HEADER HYDROLASE 07-JAN-19 6QEB
TITLE ASSESSMENT OF A LARGE ENZYME-DRUG COMPLEX BY PROTON-DETECTED SOLID-
TITLE 2 STATE NMR WITHOUT DEUTERATION
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
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 K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS HCAII SOLID STATE NMR ACETAZOLAMIDE, HYDROLASE
EXPDTA SOLID-STATE NMR
NUMMDL 20
AUTHOR S.K.VASA
REVDAT 5 14-JUN-23 6QEB 1 REMARK
REVDAT 4 21-AUG-19 6QEB 1 REMARK
REVDAT 3 17-APR-19 6QEB 1 JRNL
REVDAT 2 13-MAR-19 6QEB 1 JRNL
REVDAT 1 06-FEB-19 6QEB 0
JRNL AUTH S.K.VASA,H.SINGH,K.GROHE,R.LINSER
JRNL TITL ASSESSMENT OF A LARGE ENZYME-DRUG COMPLEX BY PROTON-DETECTED
JRNL TITL 2 SOLID-STATE NMR SPECTROSCOPY WITHOUT DEUTERATION.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 58 5758 2019
JRNL REFN ESSN 1521-3773
JRNL PMID 30688395
JRNL DOI 10.1002/ANIE.201811714
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6QEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100036.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM [U-99% 13C; U-99% 15N]
REMARK 210 HCAII, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HCCH-TOCSY; 3D 1H-15N RFDR;
REMARK 210 3D 1H-13C RFDR
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE III
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA, CCPNMR ANALYSIS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 THESE RECORDS ARE MEANINGLESS.
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: 330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 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 1 PRO A 21 33.68 -76.40
REMARK 500 1 GLN A 28 94.29 -62.66
REMARK 500 1 PRO A 42 29.29 -78.48
REMARK 500 1 TYR A 51 37.46 -173.95
REMARK 500 1 HIS A 64 -49.03 -175.03
REMARK 500 1 LYS A 76 -82.71 -64.29
REMARK 500 1 ASP A 101 38.12 -87.21
REMARK 500 1 GLU A 106 -75.72 -72.74
REMARK 500 1 PRO A 154 36.31 -79.81
REMARK 500 1 ILE A 166 51.25 -103.88
REMARK 500 1 ASP A 179 78.38 -117.47
REMARK 500 1 SER A 187 101.06 59.09
REMARK 500 1 TYR A 193 75.80 -162.64
REMARK 500 1 PRO A 200 154.17 -40.63
REMARK 500 1 PRO A 201 101.47 -57.73
REMARK 500 1 LEU A 202 -56.03 -131.94
REMARK 500 1 CYS A 205 35.69 -87.91
REMARK 500 1 ASN A 231 72.63 177.54
REMARK 500 1 GLU A 237 99.80 -52.80
REMARK 500 1 ASP A 242 38.66 -174.78
REMARK 500 1 ALA A 247 48.07 -173.19
REMARK 500 1 LYS A 251 -52.58 -161.75
REMARK 500 1 ASN A 252 90.86 57.69
REMARK 500 2 SER A 2 -66.79 -126.18
REMARK 500 2 HIS A 3 86.77 57.85
REMARK 500 2 TYR A 7 -61.46 -105.37
REMARK 500 2 HIS A 15 39.12 -165.45
REMARK 500 2 ASP A 19 -64.51 -152.57
REMARK 500 2 PRO A 21 39.44 -80.88
REMARK 500 2 GLU A 26 91.40 57.41
REMARK 500 2 GLN A 28 71.14 61.85
REMARK 500 2 PRO A 42 90.69 -58.97
REMARK 500 2 LEU A 47 -58.29 -134.94
REMARK 500 2 VAL A 49 113.96 -161.88
REMARK 500 2 TYR A 51 22.49 -150.81
REMARK 500 2 HIS A 64 -52.17 -168.29
REMARK 500 2 GLN A 74 -68.82 -141.92
REMARK 500 2 LYS A 76 -70.67 -158.14
REMARK 500 2 GLU A 106 -76.28 -83.11
REMARK 500 2 LYS A 111 10.81 59.74
REMARK 500 2 ALA A 152 103.28 -57.65
REMARK 500 2 ILE A 166 51.14 -110.19
REMARK 500 2 ALA A 173 118.65 -167.52
REMARK 500 2 SER A 187 90.23 55.09
REMARK 500 2 LEU A 188 -79.99 -144.09
REMARK 500 2 TYR A 193 73.56 -159.40
REMARK 500 2 LEU A 197 176.57 -59.67
REMARK 500 2 PRO A 200 155.46 -39.23
REMARK 500 2 PRO A 201 104.59 -34.24
REMARK 500 2 LEU A 202 -41.94 -132.46
REMARK 500
REMARK 500 THIS ENTRY HAS 489 RAMACHANDRAN OUTLIERS.
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 109.1
REMARK 620 3 HIS A 119 ND1 108.6 109.0
REMARK 620 4 AZM A 302 N1 109.9 110.1 110.0
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 AZM A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 34347 RELATED DB: BMRB
REMARK 900 ASSESSMENT OF A LARGE ENZYME-DRUG COMPLEX BY PROTON-DETECTED SOLID-
REMARK 900 STATE NMR WITHOUT DEUTERATION
DBREF 6QEB A 1 260 UNP P00918 CAH2_HUMAN 1 260
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 LEU 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 AZM A 302 13
HETNAM ZN ZINC ION
HETNAM AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 AZM C4 H6 N4 O3 S2
HELIX 1 AA1 HIS A 15 PHE A 20 1 6
HELIX 2 AA2 LYS A 126 GLY A 128 5 3
HELIX 3 AA3 ASP A 129 VAL A 134 1 6
HELIX 4 AA4 LEU A 156 ASP A 164 1 9
HELIX 5 AA5 SER A 165 LYS A 167 5 3
HELIX 6 AA6 SER A 218 LYS A 224 1 7
HELIX 7 AA7 PHE A 225 LEU A 228 5 4
SHEET 1 AA1 2 LYS A 39 TYR A 40 0
SHEET 2 AA1 2 LYS A 256 ALA A 257 1 O ALA A 257 N LYS A 39
SHEET 1 AA2 5 VAL A 78 LEU A 79 0
SHEET 2 AA2 5 TYR A 88 PHE A 95 -1 O TYR A 88 N LEU A 79
SHEET 3 AA2 5 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 4 AA2 5 SER A 56 ASN A 61 -1 N ARG A 58 O GLU A 69
SHEET 5 AA2 5 SER A 172 ASP A 174 -1 O ALA A 173 N ILE A 59
SHEET 1 AA3 6 VAL A 78 LEU A 79 0
SHEET 2 AA3 6 TYR A 88 PHE A 95 -1 O TYR A 88 N LEU A 79
SHEET 3 AA3 6 LEU A 118 ASN A 124 -1 O HIS A 119 N HIS A 94
SHEET 4 AA3 6 VAL A 142 GLY A 144 -1 O LEU A 143 N LEU A 120
SHEET 5 AA3 6 VAL A 206 VAL A 210 1 O ILE A 209 N VAL A 142
SHEET 6 AA3 6 THR A 192 GLY A 195 -1 N TYR A 193 O TRP A 208
SHEET 1 AA4 2 LEU A 147 VAL A 149 0
SHEET 2 AA4 2 ILE A 215 VAL A 217 1 O VAL A 217 N LYS A 148
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.00
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.00
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.00
LINK ZN ZN A 301 N1 AZM A 302 1555 1555 2.00
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 AZM A 302
SITE 1 AC2 5 HIS A 94 HIS A 96 HIS A 119 ASN A 243
SITE 2 AC2 5 ZN A 301
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
