HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-MAR-14 4PYQ
TITLE HUMANIZED RAT APO-COMT IN COMPLEX WITH A UREIDO-BENZAMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 44-264;
COMPND 5 EC: 2.1.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: COMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, ALTERNATIVE
KEYWDS 2 INITIATION, CATECHOLAMINE METABOLISM, CELL MEMBRANE, MAGNESIUM,
KEYWDS 3 MEMBRANE, METAL-BINDING, PHOSPHOPROTEIN, SIGNAL-ANCHOR,
KEYWDS 4 TRANSMEMBRANE ANCHOR, ENZYME MECHANISM, CONFORMATIONAL CHANGE,
KEYWDS 5 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.EHLER,J.BENZ,D.SCHLATTER,M.G.RUDOLPH
REVDAT 3 28-FEB-24 4PYQ 1 REMARK SEQADV LINK
REVDAT 2 27-AUG-14 4PYQ 1 JRNL
REVDAT 1 11-JUN-14 4PYQ 0
JRNL AUTH A.EHLER,J.BENZ,D.SCHLATTER,M.G.RUDOLPH
JRNL TITL MAPPING THE CONFORMATIONAL SPACE ACCESSIBLE TO
JRNL TITL 2 CATECHOL-O-METHYLTRANSFERASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2163 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25084335
JRNL DOI 10.1107/S1399004714012917
REMARK 2
REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1589)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 91056
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4574
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 36.4186 - 3.7695 0.95 4338 240 0.0927 0.1297
REMARK 3 2 3.7695 - 2.9924 0.94 4285 230 0.1001 0.1360
REMARK 3 3 2.9924 - 2.6143 0.95 4349 202 0.1224 0.1600
REMARK 3 4 2.6143 - 2.3753 0.94 4306 218 0.1336 0.1603
REMARK 3 5 2.3753 - 2.2051 0.95 4322 214 0.1405 0.1739
REMARK 3 6 2.2051 - 2.0751 0.94 4277 231 0.1536 0.1841
REMARK 3 7 2.0751 - 1.9712 0.95 4327 233 0.1602 0.2006
REMARK 3 8 1.9712 - 1.8854 0.95 4350 218 0.1676 0.1807
REMARK 3 9 1.8854 - 1.8128 0.95 4330 224 0.1675 0.1807
REMARK 3 10 1.8128 - 1.7502 0.94 4287 261 0.1720 0.1824
REMARK 3 11 1.7502 - 1.6955 0.95 4326 238 0.1768 0.1964
REMARK 3 12 1.6955 - 1.6470 0.95 4334 230 0.1848 0.2061
REMARK 3 13 1.6470 - 1.6037 0.95 4339 249 0.1908 0.2127
REMARK 3 14 1.6037 - 1.5646 0.95 4304 243 0.2012 0.2357
REMARK 3 15 1.5646 - 1.5290 0.95 4333 222 0.2109 0.2053
REMARK 3 16 1.5290 - 1.4964 0.95 4364 246 0.2181 0.2530
REMARK 3 17 1.4964 - 1.4665 0.96 4386 198 0.2507 0.2928
REMARK 3 18 1.4665 - 1.4388 0.95 4320 231 0.2655 0.2863
REMARK 3 19 1.4388 - 1.4131 0.95 4324 212 0.3118 0.3301
REMARK 3 20 1.4131 - 1.3892 0.94 4288 220 0.3436 0.3592
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.870
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: 0.5000
REMARK 3 OPERATOR: K,H,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 3521
REMARK 3 ANGLE : 1.333 4782
REMARK 3 CHIRALITY : 0.068 533
REMARK 3 PLANARITY : 0.006 613
REMARK 3 DIHEDRAL : 15.345 1335
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 4PYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-11
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) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91065
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 36.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.01000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.491
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.68300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.19005
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.76233
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 62.68300
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 36.19005
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.76233
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 62.68300
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 36.19005
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.76233
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.38009
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 51.52467
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 72.38009
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 51.52467
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 72.38009
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 51.52467
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 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 44
REMARK 465 GLY A 45
REMARK 465 SER A 259
REMARK 465 SER A 260
REMARK 465 PRO A 261
REMARK 465 ASP A 262
REMARK 465 LYS A 263
REMARK 465 SER A 264
REMARK 465 MET B 44
REMARK 465 GLY B 45
REMARK 465 SER B 259
REMARK 465 SER B 260
REMARK 465 PRO B 261
REMARK 465 ASP B 262
REMARK 465 LYS B 263
REMARK 465 SER B 264
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 O HOH B 448 O HOH B 487 1.89
REMARK 500 O HOH A 460 O HOH A 463 1.93
REMARK 500 O HOH A 460 O HOH A 464 1.95
REMARK 500 O HOH B 486 O HOH B 489 1.97
REMARK 500 O HOH B 422 O HOH B 423 2.02
REMARK 500 O HOH B 453 O HOH B 455 2.04
REMARK 500 O HOH A 405 O HOH A 437 2.06
REMARK 500 O HOH B 419 O HOH B 420 2.07
REMARK 500 O HOH A 440 O HOH A 456 2.09
REMARK 500 O HOH B 477 O HOH B 485 2.11
REMARK 500 O HOH A 450 O HOH A 458 2.12
REMARK 500 O HOH B 431 O HOH B 465 2.13
REMARK 500 O HOH A 468 O HOH B 407 2.14
REMARK 500 OD1 ASP B 188 O HOH B 485 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 CD GLU A 70 OE2 GLU B 70 3555 1.91
REMARK 500 OE2 GLU A 70 OE2 GLU B 70 3555 1.96
REMARK 500 OE1 GLU A 70 OE2 GLU B 70 3555 2.13
REMARK 500 OD2 ASP B 153 OG1 THR B 177 2555 2.14
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 ASN A 84 53.13 39.39
REMARK 500 LYS A 89 -45.10 -138.86
REMARK 500 SER A 101 67.22 39.24
REMARK 500 TYR A 111 -76.73 -98.40
REMARK 500 LYS A 171 -72.77 -59.84
REMARK 500 ASP A 176 -63.44 -97.70
REMARK 500 HIS A 185 -60.78 82.77
REMARK 500 THR A 219 46.64 36.90
REMARK 500 LEU A 241 -137.09 47.81
REMARK 500 ALA B 82 129.27 -175.22
REMARK 500 LYS B 89 -48.80 -131.56
REMARK 500 TYR B 111 -67.79 -101.85
REMARK 500 LYS B 171 -76.13 -54.97
REMARK 500 ASP B 176 -61.63 -95.85
REMARK 500 HIS B 185 -78.85 76.76
REMARK 500 THR B 219 42.52 35.59
REMARK 500 LEU B 241 -127.02 46.66
REMARK 500 TYR B 243 -152.28 -116.27
REMARK 500 TYR B 243 -153.39 -115.17
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 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 226 O
REMARK 620 2 ARG A 227 O 92.4
REMARK 620 3 SER A 229 O 86.9 105.4
REMARK 620 4 PHE A 232 O 95.6 163.3 89.6
REMARK 620 5 GLU B 242 O 165.1 76.1 87.0 97.9
REMARK 620 6 HOH B 401 O 100.9 83.2 168.3 81.0 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 242 O
REMARK 620 2 HOH A 489 O 87.6
REMARK 620 3 VAL B 226 O 165.7 100.9
REMARK 620 4 ARG B 227 O 82.6 82.3 87.1
REMARK 620 5 SER B 229 O 78.0 165.1 94.0 99.2
REMARK 620 6 PHE B 232 O 97.6 83.5 94.9 165.7 94.7
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 2X1 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2X1 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P7K RELATED DB: PDB
REMARK 900 RELATED ID: 4P7F RELATED DB: PDB
REMARK 900 RELATED ID: 4P7G RELATED DB: PDB
REMARK 900 RELATED ID: 4P7J RELATED DB: PDB
REMARK 900 RELATED ID: 4PYJ RELATED DB: PDB
REMARK 900 RELATED ID: 4PYI RELATED DB: PDB
REMARK 900 RELATED ID: 4PYK RELATED DB: PDB
REMARK 900 RELATED ID: 4PYL RELATED DB: PDB
REMARK 900 RELATED ID: 4PYM RELATED DB: PDB
REMARK 900 RELATED ID: 4PYN RELATED DB: PDB
REMARK 900 RELATED ID: 4PYO RELATED DB: PDB
DBREF 4PYQ A 44 264 UNP P22734 COMT_RAT 44 264
DBREF 4PYQ B 44 264 UNP P22734 COMT_RAT 44 264
SEQADV 4PYQ ILE A 134 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 4PYQ CYS A 138 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQADV 4PYQ ILE B 134 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 4PYQ CYS B 138 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQRES 1 A 221 MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES 2 A 221 GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES 3 A 221 GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES 4 A 221 MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES 5 A 221 VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES 6 A 221 GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES 7 A 221 LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES 8 A 221 ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES 9 A 221 PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES 10 A 221 ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES 11 A 221 ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES 12 A 221 LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES 13 A 221 CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES 14 A 221 ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES 15 A 221 VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES 16 A 221 SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES 17 A 221 LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
SEQRES 1 B 221 MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES 2 B 221 GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES 3 B 221 GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES 4 B 221 MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES 5 B 221 VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES 6 B 221 GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES 7 B 221 LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES 8 B 221 ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES 9 B 221 PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES 10 B 221 ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES 11 B 221 ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES 12 B 221 LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES 13 B 221 CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES 14 B 221 ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES 15 B 221 VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES 16 B 221 SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES 17 B 221 LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
HET 2X1 A 301 21
HET ACT A 302 4
HET NA A 303 1
HET SO4 A 304 5
HET SO4 A 305 5
HET NA B 301 1
HET 2X1 B 302 21
HET ACT B 303 4
HET CL B 304 1
HET SO4 B 305 5
HET SO4 B 306 5
HETNAM 2X1 4-({[3-(AMINOMETHYL)PHENYL]CARBAMOYL}AMINO)
HETNAM 2 2X1 BENZENECARBOXIMIDAMIDE
HETNAM ACT ACETATE ION
HETNAM NA SODIUM ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 3 2X1 2(C15 H17 N5 O)
FORMUL 4 ACT 2(C2 H3 O2 1-)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 11 CL CL 1-
FORMUL 14 HOH *207(H2 O)
HELIX 1 1 THR A 47 ALA A 60 1 14
HELIX 2 2 ASP A 64 LYS A 79 1 16
HELIX 3 3 ASN A 84 LYS A 89 1 6
HELIX 4 4 LYS A 89 SER A 101 1 13
HELIX 5 5 GLY A 113 ARG A 121 1 9
HELIX 6 6 ASN A 135 GLY A 150 1 16
HELIX 7 7 LEU A 151 ASP A 153 5 3
HELIX 8 8 ALA A 161 ILE A 166 1 6
HELIX 9 9 GLN A 168 ASP A 174 1 7
HELIX 10 10 TRP A 186 ASP A 188 5 3
HELIX 11 11 ARG A 189 CYS A 200 1 12
HELIX 12 12 THR A 219 SER A 229 1 11
HELIX 13 13 THR B 47 ALA B 60 1 14
HELIX 14 14 ASP B 64 GLU B 80 1 17
HELIX 15 15 ASN B 84 LYS B 89 1 6
HELIX 16 16 LYS B 89 SER B 101 1 13
HELIX 17 17 GLY B 113 ARG B 121 1 9
HELIX 18 18 ASN B 135 GLY B 150 1 16
HELIX 19 19 LEU B 151 ASP B 153 5 3
HELIX 20 20 ALA B 161 ILE B 166 1 6
HELIX 21 21 GLN B 168 ASP B 174 1 7
HELIX 22 22 TRP B 186 ASP B 188 5 3
HELIX 23 23 ARG B 189 CYS B 200 1 12
HELIX 24 24 THR B 219 SER B 229 1 11
SHEET 1 A14 VAL A 155 ASN A 159 0
SHEET 2 A14 ARG A 128 GLU A 133 1 N THR A 131 O LEU A 158
SHEET 3 A14 LEU A 104 LEU A 108 1 N GLU A 107 O LEU A 130
SHEET 4 A14 LEU A 178 LEU A 183 1 O PHE A 182 N LEU A 106
SHEET 5 A14 LEU A 203 ASP A 212 1 O LEU A 210 N LEU A 183
SHEET 6 A14 ASP A 248 TYR A 255 -1 O TYR A 255 N GLY A 206
SHEET 7 A14 PHE A 232 LEU A 241 -1 N GLU A 233 O ILE A 254
SHEET 8 A14 PHE B 232 LEU B 241 -1 O HIS B 236 N SER A 238
SHEET 9 A14 ASP B 248 TYR B 255 -1 O LEU B 250 N TYR B 237
SHEET 10 A14 LEU B 203 ASP B 212 -1 N GLY B 206 O TYR B 255
SHEET 11 A14 LEU B 178 LEU B 183 1 N VAL B 181 O VAL B 208
SHEET 12 A14 LEU B 104 LEU B 108 1 N LEU B 106 O PHE B 182
SHEET 13 A14 ARG B 128 GLU B 133 1 O LEU B 130 N GLU B 107
SHEET 14 A14 VAL B 155 ASN B 159 1 O THR B 156 N THR B 131
LINK O VAL A 226 NA NA A 303 1555 1555 2.46
LINK O ARG A 227 NA NA A 303 1555 1555 2.51
LINK O SER A 229 NA NA A 303 1555 1555 2.28
LINK O PHE A 232 NA NA A 303 1555 1555 2.46
LINK O GLU A 242 NA NA B 301 1555 1555 2.60
LINK NA NA A 303 O GLU B 242 1555 1555 2.49
LINK NA NA A 303 O HOH B 401 1555 1555 2.45
LINK O HOH A 489 NA NA B 301 1555 1555 2.40
LINK O VAL B 226 NA NA B 301 1555 1555 2.43
LINK O ARG B 227 NA NA B 301 1555 1555 2.44
LINK O SER B 229 NA NA B 301 1555 1555 2.32
LINK O PHE B 232 NA NA B 301 1555 1555 2.42
CISPEP 1 VAL A 216 PRO A 217 0 8.56
CISPEP 2 VAL B 216 PRO B 217 0 2.01
SITE 1 AC1 5 ILE A 134 ASN A 135 PRO A 136 TRP A 186
SITE 2 AC1 5 ASP A 188
SITE 1 AC2 8 LEU A 108 GLY A 109 SER A 162 ASP A 184
SITE 2 AC2 8 TRP A 186 ARG A 189 ASP A 193 HOH A 440
SITE 1 AC3 6 VAL A 226 ARG A 227 SER A 229 PHE A 232
SITE 2 AC3 6 GLU B 242 HOH B 401
SITE 1 AC4 8 ALA A 110 TYR A 111 CYS A 112 GLY A 113
SITE 2 AC4 8 TYR A 114 SER A 115 ASP A 184 HOH A 402
SITE 1 AC5 3 ARG A 51 TYR A 75 LYS A 79
SITE 1 AC6 6 GLU A 242 HOH A 489 VAL B 226 ARG B 227
SITE 2 AC6 6 SER B 229 PHE B 232
SITE 1 AC7 6 ILE B 134 ASN B 135 PRO B 136 TRP B 186
SITE 2 AC7 6 ASP B 188 ARG B 189
SITE 1 AC8 8 LEU B 108 GLY B 109 SER B 162 ASP B 184
SITE 2 AC8 8 TRP B 186 ARG B 189 ASP B 193 HOH B 468
SITE 1 AC9 2 GLY B 86 ARG B 118
SITE 1 BC1 7 TYR B 111 CYS B 112 GLY B 113 TYR B 114
SITE 2 BC1 7 SER B 115 ASP B 184 HOH B 427
SITE 1 BC2 4 ARG B 51 TYR B 75 LYS B 79 HOH B 466
CRYST1 125.366 125.366 77.287 90.00 90.00 120.00 H 3 18
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 0.007977 0.004605 0.000000 0.00000
SCALE2 0.000000 0.009211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012939 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
