -1 N LEU D 22 O VAL D 30
LINK C GLU A 52 N MSE A 53 1555 1555 1.33
LINK C MSE A 53 N SER A 54 1555 1555 1.33
LINK C LEU A 64 N MSE A 65 1555 1555 1.34
LINK C MSE A 65 N LEU A 66 1555 1555 1.32
LINK C VAL A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N ARG A 80 1555 1555 1.32
LINK C ASN A 91 N MSE A 92 1555 1555 1.32
LINK C MSE A 92 N THR A 93 1555 1555 1.33
LINK C GLU B 52 N MSE B 53 1555 1555 1.33
LINK C MSE B 53 N SER B 54 1555 1555 1.32
LINK C LEU B 64 N MSE B 65 1555 1555 1.33
LINK C MSE B 65 N LEU B 66 1555 1555 1.33
LINK C VAL B 78 N MSE B 79 1555 1555 1.33
LINK C MSE B 79 N ARG B 80 1555 1555 1.34
LINK C ASN B 91 N MSE B 92 1555 1555 1.33
LINK C MSE B 92 N THR B 93 1555 1555 1.32
LINK C MSE C 5 N SER C 6 1555 1555 1.33
LINK C GLU C 52 N MSE C 53 1555 1555 1.33
LINK C MSE C 53 N SER C 54 1555 1555 1.33
LINK C LEU C 64 N MSE C 65 1555 1555 1.33
LINK C MSE C 65 N LEU C 66 1555 1555 1.34
LINK C VAL C 78 N MSE C 79 1555 1555 1.34
LINK C MSE C 79 N ARG C 80 1555 1555 1.33
LINK C ASN C 91 N MSE C 92 1555 1555 1.33
LINK C MSE C 92 N THR C 93 1555 1555 1.33
LINK C GLU D 52 N MSE D 53 1555 1555 1.32
LINK C MSE D 53 N SER D 54 1555 1555 1.32
LINK C LEU D 64 N MSE D 65 1555 1555 1.32
LINK C MSE D 65 N LEU D 66 1555 1555 1.33
LINK C VAL D 78 N MSE D 79 1555 1555 1.33
LINK C MSE D 79 N ARG D 80 1555 1555 1.33
LINK C ASN D 91 N MSE D 92 1555 1555 1.32
LINK C MSE D 92 N THR D 93 1555 1555 1.33
LINK SG CYS A 11 ZN ZN A 201 1555 1555 2.11
LINK SG CYS A 14 ZN ZN A 201 1555 1555 2.31
LINK ND1 HIS A 49 ZN ZN A 201 1555 1555 2.04
LINK ND1 HIS A 95 ZN ZN A 201 1555 1555 2.11
LINK SG CYS B 11 ZN ZN B 201 1555 1555 2.26
LINK SG CYS B 14 ZN ZN B 201 1555 1555 2.30
LINK ND1 HIS B 49 ZN ZN B 201 1555 1555 2.10
LINK ND1 HIS B 95 ZN ZN B 201 1555 1555 2.14
LINK SG CYS C 11 ZN ZN C 201 1555 1555 2.27
LINK SG CYS C 14 ZN ZN C 201 1555 1555 2.27
LINK ND1 HIS C 49 ZN ZN C 201 1555 1555 2.05
LINK ND1 HIS C 95 ZN ZN C 201 1555 1555 2.08
LINK SG CYS D 11 ZN ZN D 201 1555 1555 2.25
LINK SG CYS D 14 ZN ZN D 201 1555 1555 2.35
LINK ND1 HIS D 49 ZN ZN D 201 1555 1555 1.93
LINK ND1 HIS D 95 ZN ZN D 201 1555 1555 2.10
CISPEP 1 PHE A 110 PRO A 111 0 -0.63
CISPEP 2 PHE B 110 PRO B 111 0 1.33
CISPEP 3 PHE C 110 PRO C 111 0 2.76
CISPEP 4 PHE D 110 PRO D 111 0 1.85
SITE 1 AC1 4 CYS A 11 CYS A 14 HIS A 49 HIS A 95
SITE 1 AC2 4 CYS B 11 CYS B 14 HIS B 49 HIS B 95
SITE 1 AC3 4 CYS C 11 CYS C 14 HIS C 49 HIS C 95
SITE 1 AC4 4 CYS D 11 CYS D 14 HIS D 49 HIS D 95
SITE 1 AC5 6 LEU A 89 GLY A 90 HIS A 97 HIS A 99
SITE 2 AC5 6 HOH A 212 HOH A 241
SITE 1 AC6 7 LEU D 89 GLY D 90 HIS D 97 HIS D 99
SITE 2 AC6 7 GOL D 204 HOH D 210 HOH D 228
SITE 1 AC7 5 LEU C 89 GLY C 90 HIS C 97 HIS C 99
SITE 2 AC7 5 HOH C 220
SITE 1 AC8 4 TRP C 115 HOH C 237 ASN D 112 SER D 113
SITE 1 AC9 7 LEU B 89 GLY B 90 HIS B 97 HIS B 99
SITE 2 AC9 7 GOL B 203 HOH B 213 HOH B 233
SITE 1 BC1 6 GLU A 12 THR A 93 HIS A 97 HIS A 99
SITE 2 BC1 6 HOH A 212 HOH A 269
SITE 1 BC2 9 GLU B 12 ARG B 43 THR B 93 HIS B 97
SITE 2 BC2 9 HIS B 99 CL B 202 HOH B 213 HOH B 223
SITE 3 BC2 9 HOH B 284
SITE 1 BC3 5 ASN B 35 VAL B 114 HOH B 214 HOH B 219
SITE 2 BC3 5 ARG D 106
SITE 1 BC4 8 GLU C 12 ARG C 43 THR C 93 HIS C 97
SITE 2 BC4 8 HIS C 99 HOH C 220 HOH C 231 HOH C 243
SITE 1 BC5 6 ARG A 106 ASN C 35 ARG C 43 HOH C 212
SITE 2 BC5 6 HOH C 225 HOH C 234
SITE 1 BC6 9 GLU D 12 ARG D 43 THR D 93 HIS D 97
SITE 2 BC6 9 HIS D 99 CL D 202 HOH D 210 HOH D 253
SITE 3 BC6 9 HOH D 282
SITE 1 BC7 2 ILE A 21 HOH A 234
SITE 1 BC8 6 ASN A 35 ARG A 43 VAL A 114 HOH A 216
SITE 2 BC8 6 HOH A 256 HOH A 283
CRYST1 45.243 47.981 69.766 108.13 98.22 90.34 P 1 4
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 0.022100 0.000130 0.003410 0.00000
SCALE2 0.000000 0.020840 0.006920 0.00000
SCALE3 0.000000 0.000000 0.015260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
