HEADER TRANSFERASE 17-MAY-16 5K01
TITLE CRYSTAL STRUCTURE OF COMT IN COMPLEX WITH 2,7-DIMETHYL-3-(1H-PYRAZOL-
TITLE 2 3-YL)IMIDAZO[1,2-A]PYRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.1.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: COMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, CATECHOL,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.EHLER,R.M.RODRIGUEZ-SARMIENTO,M.G.RUDOLPH
REVDAT 2 12-JUN-19 5K01 1 AUTHOR JRNL
REVDAT 1 07-SEP-16 5K01 0
JRNL AUTH A.EHLER,R.M.RODRIGUEZ-SARMIENTO,M.G.RUDOLPH
JRNL TITL CRYSTAL STRUCTURE OF COMT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 43626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2199
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.81
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 5K01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221524.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-10
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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44305
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380
REMARK 200 RESOLUTION RANGE LOW (A) : 40.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.990
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.73400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 7, 1.8 M AMMONIUM
REMARK 280 SULFATE, 0.2 M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 16.89450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.04650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.89400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.04650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.89450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.89400
REMARK 290 SMTRY3 4 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: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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: 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 HZ2 LYS A 144 O HOH A 402 1.41
REMARK 500 O HOH A 501 O HOH A 573 2.17
REMARK 500 NZ LYS A 144 O HOH A 402 2.19
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 407 O HOH A 566 3555 2.19
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 VAL A 42 -72.46 -119.96
REMARK 500 TYR A 68 -120.91 57.85
REMARK 500 ASP A 133 -74.50 -86.42
REMARK 500 ASP A 141 31.83 -148.26
REMARK 500 HIS A 142 -132.43 -105.75
REMARK 500 TYR A 200 -54.01 75.04
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 628 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 629 DISTANCE = 6.74 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 K A 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 183 O
REMARK 620 2 ARG A 184 O 78.5
REMARK 620 3 SER A 186 O 81.7 114.8
REMARK 620 4 PHE A 189 O 90.7 164.1 74.6
REMARK 620 5 HOH A 552 O 101.8 86.0 159.1 84.8
REMARK 620 6 HOH A 574 O 139.3 76.6 80.2 118.7 107.9
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 6OW A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 302
DBREF 5K01 A 3 216 UNP P22734 COMT_RAT 46 259
SEQADV 5K01 ARG A 11 UNP P22734 ARG 54 CONFLICT
SEQADV 5K01 TYR A 12 UNP P22734 TYR 55 CONFLICT
SEQADV 5K01 GLN A 14 UNP P22734 GLN 57 CONFLICT
SEQADV 5K01 ASN A 16 UNP P22734 ASN 59 CONFLICT
SEQADV 5K01 LYS A 18 UNP P22734 LYS 61 CONFLICT
SEQADV 5K01 ASP A 21 UNP P22734 ASP 64 CONFLICT
SEQADV 5K01 PRO A 22 UNP P22734 PRO 65 CONFLICT
SEQADV 5K01 THR A 34 UNP P22734 THR 77 CONFLICT
SEQADV 5K01 ALA A 45 UNP P22734 ALA 88 CONFLICT
SEQADV 5K01 GLN A 48 UNP P22734 GLN 91 CONFLICT
SEQADV 5K01 MET A 50 UNP P22734 MET 93 CONFLICT
SEQADV 5K01 ARG A 55 UNP P22734 ARG 98 CONFLICT
SEQADV 5K01 TYR A 57 UNP P22734 TYR 100 CONFLICT
SEQADV 5K01 SER A 58 UNP P22734 SER 101 CONFLICT
SEQADV 5K01 LEU A 61 UNP P22734 LEU 104 CONFLICT
SEQADV 5K01 VAL A 62 UNP P22734 VAL 105 CONFLICT
SEQADV 5K01 GLN A 81 UNP P22734 GLN 124 CONFLICT
SEQADV 5K01 LEU A 87 UNP P22734 LEU 130 CONFLICT
SEQADV 5K01 MET A 89 UNP P22734 MET 132 CONFLICT
SEQADV 5K01 GLN A 101 UNP P22734 GLN 144 CONFLICT
SEQADV 5K01 LEU A 103 UNP P22734 LEU 146 CONFLICT
SEQADV 5K01 ASN A 104 UNP P22734 ASN 147 CONFLICT
SEQADV 5K01 LEU A 108 UNP P22734 LEU 151 CONFLICT
SEQADV 5K01 GLN A 109 UNP P22734 GLN 152 CONFLICT
SEQADV 5K01 ILE A 114 UNP P22734 ILE 157 CONFLICT
SEQADV 5K01 LEU A 115 UNP P22734 LEU 158 CONFLICT
SEQADV 5K01 ASN A 116 UNP P22734 ASN 159 CONFLICT
SEQADV 5K01 LEU A 122 UNP P22734 LEU 165 CONFLICT
SEQADV 5K01 LYS A 156 UNP P22734 LYS 199 CONFLICT
SEQADV 5K01 VAL A 173 UNP P22734 VAL 216 CONFLICT
SEQADV 5K01 THR A 176 UNP P22734 THR 219 CONFLICT
SEQADV 5K01 TYR A 182 UNP P22734 TYR 225 CONFLICT
SEQADV 5K01 SER A 188 UNP P22734 SER 231 CONFLICT
SEQADV 5K01 SER A 195 UNP P22734 SER 238 CONFLICT
SEQADV 5K01 TYR A 197 UNP P22734 TYR 240 CONFLICT
SEQADV 5K01 MET A 201 UNP P22734 MET 244 CONFLICT
SEQADV 5K01 LYS A 202 UNP P22734 LYS 245 CONFLICT
SEQADV 5K01 GLN A 213 UNP P22734 GLN 256 CONFLICT
SEQADV 5K01 SER A 216 UNP P22734 SER 259 CONFLICT
SEQRES 1 A 214 ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL GLN GLN
SEQRES 2 A 214 ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU GLU ALA
SEQRES 3 A 214 ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA MET ASN
SEQRES 4 A 214 VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA VAL ILE
SEQRES 5 A 214 ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU GLY ALA
SEQRES 6 A 214 TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG LEU LEU
SEQRES 7 A 214 GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE ASN PRO
SEQRES 8 A 214 ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN PHE ALA
SEQRES 9 A 214 GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY ALA SER
SEQRES 10 A 214 GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR ASP VAL
SEQRES 11 A 214 ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP LYS ASP
SEQRES 12 A 214 ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS CYS GLY
SEQRES 13 A 214 LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP ASN VAL
SEQRES 14 A 214 ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR VAL ARG
SEQRES 15 A 214 GLY SER SER SER PHE GLU CYS THR HIS TYR SER SER TYR
SEQRES 16 A 214 LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU LYS ALA
SEQRES 17 A 214 ILE TYR GLN GLY PRO SER
HET 6OW A 301 27
HET K A 302 1
HETNAM 6OW 2,7-DIMETHYL-3-(1H-PYRAZOL-5-YL)IMIDAZO[1,2-A]PYRIDINE
HETNAM K POTASSIUM ION
FORMUL 2 6OW C12 H12 N4
FORMUL 3 K K 1+
FORMUL 4 HOH *229(H2 O)
HELIX 1 AA1 THR A 4 ALA A 17 1 14
HELIX 2 AA2 ASP A 21 GLU A 37 1 17
HELIX 3 AA3 GLY A 43 SER A 58 1 16
HELIX 4 AA4 GLY A 70 ARG A 78 1 9
HELIX 5 AA5 ASN A 92 GLY A 107 1 16
HELIX 6 AA6 LEU A 108 ASP A 110 5 3
HELIX 7 AA7 ALA A 118 ILE A 123 1 6
HELIX 8 AA8 GLN A 125 TYR A 130 1 6
HELIX 9 AA9 TRP A 143 ASP A 145 5 3
HELIX 10 AB1 ARG A 146 CYS A 157 1 12
HELIX 11 AB2 THR A 176 SER A 186 1 11
SHEET 1 AA1 7 VAL A 112 ASN A 116 0
SHEET 2 AA1 7 ARG A 85 GLU A 90 1 N THR A 88 O LEU A 115
SHEET 3 AA1 7 LEU A 61 LEU A 65 1 N VAL A 62 O LEU A 87
SHEET 4 AA1 7 MET A 137 LEU A 140 1 O PHE A 139 N LEU A 65
SHEET 5 AA1 7 VAL A 165 ALA A 168 1 O LEU A 167 N VAL A 138
SHEET 6 AA1 7 VAL A 203 TYR A 212 -1 O ALA A 210 N LEU A 166
SHEET 7 AA1 7 PHE A 189 LEU A 198 -1 N THR A 192 O LYS A 209
LINK O VAL A 183 K K A 302 1555 1555 2.85
LINK O ARG A 184 K K A 302 1555 1555 2.81
LINK O SER A 186 K K A 302 1555 1555 2.62
LINK O PHE A 189 K K A 302 1555 1555 2.62
LINK K K A 302 O HOH A 552 1555 1555 3.03
LINK K K A 302 O HOH A 574 1555 1555 2.84
CISPEP 1 VAL A 173 PRO A 174 0 0.71
SITE 1 AC1 12 ARG A 55 GLU A 56 GLY A 66 TYR A 68
SITE 2 AC1 12 MET A 89 GLU A 90 ILE A 91 ALA A 118
SITE 3 AC1 12 SER A 119 GLN A 120 HIS A 142 TRP A 143
SITE 1 AC2 6 VAL A 183 ARG A 184 SER A 186 PHE A 189
SITE 2 AC2 6 HOH A 552 HOH A 574
CRYST1 33.789 59.788 108.093 90.00 90.00 90.00 P 21 21 21 4
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 0.029595 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016726 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009251 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
