HEADER TRANSFERASE 20-JUN-17 5O9T
TITLE HSNMT1 IN COMPLEX WITH COA AND ACETYLATED-NCFSKPK PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE 1,TYPE I N-
COMPND 5 MYRISTOYLTRANSFERASE,PEPTIDE N-MYRISTOYLTRANSFERASE 1;
COMPND 6 EC: 2.3.1.97;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 1IP-CYS-PHE-SER-LYS-PRO-ARG;
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: N-ACETYLATED PEPTIDE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NMT1, NMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2(DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28 DERIVATIVE;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS TRANSFERASE, GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 1 N-
KEYWDS 2 MYRISTOYLTRANSFERASE 1, N-MYRISTOYLTRANSFERASE TYPE1, NMT1, NMT,
KEYWDS 3 ACYLTRANSFERASE, MYR-PEPTIDE, COA, MYR-COA, MYRISTOYL, GNAT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DIAN,T.MEINNEL,C.GIGLIONE
REVDAT 3 31-JAN-24 5O9T 1 REMARK
REVDAT 2 07-NOV-18 5O9T 1 JRNL
REVDAT 1 27-JUN-18 5O9T 0
JRNL AUTH B.CASTREC,C.DIAN,S.CICCONE,C.L.EBERT,W.V.BIENVENUT,
JRNL AUTH 2 J.P.LE CAER,J.M.STEYAERT,C.GIGLIONE,T.MEINNEL
JRNL TITL STRUCTURAL AND GENOMIC DECODING OF HUMAN AND PLANT
JRNL TITL 2 MYRISTOYLOMES REVEALS A DEFINITIVE RECOGNITION PATTERN.
JRNL REF NAT. CHEM. BIOL. V. 14 671 2018
JRNL REFN ESSN 1552-4469
JRNL PMID 29892081
JRNL DOI 10.1038/S41589-018-0077-5
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 46115
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2288
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 47.7620 - 5.4154 0.99 2938 164 0.1711 0.2151
REMARK 3 2 5.4154 - 4.2992 1.00 2808 153 0.1341 0.1710
REMARK 3 3 4.2992 - 3.7560 1.00 2782 142 0.1376 0.1858
REMARK 3 4 3.7560 - 3.4127 1.00 2742 142 0.1504 0.2063
REMARK 3 5 3.4127 - 3.1682 1.00 2780 121 0.1590 0.2116
REMARK 3 6 3.1682 - 2.9814 1.00 2720 162 0.1663 0.2029
REMARK 3 7 2.9814 - 2.8321 1.00 2725 144 0.1758 0.2405
REMARK 3 8 2.8321 - 2.7088 1.00 2736 149 0.1768 0.2218
REMARK 3 9 2.7088 - 2.6046 1.00 2711 134 0.1769 0.2258
REMARK 3 10 2.6046 - 2.5147 1.00 2686 150 0.1816 0.2332
REMARK 3 11 2.5147 - 2.4361 1.00 2728 120 0.1807 0.2333
REMARK 3 12 2.4361 - 2.3664 1.00 2734 136 0.1855 0.2509
REMARK 3 13 2.3664 - 2.3041 1.00 2674 164 0.1909 0.2692
REMARK 3 14 2.3041 - 2.2479 1.00 2680 144 0.2008 0.2576
REMARK 3 15 2.2479 - 2.1968 1.00 2708 133 0.2009 0.2564
REMARK 3 16 2.1968 - 2.1501 1.00 2675 130 0.2186 0.3161
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.33
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 : 0.008 6799
REMARK 3 ANGLE : 0.947 9251
REMARK 3 CHIRALITY : 0.063 1011
REMARK 3 PLANARITY : 0.006 1164
REMARK 3 DIHEDRAL : 15.479 4148
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 5O9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200005389.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-16
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9660
REMARK 200 MONOCHROMATOR : DIAMOND (C110)
REMARK 200 OPTICS : COMPOUND REFRACTIVE LENS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46155
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 48.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4C2Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 6000, 0.1M SODIUM CITRATE PH
REMARK 280 5.6, 0.1M MAGNESIUM CHLORIDE, 0.1M SODIUM CHLORIDE., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.82050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.49550
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.82050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 89.49550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 4140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
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: 4160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A 95
REMARK 465 GLY A 96
REMARK 465 SER A 97
REMARK 465 GLU A 98
REMARK 465 PHE A 99
REMARK 465 SER A 100
REMARK 465 VAL A 101
REMARK 465 GLY A 102
REMARK 465 GLN A 103
REMARK 465 GLY A 104
REMARK 465 GLY B 95
REMARK 465 GLY B 96
REMARK 465 SER B 97
REMARK 465 GLU B 98
REMARK 465 PHE B 99
REMARK 465 SER B 100
REMARK 465 VAL B 101
REMARK 465 GLY B 102
REMARK 465 GLN B 103
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 GLN A 118 CG CD OE1 NE2
REMARK 470 ASN A 133 CG OD1 ND2
REMARK 470 GLN A 154 CD OE1 NE2
REMARK 470 ARG A 166 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 LYS A 310 CG CD CE NZ
REMARK 470 ARG A 316 CB CG CD NE CZ NH1 NH2
REMARK 470 ASN A 317 CG OD1 ND2
REMARK 470 GLN A 321 CG CD OE1 NE2
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 379 CG CD OE1 OE2
REMARK 470 GLU B 110 CD OE1 OE2
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLN B 118 CG CD OE1 NE2
REMARK 470 ARG B 166 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 304 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 316 CB CG CD NE CZ NH1 NH2
REMARK 470 ASN B 317 CG OD1 ND2
REMARK 470 LYS B 325 CG CD CE NZ
REMARK 470 ARG B 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 334 CG CD CE NZ
REMARK 470 LYS B 414 CG CD CE NZ
REMARK 470 1IP C 1 OAG PAP OAH OAE
REMARK 470 1IP D 1 OAG PAP OAH OAE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 7 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
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 TYR A 236 -119.68 48.71
REMARK 500 ILE A 381 -62.26 -133.44
REMARK 500 PHE A 422 -102.38 -108.13
REMARK 500 GLN A 428 -41.03 -132.43
REMARK 500 MET A 456 -133.99 46.53
REMARK 500 LYS A 466 35.42 72.85
REMARK 500 TYR B 180 -159.00 -86.74
REMARK 500 TYR B 236 -114.32 48.12
REMARK 500 SER B 315 0.72 -54.99
REMARK 500 ARG B 316 -53.12 96.20
REMARK 500 ILE B 381 -62.21 -132.14
REMARK 500 PHE B 422 -102.20 -111.58
REMARK 500 MET B 456 -134.35 47.50
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 MYA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MYA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 1IP C 1 and CYS C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 1IP D 1 and CYS D 2
DBREF 5O9T A 99 496 UNP P30419 NMT1_HUMAN 99 496
DBREF 5O9T B 99 496 UNP P30419 NMT1_HUMAN 99 496
DBREF 5O9T C 1 7 PDB 5O9T 5O9T 1 7
DBREF 5O9T D 1 7 PDB 5O9T 5O9T 1 7
SEQADV 5O9T GLY A 95 UNP P30419 EXPRESSION TAG
SEQADV 5O9T GLY A 96 UNP P30419 EXPRESSION TAG
SEQADV 5O9T SER A 97 UNP P30419 EXPRESSION TAG
SEQADV 5O9T GLU A 98 UNP P30419 EXPRESSION TAG
SEQADV 5O9T GLY B 95 UNP P30419 EXPRESSION TAG
SEQADV 5O9T GLY B 96 UNP P30419 EXPRESSION TAG
SEQADV 5O9T SER B 97 UNP P30419 EXPRESSION TAG
SEQADV 5O9T GLU B 98 UNP P30419 EXPRESSION TAG
SEQRES 1 A 402 GLY GLY SER GLU PHE SER VAL GLY GLN GLY PRO ALA LYS
SEQRES 2 A 402 THR MET GLU GLU ALA SER LYS ARG SER TYR GLN PHE TRP
SEQRES 3 A 402 ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL VAL ASN
SEQRES 4 A 402 THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN ILE ARG
SEQRES 5 A 402 GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR TRP ASP
SEQRES 6 A 402 ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS GLU LEU
SEQRES 7 A 402 TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP ASP ASP
SEQRES 8 A 402 ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE LEU LEU
SEQRES 9 A 402 TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN TRP HIS
SEQRES 10 A 402 CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU VAL GLY
SEQRES 11 A 402 PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE TYR ASP
SEQRES 12 A 402 THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU CYS VAL
SEQRES 13 A 402 HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO VAL LEU
SEQRES 14 A 402 ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU GLY ILE
SEQRES 15 A 402 PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU PRO LYS
SEQRES 16 A 402 PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER LEU ASN
SEQRES 17 A 402 PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS LEU SER
SEQRES 18 A 402 ARG ASN MET THR MET GLN ARG THR MET LYS LEU TYR ARG
SEQRES 19 A 402 LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG PRO MET
SEQRES 20 A 402 GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU LEU THR
SEQRES 21 A 402 ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL MET SER
SEQRES 22 A 402 GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN GLU ASN
SEQRES 23 A 402 ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN GLY GLU
SEQRES 24 A 402 VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO SER THR
SEQRES 25 A 402 ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS ALA ALA
SEQRES 26 A 402 TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO LEU LEU
SEQRES 27 A 402 ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS MET LYS
SEQRES 28 A 402 GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET GLU ASN
SEQRES 29 A 402 LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE GLY ASP
SEQRES 30 A 402 GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS CYS PRO
SEQRES 31 A 402 SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU GLN
SEQRES 1 B 402 GLY GLY SER GLU PHE SER VAL GLY GLN GLY PRO ALA LYS
SEQRES 2 B 402 THR MET GLU GLU ALA SER LYS ARG SER TYR GLN PHE TRP
SEQRES 3 B 402 ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL VAL ASN
SEQRES 4 B 402 THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN ILE ARG
SEQRES 5 B 402 GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR TRP ASP
SEQRES 6 B 402 ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS GLU LEU
SEQRES 7 B 402 TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP ASP ASP
SEQRES 8 B 402 ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE LEU LEU
SEQRES 9 B 402 TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN TRP HIS
SEQRES 10 B 402 CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU VAL GLY
SEQRES 11 B 402 PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE TYR ASP
SEQRES 12 B 402 THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU CYS VAL
SEQRES 13 B 402 HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO VAL LEU
SEQRES 14 B 402 ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU GLY ILE
SEQRES 15 B 402 PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU PRO LYS
SEQRES 16 B 402 PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER LEU ASN
SEQRES 17 B 402 PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS LEU SER
SEQRES 18 B 402 ARG ASN MET THR MET GLN ARG THR MET LYS LEU TYR ARG
SEQRES 19 B 402 LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG PRO MET
SEQRES 20 B 402 GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU LEU THR
SEQRES 21 B 402 ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL MET SER
SEQRES 22 B 402 GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN GLU ASN
SEQRES 23 B 402 ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN GLY GLU
SEQRES 24 B 402 VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO SER THR
SEQRES 25 B 402 ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS ALA ALA
SEQRES 26 B 402 TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO LEU LEU
SEQRES 27 B 402 ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS MET LYS
SEQRES 28 B 402 GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET GLU ASN
SEQRES 29 B 402 LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE GLY ASP
SEQRES 30 B 402 GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS CYS PRO
SEQRES 31 B 402 SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU GLN
SEQRES 1 C 7 1IP CYS PHE SER LYS PRO ARG
SEQRES 1 D 7 1IP CYS PHE SER LYS PRO ARG
HET 1IP C 1 11
HET 1IP D 1 11
HET MYA A 501 63
HET GOL A 502 6
HET GOL A 503 6
HET CL A 504 1
HET MYA B 501 63
HET GOL B 502 6
HET GOL B 503 6
HET CL B 504 1
HETNAM 1IP N~2~-(PHOSPHONOACETYL)-L-ASPARAGINE
HETNAM MYA TETRADECANOYL-COA
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN MYA MYRISTOYL-COA
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 1IP 2(C6 H11 N2 O7 P)
FORMUL 5 MYA 2(C35 H62 N7 O17 P3 S)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 8 CL 2(CL 1-)
FORMUL 13 HOH *368(H2 O)
HELIX 1 AA1 THR A 108 LYS A 114 1 7
HELIX 2 AA2 PHE A 119 GLN A 123 5 5
HELIX 3 AA3 ASP A 165 TYR A 180 1 16
HELIX 4 AA4 SER A 193 ARG A 202 1 10
HELIX 5 AA5 LEU A 207 GLN A 209 5 3
HELIX 6 AA6 LYS A 252 ARG A 255 5 4
HELIX 7 AA7 ARG A 258 LEU A 273 1 16
HELIX 8 AA8 ASN A 302 VAL A 309 1 8
HELIX 9 AA9 THR A 319 ARG A 328 1 10
HELIX 10 AB1 GLU A 342 LYS A 344 5 3
HELIX 11 AB2 ASP A 345 LYS A 358 1 14
HELIX 12 AB3 SER A 367 TYR A 376 1 10
HELIX 13 AB4 PRO A 430 LYS A 445 1 16
HELIX 14 AB5 ASN A 458 GLU A 463 1 6
HELIX 15 AB6 GLY A 487 VAL A 491 5 5
HELIX 16 AB7 THR B 108 LYS B 114 1 7
HELIX 17 AB8 PHE B 119 GLN B 123 5 5
HELIX 18 AB9 ASP B 165 TYR B 180 1 16
HELIX 19 AC1 SER B 193 ARG B 202 1 10
HELIX 20 AC2 LEU B 207 GLN B 209 5 3
HELIX 21 AC3 LYS B 252 ARG B 255 5 4
HELIX 22 AC4 ARG B 258 LEU B 273 1 16
HELIX 23 AC5 ASN B 302 VAL B 309 1 8
HELIX 24 AC6 THR B 319 ARG B 328 1 10
HELIX 25 AC7 GLU B 342 LYS B 344 5 3
HELIX 26 AC8 ASP B 345 LYS B 358 1 14
HELIX 27 AC9 SER B 367 TYR B 376 1 10
HELIX 28 AD1 PRO B 430 LYS B 445 1 16
HELIX 29 AD2 GLU B 457 PHE B 461 5 5
HELIX 30 AD3 GLY B 487 VAL B 491 5 5
SHEET 1 AA111 PHE A 156 ALA A 160 0
SHEET 2 AA111 HIS A 211 VAL A 216 -1 O ARG A 215 N THR A 157
SHEET 3 AA111 LEU A 222 ILE A 235 -1 O VAL A 223 N VAL A 214
SHEET 4 AA111 THR A 238 VAL A 250 -1 O LYS A 240 N ILE A 233
SHEET 5 AA111 ALA A 279 ALA A 283 1 O VAL A 280 N VAL A 243
SHEET 6 AA111 GLY A 468 TYR A 479 -1 O TYR A 477 N TYR A 281
SHEET 7 AA111 GLY A 292 SER A 300 -1 N HIS A 298 O GLY A 468
SHEET 8 AA111 VAL A 449 LEU A 453 -1 O ALA A 452 N TRP A 297
SHEET 9 AA111 ALA A 418 SER A 421 1 N ALA A 419 O ASN A 451
SHEET 10 AA111 VAL A 394 THR A 402 -1 N TYR A 401 O TYR A 420
SHEET 11 AA111 LEU A 362 PRO A 364 0
SHEET 1 AA211 LEU A 338 PRO A 340 0
SHEET 2 AA211 ILE A 382 GLU A 388 -1 O VAL A 386 N ARG A 339
SHEET 3 AA211 VAL A 394 THR A 402 -1 O ASP A 396 N VAL A 387
SHEET 4 AA211 ALA A 418 SER A 421 -1 O TYR A 420 N TYR A 401
SHEET 5 AA211 VAL A 449 LEU A 453 1 O ASN A 451 N ALA A 419
SHEET 6 AA211 GLY A 292 SER A 300 -1 N TRP A 297 O ALA A 452
SHEET 7 AA211 GLY A 468 TYR A 479 -1 O GLY A 468 N HIS A 298
SHEET 8 AA211 ALA A 279 ALA A 283 -1 N TYR A 281 O TYR A 477
SHEET 9 AA211 THR A 238 VAL A 250 1 N VAL A 243 O VAL A 280
SHEET 10 AA211 LEU A 222 ILE A 235 -1 N ILE A 233 O LYS A 240
SHEET 11 AA211 VAL A 425 HIS A 426 0
SHEET 1 AA3 3 PHE A 188 PHE A 190 0
SHEET 2 AA3 3 SER A 405 ILE A 407 -1 O THR A 406 N ARG A 189
SHEET 3 AA3 3 SER A 415 LEU A 416 -1 O LEU A 416 N SER A 405
SHEET 1 AA411 PHE B 156 ALA B 160 0
SHEET 2 AA411 HIS B 211 VAL B 216 -1 O ARG B 215 N THR B 157
SHEET 3 AA411 LEU B 222 ILE B 235 -1 O VAL B 223 N VAL B 214
SHEET 4 AA411 THR B 238 VAL B 250 -1 O MET B 242 N ALA B 231
SHEET 5 AA411 ALA B 279 ALA B 283 1 O VAL B 280 N VAL B 243
SHEET 6 AA411 GLY B 468 TYR B 479 -1 O TYR B 477 N TYR B 281
SHEET 7 AA411 GLY B 292 SER B 300 -1 N CYS B 294 O LEU B 474
SHEET 8 AA411 VAL B 449 LEU B 453 -1 O ALA B 452 N TRP B 297
SHEET 9 AA411 ALA B 418 SER B 421 1 N ALA B 419 O ASN B 451
SHEET 10 AA411 VAL B 394 THR B 402 -1 N TYR B 401 O TYR B 420
SHEET 11 AA411 LEU B 362 VAL B 365 0
SHEET 1 AA511 LEU B 338 PRO B 340 0
SHEET 2 AA511 ILE B 382 GLU B 388 -1 O VAL B 386 N ARG B 339
SHEET 3 AA511 VAL B 394 THR B 402 -1 O ASP B 396 N VAL B 387
SHEET 4 AA511 ALA B 418 SER B 421 -1 O TYR B 420 N TYR B 401
SHEET 5 AA511 VAL B 449 LEU B 453 1 O ASN B 451 N ALA B 419
SHEET 6 AA511 GLY B 292 SER B 300 -1 N TRP B 297 O ALA B 452
SHEET 7 AA511 GLY B 468 TYR B 479 -1 O LEU B 474 N CYS B 294
SHEET 8 AA511 ALA B 279 ALA B 283 -1 N TYR B 281 O TYR B 477
SHEET 9 AA511 THR B 238 VAL B 250 1 N VAL B 243 O VAL B 280
SHEET 10 AA511 LEU B 222 ILE B 235 -1 N ALA B 231 O MET B 242
SHEET 11 AA511 VAL B 425 HIS B 426 0
SHEET 1 AA6 2 PHE B 188 PHE B 190 0
SHEET 2 AA6 2 SER B 405 ILE B 407 -1 O THR B 406 N ARG B 189
LINK C 1IP C 1 N CYS C 2 1555 1555 1.32
LINK C 1IP D 1 N CYS D 2 1555 1555 1.33
CISPEP 1 PRO A 288 LYS A 289 0 -6.27
CISPEP 2 ARG A 316 ASN A 317 0 0.00
CISPEP 3 PRO B 288 LYS B 289 0 -15.02
SITE 1 AC1 27 ARG A 115 TYR A 117 GLN A 118 PHE A 119
SITE 2 AC1 27 TRP A 120 ASN A 179 TYR A 180 VAL A 181
SITE 3 AC1 27 ILE A 245 ASN A 246 PHE A 247 LEU A 248
SITE 4 AC1 27 CYS A 249 VAL A 250 ARG A 255 SER A 256
SITE 5 AC1 27 ARG A 258 VAL A 259 ALA A 260 PRO A 261
SITE 6 AC1 27 THR A 268 TYR A 281 THR A 282 LEU A 287
SITE 7 AC1 27 TYR A 479 HOH A 673 1IP C 1
SITE 1 AC2 7 GLU A 244 TRP A 374 TYR A 423 LEU A 493
SITE 2 AC2 7 VAL A 494 LEU A 495 GLN A 496
SITE 1 AC3 9 LYS A 289 PRO A 290 VAL A 291 LEU A 478
SITE 2 AC3 9 TRP A 481 LYS A 482 CYS A 483 SER A 485
SITE 3 AC3 9 HOH A 649
SITE 1 AC4 5 LEU A 161 LEU A 163 ARG A 202 TRP A 206
SITE 2 AC4 5 HIS A 211
SITE 1 AC5 32 ARG B 115 TYR B 117 GLN B 118 PHE B 119
SITE 2 AC5 32 TRP B 120 ASN B 179 TYR B 180 VAL B 181
SITE 3 AC5 32 ASN B 246 PHE B 247 LEU B 248 CYS B 249
SITE 4 AC5 32 VAL B 250 ARG B 255 SER B 256 ARG B 258
SITE 5 AC5 32 VAL B 259 ALA B 260 PRO B 261 THR B 268
SITE 6 AC5 32 PHE B 277 TYR B 281 THR B 282 LEU B 287
SITE 7 AC5 32 TYR B 479 HOH B 616 HOH B 653 HOH B 700
SITE 8 AC5 32 HOH B 712 HOH B 717 HOH B 733 1IP D 1
SITE 1 AC6 8 PRO B 126 LYS B 289 VAL B 291 LEU B 478
SITE 2 AC6 8 TRP B 481 LYS B 482 CYS B 483 HOH B 664
SITE 1 AC7 8 GLU B 244 PRO B 364 MET B 366 TRP B 374
SITE 2 AC7 8 TYR B 423 VAL B 494 GLN B 496 HOH B 683
SITE 1 AC8 4 LEU B 163 ARG B 202 TRP B 206 HIS B 211
SITE 1 AC9 16 TYR A 180 PHE A 190 TYR A 192 ASN A 246
SITE 2 AC9 16 THR A 282 ALA A 283 GLY A 284 TYR A 296
SITE 3 AC9 16 TYR A 401 ASN A 473 GLN A 496 MYA A 501
SITE 4 AC9 16 HOH A 697 HOH A 701 PHE C 3 SER C 4
SITE 1 AD1 16 PHE B 190 ASN B 246 THR B 282 ALA B 283
SITE 2 AD1 16 TYR B 296 TYR B 401 ASN B 473 LEU B 474
SITE 3 AD1 16 GLN B 496 MYA B 501 HOH B 640 HOH B 680
SITE 4 AD1 16 HOH B 694 PHE D 3 SER D 4 HOH D 102
CRYST1 58.221 79.641 178.991 90.00 90.00 90.00 P 2 21 21 8
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 0.017176 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012556 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005587 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
