HEADER TRANSFERASE 16-NOV-09 3KPJ
TITLE CRYSTAL STRUCTURE OF HPNMT IN COMPLEX ADOHCY AND BOUND PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHENYLETHANOLAMINE N-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PNMTASE, NORADRENALINE N-METHYLTRANSFERASE;
COMPND 5 EC: 2.1.1.28;
COMPND 6 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: PENT, PNMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17 PNMT-HIS
KEYWDS METHYLTRANSFERASE, FRAGMENT SCREENING, CATECHOLAMINE BIOSYNTHESIS, S-
KEYWDS 2 ADENOSYL-L-METHIONINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.DRINKWATER,J.L.MARTIN
REVDAT 3 06-SEP-23 3KPJ 1 REMARK SEQADV
REVDAT 2 04-APR-18 3KPJ 1 REMARK
REVDAT 1 29-SEP-10 3KPJ 0
JRNL AUTH N.DRINKWATER,H.VU,K.M.LOVELL,K.R.CRISCIONE,B.M.COLLINS,
JRNL AUTH 2 T.E.PRISINZANO,S.A.POULSEN,M.J.MCLEISH,G.L.GRUNEWALD,
JRNL AUTH 3 J.L.MARTIN
JRNL TITL FRAGMENT-BASED SCREENING BY X-RAY CRYSTALLOGRAPHY, MS AND
JRNL TITL 2 ISOTHERMAL TITRATION CALORIMETRY TO IDENTIFY PNMT
JRNL TITL 3 (PHENYLETHANOLAMINE N-METHYLTRANSFERASE) INHIBITORS.
JRNL REF BIOCHEM.J. V. 431 51 2010
JRNL REFN ISSN 0264-6021
JRNL PMID 20642456
JRNL DOI 10.1042/BJ20100651
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 28975
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1435
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 33.3860 - 5.3790 0.96 2952 147 0.1890 0.2410
REMARK 3 2 5.3790 - 4.2730 0.98 2833 146 0.1560 0.2250
REMARK 3 3 4.2730 - 3.7330 0.97 2772 166 0.1780 0.2190
REMARK 3 4 3.7330 - 3.3920 0.98 2805 125 0.2120 0.2770
REMARK 3 5 3.3920 - 3.1490 0.97 2737 154 0.2500 0.3270
REMARK 3 6 3.1490 - 2.9640 0.96 2712 135 0.2560 0.3140
REMARK 3 7 2.9640 - 2.8160 0.96 2687 145 0.2540 0.3330
REMARK 3 8 2.8160 - 2.6930 0.96 2715 126 0.2830 0.3280
REMARK 3 9 2.6930 - 2.5890 0.96 2677 147 0.3160 0.3440
REMARK 3 10 2.5890 - 2.5000 0.95 2650 144 0.3580 0.4060
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 : 0.31
REMARK 3 B_SOL : 52.75
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.24800
REMARK 3 B22 (A**2) : 7.24800
REMARK 3 B33 (A**2) : -14.49600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 4270
REMARK 3 ANGLE : 1.121 5815
REMARK 3 CHIRALITY : 0.067 630
REMARK 3 PLANARITY : 0.005 759
REMARK 3 DIHEDRAL : 16.264 1557
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2957 51.7534 -5.0480
REMARK 3 T TENSOR
REMARK 3 T11: 0.4764 T22: 0.4264
REMARK 3 T33: 0.5200 T12: -0.1190
REMARK 3 T13: -0.0834 T23: 0.1536
REMARK 3 L TENSOR
REMARK 3 L11: 0.3983 L22: 0.6778
REMARK 3 L33: 2.1949 L12: -0.1155
REMARK 3 L13: -0.0215 L23: -0.1815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0687 S12: 0.0038 S13: 0.0516
REMARK 3 S21: 0.1560 S22: -0.2014 S23: -0.1463
REMARK 3 S31: -0.2722 S32: 0.1148 S33: 0.1852
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 3KPJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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 : RIGAKU FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : HIRES2
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29790
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 33.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.770
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.76
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1HNN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6K, LICL, CACODYLATE, PH 5.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.45500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.21000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 140.18250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.21000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.21000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.72750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.21000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.21000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 140.18250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.21000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.21000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.72750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.45500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 PRO A 8
REMARK 465 ASN A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 PRO A 14
REMARK 465 ASP A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 PRO A 18
REMARK 465 GLY A 19
REMARK 465 GLN A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 VAL A 23
REMARK 465 GLY A 281
REMARK 465 LEU A 282
REMARK 465 GLU A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 ALA B 4
REMARK 465 ASP B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 PRO B 8
REMARK 465 ASN B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 282
REMARK 465 GLU B 283
REMARK 465 HIS B 284
REMARK 465 HIS B 285
REMARK 465 HIS B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
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 GLN A 163 CD
REMARK 480 HIS A 261 CE1
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 PRO A 170 2.60 -65.01
REMARK 500 CYS A 183 -71.67 -105.50
REMARK 500 ASP A 267 -167.07 -164.79
REMARK 500 PRO B 42 153.17 -49.40
REMARK 500 PRO B 82 37.24 -97.02
REMARK 500 VAL B 151 99.25 -69.63
REMARK 500 ARG B 153 155.39 177.25
REMARK 500 ALA B 171 134.42 -39.97
REMARK 500 CYS B 183 -65.11 -107.10
REMARK 500 LEU B 262 -26.75 87.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 290
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KPU RELATED DB: PDB
REMARK 900 RELATED ID: 3KPV RELATED DB: PDB
REMARK 900 RELATED ID: 3KPW RELATED DB: PDB
REMARK 900 RELATED ID: 3KPY RELATED DB: PDB
REMARK 900 RELATED ID: 3KQM RELATED DB: PDB
REMARK 900 RELATED ID: 3KQO RELATED DB: PDB
REMARK 900 RELATED ID: 3KQP RELATED DB: PDB
REMARK 900 RELATED ID: 3KQQ RELATED DB: PDB
REMARK 900 RELATED ID: 3KQS RELATED DB: PDB
REMARK 900 RELATED ID: 3KQT RELATED DB: PDB
REMARK 900 RELATED ID: 3KQV RELATED DB: PDB
REMARK 900 RELATED ID: 3KQW RELATED DB: PDB
REMARK 900 RELATED ID: 3KQY RELATED DB: PDB
REMARK 900 RELATED ID: 3KR0 RELATED DB: PDB
REMARK 900 RELATED ID: 3KR1 RELATED DB: PDB
REMARK 900 RELATED ID: 3KR2 RELATED DB: PDB
DBREF 3KPJ A 1 282 UNP P11086 PNMT_HUMAN 1 282
DBREF 3KPJ B 1 282 UNP P11086 PNMT_HUMAN 1 282
SEQADV 3KPJ GLU A 283 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 284 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 285 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 286 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 287 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 288 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS A 289 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ GLU B 283 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 284 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 285 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 286 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 287 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 288 UNP P11086 EXPRESSION TAG
SEQADV 3KPJ HIS B 289 UNP P11086 EXPRESSION TAG
SEQRES 1 A 289 MET SER GLY ALA ASP ARG SER PRO ASN ALA GLY ALA ALA
SEQRES 2 A 289 PRO ASP SER ALA PRO GLY GLN ALA ALA VAL ALA SER ALA
SEQRES 3 A 289 TYR GLN ARG PHE GLU PRO ARG ALA TYR LEU ARG ASN ASN
SEQRES 4 A 289 TYR ALA PRO PRO ARG GLY ASP LEU CYS ASN PRO ASN GLY
SEQRES 5 A 289 VAL GLY PRO TRP LYS LEU ARG CYS LEU ALA GLN THR PHE
SEQRES 6 A 289 ALA THR GLY GLU VAL SER GLY ARG THR LEU ILE ASP ILE
SEQRES 7 A 289 GLY SER GLY PRO THR VAL TYR GLN LEU LEU SER ALA CYS
SEQRES 8 A 289 SER HIS PHE GLU ASP ILE THR MET THR ASP PHE LEU GLU
SEQRES 9 A 289 VAL ASN ARG GLN GLU LEU GLY ARG TRP LEU GLN GLU GLU
SEQRES 10 A 289 PRO GLY ALA PHE ASN TRP SER MET TYR SER GLN HIS ALA
SEQRES 11 A 289 CYS LEU ILE GLU GLY LYS GLY GLU CYS TRP GLN ASP LYS
SEQRES 12 A 289 GLU ARG GLN LEU ARG ALA ARG VAL LYS ARG VAL LEU PRO
SEQRES 13 A 289 ILE ASP VAL HIS GLN PRO GLN PRO LEU GLY ALA GLY SER
SEQRES 14 A 289 PRO ALA PRO LEU PRO ALA ASP ALA LEU VAL SER ALA PHE
SEQRES 15 A 289 CYS LEU GLU ALA VAL SER PRO ASP LEU ALA SER PHE GLN
SEQRES 16 A 289 ARG ALA LEU ASP HIS ILE THR THR LEU LEU ARG PRO GLY
SEQRES 17 A 289 GLY HIS LEU LEU LEU ILE GLY ALA LEU GLU GLU SER TRP
SEQRES 18 A 289 TYR LEU ALA GLY GLU ALA ARG LEU THR VAL VAL PRO VAL
SEQRES 19 A 289 SER GLU GLU GLU VAL ARG GLU ALA LEU VAL ARG SER GLY
SEQRES 20 A 289 TYR LYS VAL ARG ASP LEU ARG THR TYR ILE MET PRO ALA
SEQRES 21 A 289 HIS LEU GLN THR GLY VAL ASP ASP VAL LYS GLY VAL PHE
SEQRES 22 A 289 PHE ALA TRP ALA GLN LYS VAL GLY LEU GLU HIS HIS HIS
SEQRES 23 A 289 HIS HIS HIS
SEQRES 1 B 289 MET SER GLY ALA ASP ARG SER PRO ASN ALA GLY ALA ALA
SEQRES 2 B 289 PRO ASP SER ALA PRO GLY GLN ALA ALA VAL ALA SER ALA
SEQRES 3 B 289 TYR GLN ARG PHE GLU PRO ARG ALA TYR LEU ARG ASN ASN
SEQRES 4 B 289 TYR ALA PRO PRO ARG GLY ASP LEU CYS ASN PRO ASN GLY
SEQRES 5 B 289 VAL GLY PRO TRP LYS LEU ARG CYS LEU ALA GLN THR PHE
SEQRES 6 B 289 ALA THR GLY GLU VAL SER GLY ARG THR LEU ILE ASP ILE
SEQRES 7 B 289 GLY SER GLY PRO THR VAL TYR GLN LEU LEU SER ALA CYS
SEQRES 8 B 289 SER HIS PHE GLU ASP ILE THR MET THR ASP PHE LEU GLU
SEQRES 9 B 289 VAL ASN ARG GLN GLU LEU GLY ARG TRP LEU GLN GLU GLU
SEQRES 10 B 289 PRO GLY ALA PHE ASN TRP SER MET TYR SER GLN HIS ALA
SEQRES 11 B 289 CYS LEU ILE GLU GLY LYS GLY GLU CYS TRP GLN ASP LYS
SEQRES 12 B 289 GLU ARG GLN LEU ARG ALA ARG VAL LYS ARG VAL LEU PRO
SEQRES 13 B 289 ILE ASP VAL HIS GLN PRO GLN PRO LEU GLY ALA GLY SER
SEQRES 14 B 289 PRO ALA PRO LEU PRO ALA ASP ALA LEU VAL SER ALA PHE
SEQRES 15 B 289 CYS LEU GLU ALA VAL SER PRO ASP LEU ALA SER PHE GLN
SEQRES 16 B 289 ARG ALA LEU ASP HIS ILE THR THR LEU LEU ARG PRO GLY
SEQRES 17 B 289 GLY HIS LEU LEU LEU ILE GLY ALA LEU GLU GLU SER TRP
SEQRES 18 B 289 TYR LEU ALA GLY GLU ALA ARG LEU THR VAL VAL PRO VAL
SEQRES 19 B 289 SER GLU GLU GLU VAL ARG GLU ALA LEU VAL ARG SER GLY
SEQRES 20 B 289 TYR LYS VAL ARG ASP LEU ARG THR TYR ILE MET PRO ALA
SEQRES 21 B 289 HIS LEU GLN THR GLY VAL ASP ASP VAL LYS GLY VAL PHE
SEQRES 22 B 289 PHE ALA TRP ALA GLN LYS VAL GLY LEU GLU HIS HIS HIS
SEQRES 23 B 289 HIS HIS HIS
HET SAH A3001 26
HET PO4 A 290 5
HET SAH B3002 26
HET PO4 B 290 5
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM PO4 PHOSPHATE ION
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 7 HOH *94(H2 O)
HELIX 1 1 ALA A 24 ARG A 29 5 6
HELIX 2 2 GLU A 31 ALA A 41 1 11
HELIX 3 3 GLY A 52 THR A 67 1 16
HELIX 4 4 VAL A 84 LEU A 88 5 5
HELIX 5 5 SER A 89 HIS A 93 5 5
HELIX 6 6 LEU A 103 GLN A 115 1 13
HELIX 7 7 TRP A 123 GLY A 135 1 13
HELIX 8 8 CYS A 139 ARG A 150 1 12
HELIX 9 9 CYS A 183 SER A 188 1 6
HELIX 10 10 ASP A 190 THR A 203 1 14
HELIX 11 11 SER A 235 SER A 246 1 12
HELIX 12 12 PRO A 259 GLN A 263 5 5
HELIX 13 13 SER B 16 GLN B 28 1 13
HELIX 14 14 GLU B 31 ALA B 41 1 11
HELIX 15 15 GLY B 52 THR B 67 1 16
HELIX 16 16 VAL B 84 LEU B 88 5 5
HELIX 17 17 ALA B 90 SER B 92 5 3
HELIX 18 18 LEU B 103 GLN B 115 1 13
HELIX 19 19 TRP B 123 GLY B 135 1 13
HELIX 20 20 CYS B 139 ARG B 150 1 12
HELIX 21 21 CYS B 183 SER B 188 1 6
HELIX 22 22 ASP B 190 THR B 203 1 14
HELIX 23 23 SER B 235 SER B 246 1 12
SHEET 1 A 7 VAL A 151 PRO A 156 0
SHEET 2 A 7 ASP A 96 ASP A 101 1 N MET A 99 O LEU A 155
SHEET 3 A 7 THR A 74 ILE A 78 1 N ASP A 77 O THR A 98
SHEET 4 A 7 ALA A 175 ALA A 181 1 O VAL A 179 N ILE A 78
SHEET 5 A 7 LEU A 205 LEU A 217 1 O ILE A 214 N SER A 180
SHEET 6 A 7 GLY A 271 LYS A 279 -1 O ALA A 275 N LEU A 213
SHEET 7 A 7 TYR A 248 ILE A 257 -1 N LYS A 249 O GLN A 278
SHEET 1 B 2 TRP A 221 ALA A 224 0
SHEET 2 B 2 ALA A 227 THR A 230 -1 O LEU A 229 N TYR A 222
SHEET 1 C 7 VAL B 151 PRO B 156 0
SHEET 2 C 7 PHE B 94 ASP B 101 1 N MET B 99 O ARG B 153
SHEET 3 C 7 GLY B 72 ILE B 78 1 N ASP B 77 O THR B 98
SHEET 4 C 7 ALA B 175 ALA B 181 1 O VAL B 179 N ILE B 78
SHEET 5 C 7 LEU B 205 LEU B 217 1 O LEU B 212 N LEU B 178
SHEET 6 C 7 GLY B 271 LYS B 279 -1 O LYS B 279 N GLY B 208
SHEET 7 C 7 TYR B 248 ILE B 257 -1 N TYR B 256 O VAL B 272
SHEET 1 D 2 TRP B 221 ALA B 224 0
SHEET 2 D 2 ALA B 227 THR B 230 -1 O LEU B 229 N TYR B 222
SSBOND 1 CYS A 48 CYS B 139 1555 1555 2.03
SSBOND 2 CYS A 139 CYS B 48 1555 1555 2.03
CISPEP 1 PRO A 42 PRO A 43 0 2.64
CISPEP 2 LEU A 173 PRO A 174 0 -5.69
CISPEP 3 PRO B 42 PRO B 43 0 5.55
CISPEP 4 LEU B 173 PRO B 174 0 -1.77
SITE 1 AC1 19 TYR A 27 TYR A 35 TYR A 40 GLY A 79
SITE 2 AC1 19 SER A 80 GLY A 81 THR A 83 TYR A 85
SITE 3 AC1 19 ASP A 101 PHE A 102 ASN A 106 ILE A 157
SITE 4 AC1 19 ASP A 158 VAL A 159 HIS A 160 ALA A 181
SITE 5 AC1 19 PHE A 182 CYS A 183 VAL A 187
SITE 1 AC2 19 TYR B 35 TYR B 40 GLY B 79 SER B 80
SITE 2 AC2 19 GLY B 81 THR B 83 TYR B 85 ASP B 101
SITE 3 AC2 19 PHE B 102 LEU B 103 ASN B 106 ILE B 157
SITE 4 AC2 19 ASP B 158 VAL B 159 HIS B 160 ALA B 181
SITE 5 AC2 19 PHE B 182 CYS B 183 VAL B 187
SITE 1 AC3 4 ASN A 39 LYS A 57 PHE A 182 HOH A 291
SITE 1 AC4 4 ASN B 39 ARG B 44 LYS B 57 PHE B 182
CRYST1 94.420 94.420 186.910 90.00 90.00 90.00 P 43 21 2 16
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 0.010591 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010591 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005350 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
