HEADER LYASE 29-AUG-14 4WAM
TITLE H. INFLUENZAE BETA-CARBONIC ANHYDRASE VARIANT W39V/G41A/P48S/A49P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-CARBONIC ANHYDRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE 2;
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: 71421;
SOURCE 4 STRAIN: ATCC 51907 / DSM 11121 / KW20 / RD;
SOURCE 5 GENE: CAN, HI_1301;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS BETA-CARBONIC ANHYDRASE ALLOSTERIC SITE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.S.ROWLETT,K.M.HOFFMAN
REVDAT 6 27-DEC-23 4WAM 1 REMARK
REVDAT 5 27-NOV-19 4WAM 1 REMARK
REVDAT 4 20-SEP-17 4WAM 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 28-JAN-15 4WAM 1 JRNL
REVDAT 2 14-JAN-15 4WAM 1 JRNL
REVDAT 1 31-DEC-14 4WAM 0
JRNL AUTH K.M.HOFFMANN,H.R.MILLION-PEREZ,R.MERKHOFER,H.NICHOLSON,
JRNL AUTH 2 R.S.ROWLETT
JRNL TITL ALLOSTERIC REVERSION OF HAEMOPHILUS INFLUENZAE BETA-CARBONIC
JRNL TITL 2 ANHYDRASE VIA A PROLINE SHIFT.
JRNL REF BIOCHEMISTRY V. 54 598 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 25506786
JRNL DOI 10.1021/BI501116E
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 21239
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1163
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1173
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.6280
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.6630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2835
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 0.12000
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): 0.302
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.246
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.166
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.834
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.878
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.846
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2924 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2834 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3955 ; 1.793 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6477 ; 0.918 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 7.526 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;34.839 ;23.712
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 506 ;19.174 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.506 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 453 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3236 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 690 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1428 ; 1.631 ; 1.735
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1427 ; 1.631 ; 1.732
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1775 ; 2.744 ; 2.574
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1776 ; 2.743 ; 2.577
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1496 ; 1.989 ; 2.038
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1478 ; 1.886 ; 2.017
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2155 ; 3.207 ; 2.933
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3417 ; 6.081 ;14.371
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3369 ; 5.869 ;14.219
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 : 2
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 34 A 221
REMARK 3 ORIGIN FOR THE GROUP (A): -8.821 3.319 17.499
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: 0.1223
REMARK 3 T33: 0.0174 T12: 0.0057
REMARK 3 T13: -0.0095 T23: 0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.3453 L22: 0.6665
REMARK 3 L33: 0.7042 L12: -0.2758
REMARK 3 L13: 0.2208 L23: 0.1805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0107 S12: 0.2223 S13: 0.1255
REMARK 3 S21: -0.0862 S22: -0.0041 S23: 0.0072
REMARK 3 S31: -0.0096 S32: -0.0065 S33: -0.0066
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 34 B 217
REMARK 3 ORIGIN FOR THE GROUP (A): -2.808 -18.636 32.813
REMARK 3 T TENSOR
REMARK 3 T11: 0.0172 T22: 0.0338
REMARK 3 T33: 0.0415 T12: 0.0147
REMARK 3 T13: 0.0030 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.4342 L22: 0.7202
REMARK 3 L33: 0.6515 L12: -0.3170
REMARK 3 L13: 0.1856 L23: -0.0758
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: -0.0004 S13: -0.2002
REMARK 3 S21: -0.0421 S22: 0.0056 S23: 0.0262
REMARK 3 S31: 0.0831 S32: 0.0290 S33: -0.0038
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD RUBY CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22403
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 96.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: ORTHORHOMBIC PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.30 M SODIUM POTASSIUM PHOSPHATE, 12
REMARK 280 MG/ML PROTEIN, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.08100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.93400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.12950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.93400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.08100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.12950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.08100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.12950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.93400
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.12950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.08100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 71.93400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.0 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 71.93400
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 418 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 3
REMARK 465 ILE A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 LEU A 7
REMARK 465 PHE A 8
REMARK 465 ALA A 9
REMARK 465 ASN A 10
REMARK 465 ASN A 11
REMARK 465 TYR A 12
REMARK 465 SER A 13
REMARK 465 TRP A 14
REMARK 465 ALA A 15
REMARK 465 GLN A 16
REMARK 465 ARG A 17
REMARK 465 MET A 18
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 GLN A 33
REMARK 465 THR A 53
REMARK 465 ASN A 54
REMARK 465 LEU A 55
REMARK 465 GLU A 56
REMARK 465 ASP A 182
REMARK 465 VAL A 183
REMARK 465 ASN A 184
REMARK 465 ASP A 185
REMARK 465 ASP A 190
REMARK 465 GLN A 191
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 MET B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 3
REMARK 465 ILE B 4
REMARK 465 LYS B 5
REMARK 465 GLN B 6
REMARK 465 LEU B 7
REMARK 465 PHE B 8
REMARK 465 ALA B 9
REMARK 465 ASN B 10
REMARK 465 ASN B 11
REMARK 465 TYR B 12
REMARK 465 SER B 13
REMARK 465 TRP B 14
REMARK 465 ALA B 15
REMARK 465 GLN B 16
REMARK 465 ARG B 17
REMARK 465 MET B 18
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 GLN B 33
REMARK 465 ASN B 54
REMARK 465 LEU B 55
REMARK 465 GLU B 56
REMARK 465 PRO B 57
REMARK 465 GLU B 218
REMARK 465 ASN B 219
REMARK 465 ILE B 220
REMARK 465 LEU B 221
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 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 NH1 ARG A 64 O1 PO4 A 303 2.07
REMARK 500 OD2 ASP B 110 O3 PO4 A 304 2.07
REMARK 500 O HOH A 459 O HOH B 448 2.12
REMARK 500 OD2 ASP A 110 O1 PO4 A 305 2.13
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 O HOH A 464 O HOH A 464 7455 1.80
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 A 125 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 110 C - N - CA ANGL. DEV. = -15.3 DEGREES
REMARK 500 ASP B 182 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 SER A 48 135.89 -39.53
REMARK 500 GLU A 50 23.22 -67.01
REMARK 500 LYS A 51 -159.59 -73.20
REMARK 500 LEU A 188 48.66 -100.00
REMARK 500 ALA B 67 30.07 71.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 50 LYS A 51 145.01
REMARK 500 THR B 34 PRO B 35 -143.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 462 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 464 DISTANCE = 7.31 ANGSTROMS
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 42 SG
REMARK 620 2 ASP A 44 OD1 98.1
REMARK 620 3 HIS A 98 NE2 113.1 88.4
REMARK 620 4 CYS A 101 SG 113.1 132.9 109.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 42 SG
REMARK 620 2 ASP B 44 OD1 101.0
REMARK 620 3 HIS B 98 NE2 119.0 92.0
REMARK 620 4 CYS B 101 SG 116.0 125.1 102.6
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8D RELATED DB: PDB
REMARK 900 2A8D IS THE WILD-TYPE ENZYME COMPLEXED WITH BICARBONATE
REMARK 900 RELATED ID: 4WAJ RELATED DB: PDB
REMARK 900 RELATED ID: 4WAM RELATED DB: PDB
DBREF 4WAM A 1 229 UNP P45148 CAN_HAEIN 1 229
DBREF 4WAM B 1 229 UNP P45148 CAN_HAEIN 1 229
SEQADV 4WAM VAL A 39 UNP P45148 TRP 39 ENGINEERED MUTATION
SEQADV 4WAM ALA A 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 4WAM SER A 48 UNP P45148 PRO 48 ENGINEERED MUTATION
SEQADV 4WAM PRO A 49 UNP P45148 ALA 49 ENGINEERED MUTATION
SEQADV 4WAM VAL B 39 UNP P45148 TRP 39 ENGINEERED MUTATION
SEQADV 4WAM ALA B 41 UNP P45148 GLY 41 ENGINEERED MUTATION
SEQADV 4WAM SER B 48 UNP P45148 PRO 48 ENGINEERED MUTATION
SEQADV 4WAM PRO B 49 UNP P45148 ALA 49 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 VAL
SEQRES 4 A 229 ILE ALA CYS SER ASP SER ARG VAL SER PRO 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 VAL
SEQRES 4 B 229 ILE ALA CYS SER ASP SER ARG VAL SER PRO 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
HET ZN A 301 1
HET PO4 A 302 5
HET PO4 A 303 5
HET PO4 A 304 5
HET PO4 A 305 5
HET ZN B 301 1
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 PO4 4(O4 P 3-)
FORMUL 9 HOH *144(H2 O)
HELIX 1 AA1 ASP A 74 VAL A 87 1 14
HELIX 2 AA2 CYS A 101 ASP A 110 1 10
HELIX 3 AA3 LEU A 115 HIS A 130 1 16
HELIX 4 AA4 HIS A 130 LYS A 136 1 7
HELIX 5 AA5 LEU A 137 GLU A 140 5 4
HELIX 6 AA6 LYS A 141 ARG A 160 1 20
HELIX 7 AA7 THR A 161 ARG A 170 1 10
HELIX 8 AA8 SER A 197 ILE A 214 1 18
HELIX 9 AA9 SER B 48 THR B 53 1 6
HELIX 10 AB1 ASP B 74 VAL B 87 1 14
HELIX 11 AB2 CYS B 101 ALA B 109 1 9
HELIX 12 AB3 LEU B 115 HIS B 130 1 16
HELIX 13 AB4 HIS B 130 LEU B 137 1 8
HELIX 14 AB5 LYS B 141 THR B 161 1 21
HELIX 15 AB6 THR B 161 ARG B 170 1 10
HELIX 16 AB7 SER B 197 SER B 213 1 17
SHEET 1 AA1 5 LEU A 60 ASN A 65 0
SHEET 2 AA1 5 TYR A 37 CYS A 42 1 N VAL A 39 O HIS A 63
SHEET 3 AA1 5 HIS A 92 HIS A 98 1 O ILE A 94 N ILE A 40
SHEET 4 AA1 5 SER A 175 TYR A 181 1 O TRP A 179 N GLY A 97
SHEET 5 AA1 5 VAL A 193 ALA A 195 -1 O ALA A 195 N LEU A 176
SHEET 1 AA2 5 LEU B 60 ASN B 65 0
SHEET 2 AA2 5 TYR B 37 CYS B 42 1 N TYR B 37 O PHE B 61
SHEET 3 AA2 5 HIS B 92 HIS B 98 1 O ILE B 94 N ILE B 40
SHEET 4 AA2 5 SER B 175 ASP B 182 1 O HIS B 177 N ILE B 95
SHEET 5 AA2 5 PHE B 187 ALA B 195 -1 O ALA B 195 N LEU B 176
LINK SG CYS A 42 ZN ZN A 301 1555 1555 2.31
LINK OD1 ASP A 44 ZN ZN A 301 1555 1555 1.96
LINK NE2 HIS A 98 ZN ZN A 301 1555 1555 2.04
LINK SG CYS A 101 ZN ZN A 301 1555 1555 2.23
LINK SG CYS B 42 ZN ZN B 301 1555 1555 2.33
LINK OD1 ASP B 44 ZN ZN B 301 1555 1555 1.98
LINK NE2 HIS B 98 ZN ZN B 301 1555 1555 2.06
LINK SG CYS B 101 ZN ZN B 301 1555 1555 2.25
SITE 1 AC1 4 CYS A 42 ASP A 44 HIS A 98 CYS A 101
SITE 1 AC2 9 THR A 73 ASP A 74 PHE A 75 ASN A 76
SITE 2 AC2 9 HOH A 403 THR B 73 ASP B 74 PHE B 75
SITE 3 AC2 9 ASN B 76
SITE 1 AC3 8 PRO A 49 VAL A 62 ARG A 64 SER B 48
SITE 2 AC3 8 PRO B 49 GLU B 50 VAL B 62 ARG B 64
SITE 1 AC4 9 ARG A 160 LYS A 165 ARG A 198 HOH A 433
SITE 2 AC4 9 HOH A 437 HOH A 446 ASP B 110 LEU B 121
SITE 3 AC4 9 ARG B 124
SITE 1 AC5 6 ASP A 110 LEU A 121 ARG A 124 ARG B 160
SITE 2 AC5 6 LYS B 165 ARG B 198
SITE 1 AC6 4 CYS B 42 ASP B 44 HIS B 98 CYS B 101
CRYST1 48.162 130.259 143.868 90.00 90.00 90.00 I 21 21 21 16
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 0.020763 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006951 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
