HEADER LYASE/LYASE INHIBITOR 29-SEP-16 5THI
TITLE CRYSTAL STRUCTURE OF 2-HYDROXYCYCLOHEPTA-2,4,6-TRIEN-1-ONE BOUND TO
TITLE 2 HUMAN CARBONIC ANHYDRASE 2 L198G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II,CARBONIC ANHYDRASE C,CAC,CARBONIC
COMPND 5 ANHYDRASE II,CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBONIC ANHYDRASE 2, COMPLEX, METALLOENZYME INHIBITOR, LYASE-LYASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.DICK,S.COHEN
REVDAT 3 04-OCT-23 5THI 1 REMARK
REVDAT 2 07-JUN-17 5THI 1 JRNL
REVDAT 1 26-APR-17 5THI 0
JRNL AUTH B.L.DICK,A.PATEL,J.A.MCCAMMON,S.M.COHEN
JRNL TITL EFFECT OF DONOR ATOM IDENTITY ON METAL-BINDING PHARMACOPHORE
JRNL TITL 2 COORDINATION.
JRNL REF J. BIOL. INORG. CHEM. V. 22 605 2017
JRNL REFN ESSN 1432-1327
JRNL PMID 28389830
JRNL DOI 10.1007/S00775-017-1454-3
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 36588
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1885
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2578
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.077
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.491
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2263 ; 0.022 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2084 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3082 ; 2.147 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4846 ; 1.554 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 278 ; 7.223 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;33.717 ;24.854
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 373 ;13.468 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;23.579 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2588 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 518 ; 0.002 ; 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): 1085 ; 1.551 ; 1.133
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1084 ; 1.532 ; 1.129
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1372 ; 2.312 ; 1.694
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1373 ; 2.316 ; 1.697
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1178 ; 2.575 ; 1.406
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1179 ; 2.574 ; 1.408
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1711 ; 3.892 ; 1.994
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2707 ; 5.153 ;10.269
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2708 ; 5.152 ;10.278
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5THI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224237.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5478
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER SMART 6000
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38528
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 69.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.090
REMARK 200 R MERGE (I) : 0.05380
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.43790
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3KS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, PH 8.0, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 20.68400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
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 O1 GOL A 306 O HOH A 401 2.05
REMARK 500 O HOH A 534 O HOH A 564 2.13
REMARK 500 O HOH A 403 O HOH A 435 2.18
REMARK 500 O LYS A 76 O HOH A 402 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 14 CD GLU A 14 OE1 0.071
REMARK 500 GLU A 14 CD GLU A 14 OE2 0.101
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 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ASP A 101 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ARG A 27 55.23 -144.08
REMARK 500 LYS A 111 -1.33 72.75
REMARK 500 PHE A 176 69.33 -150.41
REMARK 500 ASN A 244 45.01 -94.03
REMARK 500 LYS A 252 -137.45 59.95
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 105.5
REMARK 620 3 HIS A 119 ND1 114.0 93.2
REMARK 620 4 0TR A 302 OA2 105.9 105.6 129.1
REMARK 620 5 0TR A 302 OA1 92.4 162.2 79.1 68.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MBO A 304 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 135 O
REMARK 620 2 MBO A 304 CE1 94.1
REMARK 620 3 GLN A 137 O 108.2 94.1
REMARK 620 N 1 2
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 0TR A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MBO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5THJ RELATED DB: PDB
REMARK 900 RELATED ID: 5THN RELATED DB: PDB
REMARK 900 RELATED ID: 5TH4 RELATED DB: PDB
REMARK 900 RELATED ID: 5TI0 RELATED DB: PDB
DBREF 5THI A 1 261 UNP P00918 CAH2_HUMAN 1 260
SEQADV 5THI GLY A 198 UNP P00918 LEU 197 ENGINEERED MUTATION
SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 A 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 A 260 SER GLY THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET 0TR A 302 9
HET CIT A 303 13
HET MBO A 304 10
HET GOL A 305 6
HET GOL A 306 6
HETNAM ZN ZINC ION
HETNAM 0TR 2-HYDROXYCYCLOHEPTA-2,4,6-TRIEN-1-ONE
HETNAM CIT CITRIC ACID
HETNAM MBO MERCURIBENZOIC ACID
HETNAM GOL GLYCEROL
HETSYN 0TR TROPOLONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 0TR C7 H6 O2
FORMUL 4 CIT C6 H8 O7
FORMUL 5 MBO C7 H5 HG O2
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 HOH *207(H2 O)
HELIX 1 AA1 GLY A 12 TRP A 16 5 5
HELIX 2 AA2 PHE A 20 GLY A 25 5 6
HELIX 3 AA3 LYS A 127 GLY A 129 5 3
HELIX 4 AA4 ASP A 130 VAL A 135 1 6
HELIX 5 AA5 LYS A 154 GLY A 156 5 3
HELIX 6 AA6 LEU A 157 LEU A 164 1 8
HELIX 7 AA7 ASP A 165 LYS A 168 5 4
HELIX 8 AA8 ASP A 180 LEU A 185 5 6
HELIX 9 AA9 SER A 219 ARG A 227 1 9
SHEET 1 AA1 2 ASP A 32 ILE A 33 0
SHEET 2 AA1 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 AA210 LYS A 39 TYR A 40 0
SHEET 2 AA210 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 AA210 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 AA210 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AA210 LEU A 141 VAL A 150 1 N GLY A 145 O ILE A 210
SHEET 6 AA210 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 146
SHEET 7 AA210 TYR A 88 TRP A 97 -1 N GLN A 92 O VAL A 121
SHEET 8 AA210 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 9 AA210 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 10 AA210 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 AA3 6 LEU A 47 SER A 50 0
SHEET 2 AA3 6 VAL A 78 GLY A 81 -1 O VAL A 78 N SER A 50
SHEET 3 AA3 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AA3 6 ALA A 116 ASN A 124 -1 O VAL A 121 N GLN A 92
SHEET 5 AA3 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118
SHEET 6 AA3 6 ILE A 216 VAL A 218 1 O VAL A 218 N LYS A 149
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.08
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.01
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.09
LINK O VAL A 135 HG MBO A 304 1555 1555 2.92
LINK O GLN A 137 HG MBO A 304 1555 1555 2.91
LINK ZN ZN A 301 OA2 0TR A 302 1555 1555 1.90
LINK ZN ZN A 301 OA1 0TR A 302 1555 1555 2.38
CISPEP 1 SER A 29 PRO A 30 0 -2.50
CISPEP 2 PRO A 201 PRO A 202 0 5.97
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 0TR A 302
SITE 1 AC2 10 HIS A 94 HIS A 96 HIS A 119 GLY A 198
SITE 2 AC2 10 THR A 199 THR A 200 ZN A 301 HOH A 417
SITE 3 AC2 10 HOH A 534 HOH A 594
SITE 1 AC3 8 LYS A 111 LYS A 113 LYS A 133 GLN A 137
SITE 2 AC3 8 HOH A 408 HOH A 444 HOH A 448 HOH A 489
SITE 1 AC4 7 VAL A 135 GLN A 136 GLN A 137 PRO A 138
SITE 2 AC4 7 GLU A 205 CYS A 206 HOH A 522
SITE 1 AC5 4 TYR A 7 ASP A 243 TRP A 245 PRO A 247
SITE 1 AC6 7 THR A 35 HIS A 36 ALA A 38 LYS A 39
SITE 2 AC6 7 HOH A 401 HOH A 406 HOH A 410
CRYST1 42.186 41.368 71.727 90.00 104.20 90.00 P 1 21 1 2
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 0.023705 0.000000 0.005997 0.00000
SCALE2 0.000000 0.024173 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
