HEADER LYASE 07-AUG-08 3E3G
TITLE H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT G41A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE 2; BETA CARBONIC ANHYDRASE;
COMPND 5 EC: 4.2.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: CAN, HI1301;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99
KEYWDS BETA CARBONIC ANHYDRASE, ALLOSTERIC SITE MUTANT, LYASE, METAL-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR R.S.ROWLETT,H.FAILING
REVDAT 5 21-FEB-24 3E3G 1 REMARK
REVDAT 4 20-OCT-21 3E3G 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 3E3G 1 VERSN
REVDAT 2 26-MAY-10 3E3G 1 JRNL
REVDAT 1 18-AUG-09 3E3G 0
JRNL AUTH R.S.ROWLETT,K.M.HOFFMANN,H.FAILING,M.M.MYSLIWIEC,D.SAMARDZIC
JRNL TITL EVIDENCE FOR A BICARBONATE "ESCORT" SITE IN HAEMOPHILUS
JRNL TITL 2 INFLUENZAE BETA-CARBONIC ANHYDRASE .
JRNL REF BIOCHEMISTRY V. 49 3640 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20359198
JRNL DOI 10.1021/BI100328J
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 76058
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3804
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4534
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9878
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.34000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.262
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.206
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.165
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.627
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10225 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6749 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13851 ; 1.161 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16417 ; 0.841 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1231 ; 5.814 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 494 ;37.586 ;24.130
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1772 ;16.101 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;17.649 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1536 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11227 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2075 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2254 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6819 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4954 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5146 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 298 ; 0.170 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.181 ; 0.200
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): 30 ; 0.135 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 100 ; 0.195 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.240 ; 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): 7986 ; 0.884 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2514 ; 0.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9851 ; 1.010 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4824 ; 1.498 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3994 ; 2.131 ; 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 : 6
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 1 A 221
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7200 51.8410 28.1660
REMARK 3 T TENSOR
REMARK 3 T11: -0.0071 T22: -0.0204
REMARK 3 T33: -0.1190 T12: 0.0231
REMARK 3 T13: 0.1322 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.2589 L22: 0.9970
REMARK 3 L33: 0.7901 L12: 0.0156
REMARK 3 L13: 0.7961 L23: -0.2399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: 0.0558 S13: -0.5332
REMARK 3 S21: 0.0563 S22: -0.0003 S23: -0.1555
REMARK 3 S31: 0.0824 S32: 0.0820 S33: -0.0764
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 1 B 221
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1660 86.2840 23.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0912 T22: -0.0519
REMARK 3 T33: -0.1778 T12: -0.0687
REMARK 3 T13: 0.0739 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 2.1487 L22: 1.7470
REMARK 3 L33: 1.0736 L12: 0.0545
REMARK 3 L13: -0.4556 L23: -0.3977
REMARK 3 S TENSOR
REMARK 3 S11: -0.0582 S12: 0.1012 S13: 0.4100
REMARK 3 S21: 0.0012 S22: -0.0626 S23: -0.2068
REMARK 3 S31: -0.3771 S32: 0.1355 S33: 0.1208
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 1 C 219
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0200 122.7470 4.3390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1148 T22: -0.0075
REMARK 3 T33: -0.2817 T12: 0.0692
REMARK 3 T13: 0.1322 T23: 0.0560
REMARK 3 L TENSOR
REMARK 3 L11: 1.4644 L22: 3.2012
REMARK 3 L33: 1.5276 L12: -0.2343
REMARK 3 L13: 0.1921 L23: -0.9274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0502 S12: 0.0093 S13: 0.1875
REMARK 3 S21: -0.0475 S22: 0.1276 S23: 0.3603
REMARK 3 S31: -0.4130 S32: -0.4456 S33: -0.0774
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 1 D 215
REMARK 3 ORIGIN FOR THE GROUP (A): 77.7350 107.1190 8.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: -0.0788
REMARK 3 T33: -0.1043 T12: -0.0732
REMARK 3 T13: 0.1256 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 2.0051 L22: 2.6060
REMARK 3 L33: 0.9770 L12: 0.2398
REMARK 3 L13: 0.6022 L23: 0.3031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: 0.0244 S13: -0.1593
REMARK 3 S21: 0.0247 S22: 0.0313 S23: -0.7464
REMARK 3 S31: 0.0514 S32: 0.1107 S33: -0.0833
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 220
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3910 106.9070 10.7950
REMARK 3 T TENSOR
REMARK 3 T11: -0.0176 T22: 0.1204
REMARK 3 T33: -0.2063 T12: -0.0477
REMARK 3 T13: 0.1925 T23: 0.0886
REMARK 3 L TENSOR
REMARK 3 L11: 2.1327 L22: 2.7520
REMARK 3 L33: 1.6503 L12: 0.5515
REMARK 3 L13: 0.0836 L23: -0.8624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: -0.1110 S13: 0.0675
REMARK 3 S21: 0.1437 S22: 0.2111 S23: 0.6995
REMARK 3 S31: -0.0708 S32: -0.5794 S33: -0.2337
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 219
REMARK 3 ORIGIN FOR THE GROUP (A): 69.6880 91.2640 4.2130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1635 T22: -0.1213
REMARK 3 T33: -0.1912 T12: -0.0418
REMARK 3 T13: 0.1398 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 1.5195 L22: 2.5521
REMARK 3 L33: 0.9622 L12: 0.4337
REMARK 3 L13: 0.3139 L23: 0.4420
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: 0.1381 S13: -0.3129
REMARK 3 S21: -0.0638 S22: 0.0888 S23: -0.4150
REMARK 3 S31: 0.3222 S32: 0.0823 S33: -0.1397
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3E3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.974
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76059
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 39.406
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.51600
REMARK 200 R SYM FOR SHELL (I) : 0.51600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.8 M AMMONIUM SULFATE,
REMARK 280 4% PEG 400, 12 MG/ML PROTEIN, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 115.96250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.61550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 115.96250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 72.61550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -255.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 -3.52911
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 52.85431
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -227.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 ASN A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 TYR A 25
REMARK 465 PHE A 26
REMARK 465 LYS A 27
REMARK 465 GLU A 28
REMARK 465 LEU A 29
REMARK 465 ALA A 30
REMARK 465 ASP A 31
REMARK 465 HIS A 32
REMARK 465 LYS A 222
REMARK 465 LYS A 223
REMARK 465 ASP A 224
REMARK 465 HIS A 225
REMARK 465 LEU A 226
REMARK 465 GLU A 227
REMARK 465 ASN A 228
REMARK 465 THR A 229
REMARK 465 LYS B 19
REMARK 465 GLU B 20
REMARK 465 GLU B 21
REMARK 465 ASN B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 TYR B 25
REMARK 465 PHE B 26
REMARK 465 LYS B 27
REMARK 465 GLU B 28
REMARK 465 LEU B 29
REMARK 465 ALA B 30
REMARK 465 ASP B 31
REMARK 465 HIS B 32
REMARK 465 LYS B 222
REMARK 465 LYS B 223
REMARK 465 ASP B 224
REMARK 465 HIS B 225
REMARK 465 LEU B 226
REMARK 465 GLU B 227
REMARK 465 ASN B 228
REMARK 465 THR B 229
REMARK 465 LYS C 19
REMARK 465 GLU C 20
REMARK 465 GLU C 21
REMARK 465 ASN C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 TYR C 25
REMARK 465 PHE C 26
REMARK 465 LYS C 27
REMARK 465 GLU C 28
REMARK 465 LEU C 29
REMARK 465 ALA C 30
REMARK 465 ASP C 31
REMARK 465 HIS C 32
REMARK 465 GLN C 33
REMARK 465 ILE C 220
REMARK 465 LEU C 221
REMARK 465 LYS C 222
REMARK 465 LYS C 223
REMARK 465 ASP C 224
REMARK 465 HIS C 225
REMARK 465 LEU C 226
REMARK 465 GLU C 227
REMARK 465 ASN C 228
REMARK 465 THR C 229
REMARK 465 LYS D 19
REMARK 465 GLU D 20
REMARK 465 GLU D 21
REMARK 465 ASN D 22
REMARK 465 SER D 23
REMARK 465 THR D 24
REMARK 465 TYR D 25
REMARK 465 PHE D 26
REMARK 465 LYS D 27
REMARK 465 GLU D 28
REMARK 465 LEU D 29
REMARK 465 ALA D 30
REMARK 465 ASP D 31
REMARK 465 HIS D 32
REMARK 465 GLN D 33
REMARK 465 ASP D 216
REMARK 465 GLU D 217
REMARK 465 GLU D 218
REMARK 465 ASN D 219
REMARK 465 ILE D 220
REMARK 465 LEU D 221
REMARK 465 LYS D 222
REMARK 465 LYS D 223
REMARK 465 ASP D 224
REMARK 465 HIS D 225
REMARK 465 LEU D 226
REMARK 465 GLU D 227
REMARK 465 ASN D 228
REMARK 465 THR D 229
REMARK 465 LYS E 19
REMARK 465 GLU E 20
REMARK 465 GLU E 21
REMARK 465 ASN E 22
REMARK 465 SER E 23
REMARK 465 THR E 24
REMARK 465 TYR E 25
REMARK 465 PHE E 26
REMARK 465 LYS E 27
REMARK 465 GLU E 28
REMARK 465 LEU E 29
REMARK 465 ALA E 30
REMARK 465 ASP E 31
REMARK 465 LEU E 221
REMARK 465 LYS E 222
REMARK 465 LYS E 223
REMARK 465 ASP E 224
REMARK 465 HIS E 225
REMARK 465 LEU E 226
REMARK 465 GLU E 227
REMARK 465 ASN E 228
REMARK 465 THR E 229
REMARK 465 LYS F 19
REMARK 465 GLU F 20
REMARK 465 GLU F 21
REMARK 465 ASN F 22
REMARK 465 SER F 23
REMARK 465 THR F 24
REMARK 465 TYR F 25
REMARK 465 PHE F 26
REMARK 465 LYS F 27
REMARK 465 GLU F 28
REMARK 465 LEU F 29
REMARK 465 ALA F 30
REMARK 465 ASP F 31
REMARK 465 ILE F 220
REMARK 465 LEU F 221
REMARK 465 LYS F 222
REMARK 465 LYS F 223
REMARK 465 ASP F 224
REMARK 465 HIS F 225
REMARK 465 LEU F 226
REMARK 465 GLU F 227
REMARK 465 ASN F 228
REMARK 465 THR F 229
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 OH TYR D 181 O2 SO4 D 231 1.95
REMARK 500 OH TYR A 181 O2 SO4 A 234 2.06
REMARK 500 N ARG B 46 O3 SO4 B 232 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O4 SO4 A 233 O HOH A 267 2556 1.94
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 D 44 CB - CA - C ANGL. DEV. = -14.6 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 SER B 45 126.97 -39.52
REMARK 500 ASP B 110 44.54 -100.26
REMARK 500 SER B 197 170.63 176.03
REMARK 500 GLU B 217 -50.41 78.24
REMARK 500 ARG C 46 -79.42 -59.54
REMARK 500 ASN C 68 61.98 39.35
REMARK 500 GLU C 218 38.32 -76.53
REMARK 500 ARG D 17 19.94 -66.95
REMARK 500 VAL D 87 -61.60 -104.04
REMARK 500 ASP E 2 -48.53 -9.44
REMARK 500 SER E 45 131.23 -19.16
REMARK 500 ASN E 54 38.01 38.69
REMARK 500 SER F 45 132.60 -33.18
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 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 42 SG
REMARK 620 2 ASP A 44 OD2 102.3
REMARK 620 3 HIS A 98 NE2 111.0 89.7
REMARK 620 4 CYS A 101 SG 111.9 126.8 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 42 SG
REMARK 620 2 ASP B 44 OD2 91.6
REMARK 620 3 HIS B 98 NE2 116.0 127.3
REMARK 620 4 CYS B 101 SG 114.1 92.7 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 42 SG
REMARK 620 2 ASP C 44 OD2 98.0
REMARK 620 3 HIS C 98 NE2 114.4 114.6
REMARK 620 4 CYS C 101 SG 112.8 96.9 117.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 42 SG
REMARK 620 2 ASP D 44 OD2 93.1
REMARK 620 3 HIS D 98 NE2 109.1 132.4
REMARK 620 4 CYS D 101 SG 111.0 94.9 114.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 42 SG
REMARK 620 2 ASP E 44 OD2 106.5
REMARK 620 3 HIS E 98 NE2 107.5 121.4
REMARK 620 4 CYS E 101 SG 111.6 91.7 117.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 230 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 42 SG
REMARK 620 2 ASP F 44 OD2 99.4
REMARK 620 3 HIS F 98 NE2 114.9 122.5
REMARK 620 4 CYS F 101 SG 112.9 96.5 109.2
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 ZN A 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 231
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8C RELATED DB: PDB
REMARK 900 RELATED ID: 2A8D RELATED DB: PDB
REMARK 900 RELATED ID: 3E24 RELATED DB: PDB
REMARK 900 RELATED ID: 3E28 RELATED DB: PDB
REMARK 900 RELATED ID: 3E2A RELATED DB: PDB
REMARK 900 RELATED ID: 3E2W RELATED DB: PDB
REMARK 900 RELATED ID: 3E2X RELATED DB: PDB
REMARK 900 RELATED ID: 3E31 RELATED DB: PDB
REMARK 900 RELATED ID: 3E3F RELATED DB: PDB
REMARK 900 RELATED ID: 3E3I RELATED DB: PDB
DBREF 3E3G A 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 3E3G B 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 3E3G C 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 3E3G D 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 3E3G E 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 3E3G F 1 229 UNP P45148 CAN_HAEIN 1 229
SEQADV 3E3G ALA A 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 3E3G ALA B 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 3E3G ALA C 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 3E3G ALA D 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 3E3G ALA E 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 3E3G ALA F 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQRES 1 A 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 A 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 A 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 A 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 A 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 A 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 A 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 A 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 A 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 A 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 A 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 A 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 A 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 A 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 A 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 A 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 A 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 A 229 LYS LYS ASP HIS LEU GLU ASN THR
SEQRES 1 B 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 B 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 B 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 B 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 B 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 B 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 B 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 B 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 B 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 B 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 B 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 B 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 B 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 B 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 B 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 B 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 B 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 B 229 LYS LYS ASP HIS LEU GLU ASN THR
SEQRES 1 C 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 C 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 C 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 C 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 C 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 C 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 C 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 C 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 C 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 C 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 C 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 C 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 C 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 C 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 C 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 C 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 C 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 C 229 LYS LYS ASP HIS LEU GLU ASN THR
SEQRES 1 D 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 D 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 D 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 D 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 D 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 D 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 D 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 D 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 D 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 D 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 D 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 D 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 D 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 D 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 D 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 D 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 D 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 D 229 LYS LYS ASP HIS LEU GLU ASN THR
SEQRES 1 E 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 E 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 E 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 E 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 E 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 E 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 E 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 E 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 E 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 E 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 E 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 E 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 E 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 E 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 E 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 E 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 E 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 E 229 LYS LYS ASP HIS LEU GLU ASN THR
SEQRES 1 F 229 MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES 2 F 229 TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES 3 F 229 LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES 4 F 229 ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES 5 F 229 THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES 6 F 229 VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES 7 F 229 SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES 8 F 229 HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES 9 F 229 HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES 10 F 229 ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES 11 F 229 GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES 12 F 229 ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES 13 F 229 ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES 14 F 229 ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES 15 F 229 VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES 16 F 229 THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES 17 F 229 ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES 18 F 229 LYS LYS ASP HIS LEU GLU ASN THR
HET ZN A 230 1
HET SO4 A 231 5
HET SO4 A 232 5
HET SO4 A 233 5
HET SO4 A 234 5
HET ZN B 230 1
HET SO4 B 231 5
HET SO4 B 232 5
HET ZN C 230 1
HET SO4 C 231 5
HET SO4 C 232 5
HET ZN D 230 1
HET SO4 D 231 5
HET ZN E 230 1
HET SO4 E 231 5
HET SO4 E 232 5
HET SO4 E 233 5
HET ZN F 230 1
HET SO4 F 231 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 7 ZN 6(ZN 2+)
FORMUL 8 SO4 13(O4 S 2-)
FORMUL 26 HOH *133(H2 O)
HELIX 1 1 MET A 1 MET A 18 1 18
HELIX 2 2 PRO A 48 ASN A 54 1 7
HELIX 3 3 ASP A 74 VAL A 87 1 14
HELIX 4 4 CYS A 101 ALA A 109 1 9
HELIX 5 5 GLY A 114 HIS A 130 1 17
HELIX 6 6 HIS A 130 LYS A 136 1 7
HELIX 7 7 LEU A 137 GLU A 140 5 4
HELIX 8 8 LYS A 141 ARG A 160 1 20
HELIX 9 9 THR A 161 ARG A 170 1 10
HELIX 10 10 SER A 197 SER A 213 1 17
HELIX 11 11 ASP A 216 ILE A 220 5 5
HELIX 12 12 MET B 1 MET B 18 1 18
HELIX 13 13 PRO B 48 ASN B 54 1 7
HELIX 14 14 ASP B 74 VAL B 87 1 14
HELIX 15 15 CYS B 101 ALA B 109 1 9
HELIX 16 16 GLY B 114 HIS B 130 1 17
HELIX 17 17 HIS B 130 LYS B 136 1 7
HELIX 18 18 LEU B 137 GLU B 140 5 4
HELIX 19 19 LYS B 141 ARG B 160 1 20
HELIX 20 20 THR B 161 ARG B 170 1 10
HELIX 21 21 SER B 197 SER B 213 1 17
HELIX 22 22 MET C 1 ARG C 17 1 17
HELIX 23 23 PRO C 48 ASN C 54 1 7
HELIX 24 24 ASP C 74 VAL C 87 1 14
HELIX 25 25 CYS C 101 ALA C 109 1 9
HELIX 26 26 LEU C 115 HIS C 130 1 16
HELIX 27 27 HIS C 130 LYS C 136 1 7
HELIX 28 28 LEU C 137 GLU C 140 5 4
HELIX 29 29 LYS C 141 THR C 161 1 21
HELIX 30 30 THR C 161 ARG C 170 1 10
HELIX 31 31 SER C 197 ILE C 214 1 18
HELIX 32 32 MET D 1 ARG D 17 1 17
HELIX 33 33 PRO D 48 ASN D 54 1 7
HELIX 34 34 ASP D 74 VAL D 87 1 14
HELIX 35 35 CYS D 101 ALA D 109 1 9
HELIX 36 36 LEU D 115 HIS D 130 1 16
HELIX 37 37 HIS D 130 LYS D 136 1 7
HELIX 38 38 SER D 138 ARG D 160 1 23
HELIX 39 39 THR D 161 ARG D 170 1 10
HELIX 40 40 SER D 197 SER D 213 1 17
HELIX 41 41 ASP E 2 MET E 18 1 17
HELIX 42 42 PRO E 48 ASN E 54 1 7
HELIX 43 43 ASP E 74 VAL E 87 1 14
HELIX 44 44 CYS E 101 ALA E 109 1 9
HELIX 45 45 GLY E 114 HIS E 130 1 17
HELIX 46 46 HIS E 130 LEU E 137 1 8
HELIX 47 47 SER E 138 GLU E 140 5 3
HELIX 48 48 LYS E 141 THR E 161 1 21
HELIX 49 49 THR E 161 ARG E 170 1 10
HELIX 50 50 SER E 197 SER E 213 1 17
HELIX 51 51 MET F 1 MET F 18 1 18
HELIX 52 52 PRO F 48 ASN F 54 1 7
HELIX 53 53 ASP F 74 VAL F 87 1 14
HELIX 54 54 CYS F 101 ALA F 109 1 9
HELIX 55 55 GLY F 114 HIS F 130 1 17
HELIX 56 56 HIS F 130 LYS F 136 1 7
HELIX 57 57 SER F 138 ARG F 160 1 23
HELIX 58 58 THR F 161 ARG F 170 1 10
HELIX 59 59 SER F 197 ILE F 214 1 18
SHEET 1 A 5 LEU A 60 ASN A 65 0
SHEET 2 A 5 TYR A 37 CYS A 42 1 N TRP A 39 O PHE A 61
SHEET 3 A 5 HIS A 92 HIS A 98 1 O ILE A 94 N ILE A 40
SHEET 4 A 5 SER A 175 TYR A 181 1 O TRP A 179 N GLY A 97
SHEET 5 A 5 LEU A 188 ALA A 195 -1 O VAL A 189 N VAL A 180
SHEET 1 B 5 LEU B 60 ASN B 65 0
SHEET 2 B 5 TYR B 37 CYS B 42 1 N TRP B 39 O PHE B 61
SHEET 3 B 5 HIS B 92 HIS B 98 1 O ILE B 94 N ILE B 40
SHEET 4 B 5 SER B 175 TYR B 181 1 O TRP B 179 N ILE B 95
SHEET 5 B 5 LEU B 188 ALA B 195 -1 O ALA B 195 N LEU B 176
SHEET 1 C 5 LEU C 60 ASN C 65 0
SHEET 2 C 5 TYR C 37 CYS C 42 1 N TRP C 39 O HIS C 63
SHEET 3 C 5 HIS C 92 HIS C 98 1 O ILE C 94 N LEU C 38
SHEET 4 C 5 SER C 175 TYR C 181 1 O HIS C 177 N ILE C 93
SHEET 5 C 5 LEU C 188 ALA C 195 -1 O ALA C 195 N LEU C 176
SHEET 1 D 5 LEU D 60 ASN D 65 0
SHEET 2 D 5 TYR D 37 CYS D 42 1 N TRP D 39 O PHE D 61
SHEET 3 D 5 HIS D 92 HIS D 98 1 O ILE D 94 N ILE D 40
SHEET 4 D 5 SER D 175 TYR D 181 1 O HIS D 177 N ILE D 95
SHEET 5 D 5 LEU D 188 ALA D 195 -1 O ALA D 195 N LEU D 176
SHEET 1 E 5 LEU E 60 ASN E 65 0
SHEET 2 E 5 TYR E 37 CYS E 42 1 N TRP E 39 O PHE E 61
SHEET 3 E 5 HIS E 92 HIS E 98 1 O ILE E 94 N ILE E 40
SHEET 4 E 5 SER E 175 TYR E 181 1 O TRP E 179 N GLY E 97
SHEET 5 E 5 LEU E 188 ALA E 195 -1 O VAL E 189 N VAL E 180
SHEET 1 F 5 LEU F 60 ASN F 65 0
SHEET 2 F 5 TYR F 37 CYS F 42 1 N TRP F 39 O PHE F 61
SHEET 3 F 5 HIS F 92 HIS F 98 1 O ILE F 94 N ILE F 40
SHEET 4 F 5 SER F 175 TYR F 181 1 O HIS F 177 N ILE F 95
SHEET 5 F 5 LEU F 188 ALA F 195 -1 O GLN F 191 N GLY F 178
LINK SG CYS A 42 ZN ZN A 230 1555 1555 2.36
LINK OD2 ASP A 44 ZN ZN A 230 1555 1555 1.97
LINK NE2 HIS A 98 ZN ZN A 230 1555 1555 2.08
LINK SG CYS A 101 ZN ZN A 230 1555 1555 2.31
LINK SG CYS B 42 ZN ZN B 230 1555 1555 2.30
LINK OD2 ASP B 44 ZN ZN B 230 1555 1555 2.58
LINK NE2 HIS B 98 ZN ZN B 230 1555 1555 2.12
LINK SG CYS B 101 ZN ZN B 230 1555 1555 2.29
LINK SG CYS C 42 ZN ZN C 230 1555 1555 2.32
LINK OD2 ASP C 44 ZN ZN C 230 1555 1555 2.03
LINK NE2 HIS C 98 ZN ZN C 230 1555 1555 2.11
LINK SG CYS C 101 ZN ZN C 230 1555 1555 2.27
LINK SG CYS D 42 ZN ZN D 230 1555 1555 2.34
LINK OD2 ASP D 44 ZN ZN D 230 1555 1555 1.99
LINK NE2 HIS D 98 ZN ZN D 230 1555 1555 2.09
LINK SG CYS D 101 ZN ZN D 230 1555 1555 2.30
LINK SG CYS E 42 ZN ZN E 230 1555 1555 2.32
LINK OD2 ASP E 44 ZN ZN E 230 1555 1555 2.01
LINK NE2 HIS E 98 ZN ZN E 230 1555 1555 2.11
LINK SG CYS E 101 ZN ZN E 230 1555 1555 2.30
LINK SG CYS F 42 ZN ZN F 230 1555 1555 2.35
LINK OD2 ASP F 44 ZN ZN F 230 1555 1555 1.99
LINK NE2 HIS F 98 ZN ZN F 230 1555 1555 2.11
LINK SG CYS F 101 ZN ZN F 230 1555 1555 2.29
SITE 1 AC1 4 CYS A 42 ASP A 44 HIS A 98 CYS A 101
SITE 1 AC2 5 ARG A 124 PHE A 128 HOH A 268 ARG B 160
SITE 2 AC2 5 ARG B 198
SITE 1 AC3 5 ARG A 160 LYS A 165 ARG A 198 ARG B 124
SITE 2 AC3 5 PHE B 128
SITE 1 AC4 5 PRO A 48 ALA A 49 ARG A 64 HOH A 251
SITE 2 AC4 5 HOH A 267
SITE 1 AC5 7 ASP A 44 SER A 45 ARG A 46 VAL A 47
SITE 2 AC5 7 HIS A 98 TYR A 181 VAL A 183
SITE 1 AC6 4 CYS B 42 ASP B 44 HIS B 98 CYS B 101
SITE 1 AC7 3 PRO B 48 ARG B 64 HOH B 252
SITE 1 AC8 6 SER B 45 ARG B 46 VAL B 47 HIS B 98
SITE 2 AC8 6 TYR B 181 VAL B 183
SITE 1 AC9 4 CYS C 42 ASP C 44 HIS C 98 CYS C 101
SITE 1 BC1 4 LEU C 121 ARG C 124 ARG D 160 ARG D 198
SITE 1 BC2 6 ARG C 160 LYS C 165 ARG C 198 HOH C 252
SITE 2 BC2 6 ARG D 124 PHE D 128
SITE 1 BC3 4 CYS D 42 ASP D 44 HIS D 98 CYS D 101
SITE 1 BC4 7 ASP D 44 SER D 45 ARG D 46 VAL D 47
SITE 2 BC4 7 HIS D 98 TYR D 181 VAL D 183
SITE 1 BC5 4 CYS E 42 ASP E 44 HIS E 98 CYS E 101
SITE 1 BC6 5 SER C 45 ARG C 64 PRO E 48 VAL E 62
SITE 2 BC6 5 ARG E 64
SITE 1 BC7 5 LEU E 121 ARG E 124 PHE E 128 ARG F 160
SITE 2 BC7 5 ARG F 198
SITE 1 BC8 5 ARG E 160 ARG E 198 LEU F 121 ARG F 124
SITE 2 BC8 5 PHE F 128
SITE 1 BC9 4 CYS F 42 ASP F 44 HIS F 98 CYS F 101
SITE 1 CC1 6 PRO D 48 ARG D 64 PRO F 48 ALA F 49
SITE 2 CC1 6 ARG F 64 HOH F 248
CRYST1 231.925 145.231 52.972 90.00 93.82 90.00 C 1 2 1 24
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 0.004312 0.000000 0.000288 0.00000
SCALE2 0.000000 0.006886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018920 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
