HEADER LYASE 18-APR-16 5JES
TITLE HUMAN CARBONIC ANHYDRASE II (V121T) COMPLEXED WITH BENZO[D]THIAZOLE-2-
TITLE 2 SULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: B;
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 ANHYDRASE, MUTANT, HYDROPHOBIC, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.FOX,K.KANG,M.SASTRY,W.SHERMAN,B.SANKARAN,P.H.ZWART,G.M.WHITESIDES
REVDAT 6 27-SEP-23 5JES 1 REMARK
REVDAT 5 27-NOV-19 5JES 1 REMARK
REVDAT 4 20-SEP-17 5JES 1 HEADER
REVDAT 3 29-MAR-17 5JES 1 JRNL
REVDAT 2 15-MAR-17 5JES 1 JRNL
REVDAT 1 11-JAN-17 5JES 0
JRNL AUTH J.M.FOX,K.KANG,M.SASTRY,W.SHERMAN,B.SANKARAN,P.H.ZWART,
JRNL AUTH 2 G.M.WHITESIDES
JRNL TITL WATER-RESTRUCTURING MUTATIONS CAN REVERSE THE THERMODYNAMIC
JRNL TITL 2 SIGNATURE OF LIGAND BINDING TO HUMAN CARBONIC ANHYDRASE.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 3833 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28252841
JRNL DOI 10.1002/ANIE.201609409
REMARK 2
REMARK 2 RESOLUTION. 1.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.3
REMARK 3 NUMBER OF REFLECTIONS : 117955
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.122
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.147
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.120
REMARK 3 FREE R VALUE TEST SET COUNT : 3682
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.9063 - 3.5675 0.99 5354 177 0.1205 0.1349
REMARK 3 2 3.5675 - 2.8320 0.98 5277 161 0.1265 0.1426
REMARK 3 3 2.8320 - 2.4742 0.97 5225 184 0.1249 0.1274
REMARK 3 4 2.4742 - 2.2480 0.97 5247 165 0.1182 0.1249
REMARK 3 5 2.2480 - 2.0869 0.96 5238 174 0.1069 0.1464
REMARK 3 6 2.0869 - 1.9639 0.96 5164 149 0.1100 0.1491
REMARK 3 7 1.9639 - 1.8655 0.96 5242 173 0.1078 0.1709
REMARK 3 8 1.8655 - 1.7843 0.96 5191 180 0.1097 0.1246
REMARK 3 9 1.7843 - 1.7156 0.96 5152 165 0.1093 0.1465
REMARK 3 10 1.7156 - 1.6564 0.96 5252 162 0.1073 0.1317
REMARK 3 11 1.6564 - 1.6046 0.96 5213 158 0.1098 0.1732
REMARK 3 12 1.6046 - 1.5588 0.96 5226 158 0.1095 0.1371
REMARK 3 13 1.5588 - 1.5177 0.96 5151 165 0.1137 0.1414
REMARK 3 14 1.5177 - 1.4807 0.96 5186 183 0.1125 0.1381
REMARK 3 15 1.4807 - 1.4470 0.96 5203 150 0.1180 0.1654
REMARK 3 16 1.4470 - 1.4162 0.90 4876 152 0.1211 0.1743
REMARK 3 17 1.4162 - 1.3879 0.85 4546 167 0.1305 0.1886
REMARK 3 18 1.3879 - 1.3617 0.81 4368 122 0.1430 0.2012
REMARK 3 19 1.3617 - 1.3374 0.75 4084 116 0.1481 0.1887
REMARK 3 20 1.3374 - 1.3147 0.70 3765 153 0.1612 0.1949
REMARK 3 21 1.3147 - 1.2935 0.61 3305 102 0.1646 0.2140
REMARK 3 22 1.2935 - 1.2736 0.53 2831 110 0.1737 0.1867
REMARK 3 23 1.2736 - 1.2549 0.47 2553 81 0.1920 0.2316
REMARK 3 24 1.2549 - 1.2372 0.42 2246 69 0.2017 0.2403
REMARK 3 25 1.2372 - 1.2205 0.35 1940 62 0.2179 0.2411
REMARK 3 26 1.2205 - 1.2046 0.27 1438 44 0.2136 0.2679
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2246
REMARK 3 ANGLE : 1.774 3074
REMARK 3 CHIRALITY : 0.189 318
REMARK 3 PLANARITY : 0.007 394
REMARK 3 DIHEDRAL : 12.903 821
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.205
REMARK 200 RESOLUTION RANGE LOW (A) : 34.892
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 3S73
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WE SOAKED MONOCLINIC CRYSTALS OF HCAII
REMARK 280 WITH BTA (EVF) BY CARRYING OUT THE FOLLOWING STEPS: (I) WE
REMARK 280 PREPARED SOAKING SOLUTIONS CONTAINING 1.32 M SODIUM CITRATE, 1
REMARK 280 MM ZNSO4, 100 MM TRIS-HCL (PH 7.8), AND 5 MM LIGAND. (II) WE
REMARK 280 COMBINED 4 UL OF SOAKING SOLUTION AND 1-2 CRYSTALS OF HCAII
REMARK 280 WITHIN A DROP ON THE SURFACE OF A RESERVOIR COVER (EASYXTAL
REMARK 280 CRYSTALSUPPORT, QIAGEN). (III) TO A CLEAR PLASTIC RESERVOIR IN A
REMARK 280 15-RESERVOIR PLATE (EASYXTAL, QIAGEN), WE ADDED 1 ML OF SOAKING
REMARK 280 SOLUTION (WITHOUT LIGAND PRESENT). WE ATTACHED THE RESERVOIR
REMARK 280 COVER TO THE RESERVOIR AND LEFT THE ENTIRE SETUP AT 4 DEG C FOR
REMARK 280 1 WEEK., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 20.64000
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 APPLY THE FOLLOWING TO CHAINS: 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS B 45 CD CE NZ
REMARK 480 ASP B 85 OD2
REMARK 480 LEU B 198 CG CD1 CD2
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 HE2 HIS B 107 HH TYR B 194 1.07
REMARK 500 HE2 HIS B 64 O HOH B 412 1.57
REMARK 500 O HOH B 620 O HOH B 628 1.94
REMARK 500 O HOH B 451 O HOH B 454 1.95
REMARK 500 O HOH B 427 O HOH B 709 1.97
REMARK 500 O HOH B 636 O HOH B 662 1.99
REMARK 500 O HOH B 662 O HOH B 694 1.99
REMARK 500 O HOH B 619 O HOH B 682 2.02
REMARK 500 O HOH B 744 O HOH B 747 2.02
REMARK 500 OE1 GLU B 187 O HOH B 401 2.02
REMARK 500 O LYS B 76 O HOH B 402 2.03
REMARK 500 O HOH B 404 O HOH B 428 2.05
REMARK 500 O HOH B 412 O HOH B 513 2.08
REMARK 500 O HOH B 411 O HOH B 666 2.08
REMARK 500 O HOH B 412 O HOH B 655 2.11
REMARK 500 OE1 GLU B 238 O HOH B 403 2.13
REMARK 500 O HOH B 523 O HOH B 671 2.13
REMARK 500 OE1 GLN B 255 O HOH B 404 2.13
REMARK 500 O HOH B 454 O HOH B 615 2.16
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 N HIS B 3 O HOH B 465 1655 1.93
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 B 27 54.02 -142.03
REMARK 500 LYS B 111 -2.54 75.79
REMARK 500 PHE B 176 72.69 -152.98
REMARK 500 ASN B 244 47.71 -92.98
REMARK 500 LYS B 252 -134.97 52.97
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 B 771 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 772 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 773 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 774 DISTANCE = 6.55 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 B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 94 NE2
REMARK 620 2 HIS B 96 NE2 103.5
REMARK 620 3 HIS B 119 ND1 114.2 99.5
REMARK 620 4 EVF B 302 N 109.4 111.8 117.2
REMARK 620 5 EVF B 302 N 109.1 117.0 113.1 5.6
REMARK 620 6 EVF B 302 S 101.5 140.3 97.8 29.5 24.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EVF B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EVF B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JDV RELATED DB: PDB
REMARK 900 RELATED ID: 5JE7 RELATED DB: PDB
REMARK 900 RELATED ID: 5JEG RELATED DB: PDB
REMARK 900 RELATED ID: 5JEH RELATED DB: PDB
REMARK 900 RELATED ID: 5JEP RELATED DB: PDB
REMARK 900 RELATED ID: 5JG3 RELATED DB: PDB
REMARK 900 RELATED ID: 5JG5 RELATED DB: PDB
DBREF 5JES B 3 260 UNP P00918 CAH2_HUMAN 3 260
SEQADV 5JES THR B 121 UNP P00918 VAL 121 ENGINEERED MUTATION
SEQRES 1 B 258 HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES 2 B 258 TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES 3 B 258 SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES 4 B 258 PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES 5 B 258 THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN
SEQRES 6 B 258 VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES 7 B 258 GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES 8 B 258 HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES 9 B 258 HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES 10 B 258 LEU THR HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES 11 B 258 ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES 12 B 258 PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES 13 B 258 VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES 14 B 258 SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES 15 B 258 PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES 16 B 258 THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES 17 B 258 LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES 18 B 258 LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES 19 B 258 GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES 20 B 258 LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN B 301 1
HET EVF B 302 26
HET EVF B 303 38
HETNAM ZN ZINC ION
HETNAM EVF 1,3-BENZOTHIAZOLE-2-SULFONAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 EVF 2(C7 H6 N2 O2 S2)
FORMUL 5 HOH *374(H2 O)
HELIX 1 AA1 GLY B 12 ASP B 19 5 8
HELIX 2 AA2 PHE B 20 GLY B 25 5 6
HELIX 3 AA3 LYS B 127 GLY B 129 5 3
HELIX 4 AA4 ASP B 130 VAL B 135 1 6
HELIX 5 AA5 LYS B 154 GLY B 156 5 3
HELIX 6 AA6 LEU B 157 LEU B 164 1 8
HELIX 7 AA7 ASP B 165 LYS B 168 5 4
HELIX 8 AA8 ASP B 180 LEU B 185 5 6
HELIX 9 AA9 SER B 219 ARG B 227 1 9
SHEET 1 AA1 2 ASP B 32 ILE B 33 0
SHEET 2 AA1 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 33
SHEET 1 AA210 LYS B 39 TYR B 40 0
SHEET 2 AA210 LYS B 257 ALA B 258 1 O ALA B 258 N LYS B 39
SHEET 3 AA210 TYR B 191 GLY B 196 -1 N THR B 193 O LYS B 257
SHEET 4 AA210 VAL B 207 LEU B 212 -1 O VAL B 207 N GLY B 196
SHEET 5 AA210 LEU B 141 VAL B 150 1 N GLY B 145 O ILE B 210
SHEET 6 AA210 ALA B 116 ASN B 124 -1 N LEU B 118 O ILE B 146
SHEET 7 AA210 TYR B 88 TRP B 97 -1 N HIS B 94 O HIS B 119
SHEET 8 AA210 PHE B 66 PHE B 70 -1 N VAL B 68 O PHE B 93
SHEET 9 AA210 SER B 56 ASN B 61 -1 N LEU B 57 O GLU B 69
SHEET 10 AA210 SER B 173 ASP B 175 -1 O ALA B 174 N ILE B 59
SHEET 1 AA3 6 LEU B 47 SER B 50 0
SHEET 2 AA3 6 VAL B 78 GLY B 81 -1 O VAL B 78 N SER B 50
SHEET 3 AA3 6 TYR B 88 TRP B 97 -1 O TYR B 88 N LEU B 79
SHEET 4 AA3 6 ALA B 116 ASN B 124 -1 O HIS B 119 N HIS B 94
SHEET 5 AA3 6 LEU B 141 VAL B 150 -1 O ILE B 146 N LEU B 118
SHEET 6 AA3 6 ILE B 216 VAL B 218 1 O ILE B 216 N PHE B 147
LINK ND1 HIS B 4 C7 AEVF B 303 1555 1555 1.36
LINK CE1 HIS B 4 N3 BEVF B 303 1555 1555 1.35
LINK CE1 HIS B 4 C8 BEVF B 303 1555 1555 1.09
LINK CE1 HIS B 4 C9 AEVF B 303 1555 1555 1.38
LINK NE2 HIS B 4 C2 AEVF B 303 1555 1555 1.56
LINK NE2 HIS B 4 C2 BEVF B 303 1555 1555 1.37
LINK NE2 HIS B 4 C9 BEVF B 303 1555 1555 1.39
LINK NE2 HIS B 4 C8 AEVF B 303 1555 1555 1.59
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 2.02
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.04
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 2.01
LINK ZN ZN B 301 N AEVF B 302 1555 1555 1.95
LINK ZN ZN B 301 N BEVF B 302 1555 1555 1.88
LINK ZN ZN B 301 S AEVF B 302 1555 1555 3.00
CISPEP 1 SER B 29 PRO B 30 0 -0.96
CISPEP 2 PRO B 201 PRO B 202 0 11.07
SITE 1 AC1 4 HIS B 94 HIS B 96 HIS B 119 EVF B 302
SITE 1 AC2 11 HIS B 94 HIS B 96 HIS B 119 THR B 121
SITE 2 AC2 11 PHE B 131 LEU B 198 THR B 199 THR B 200
SITE 3 AC2 11 TRP B 209 ZN B 301 HOH B 565
SITE 1 AC3 13 HIS B 4 TRP B 5 HIS B 10 ASN B 11
SITE 2 AC3 13 HIS B 15 TRP B 16 ASP B 19 ASP B 180
SITE 3 AC3 13 ARG B 182 GLY B 183 HOH B 405 HOH B 459
SITE 4 AC3 13 HOH B 547
CRYST1 42.080 41.280 72.050 90.00 104.41 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 0.023764 0.000000 0.006106 0.00000
SCALE2 0.000000 0.024225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014330 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
