HEADER TRANSFERASE 12-JAN-17 5MU6
TITLE HUMAN N-MYRISTOYLTRANSFERASE (NMT1) WITH MYRISTOYL-COA AND IMP-1088
TITLE 2 INHIBITOR BOUND
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
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_STRAIN: PRARES;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28
KEYWDS N-MYRISTOYLATION, INHIBITOR, RHINOVIRUS CAPSULE ASSEMBLY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PEREZ-DORADO,A.S.BELL,E.W.TATE
REVDAT 4 17-JAN-24 5MU6 1 LINK
REVDAT 3 04-JUL-18 5MU6 1 JRNL
REVDAT 2 23-MAY-18 5MU6 1 JRNL
REVDAT 1 14-FEB-18 5MU6 0
JRNL AUTH A.MOUSNIER,A.S.BELL,D.P.SWIEBODA,J.MORALES-SANFRUTOS,
JRNL AUTH 2 I.PEREZ-DORADO,J.A.BRANNIGAN,J.NEWMAN,M.RITZEFELD,
JRNL AUTH 3 J.A.HUTTON,A.GUEDAN,A.S.ASFOR,S.W.ROBINSON,
JRNL AUTH 4 I.HOPKINS-NAVRATILOVA,A.J.WILKINSON,S.L.JOHNSTON,
JRNL AUTH 5 R.J.LEATHERBARROW,T.J.TUTHILL,R.SOLARI,E.W.TATE
JRNL TITL FRAGMENT-DERIVED INHIBITORS OF HUMAN N-MYRISTOYLTRANSFERASE
JRNL TITL 2 BLOCK CAPSID ASSEMBLY AND REPLICATION OF THE COMMON COLD
JRNL TITL 3 VIRUS.
JRNL REF NAT CHEM V. 10 599 2018
JRNL REFN ESSN 1755-4349
JRNL PMID 29760414
JRNL DOI 10.1038/S41557-018-0039-2
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 69279
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3449
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 72.2320 - 5.4964 1.00 2842 164 0.1799 0.2099
REMARK 3 2 5.4964 - 4.3628 1.00 2728 134 0.1465 0.1492
REMARK 3 3 4.3628 - 3.8114 1.00 2693 138 0.1475 0.1635
REMARK 3 4 3.8114 - 3.4629 1.00 2646 151 0.1650 0.2261
REMARK 3 5 3.4629 - 3.2147 1.00 2679 141 0.1769 0.2251
REMARK 3 6 3.2147 - 3.0252 1.00 2636 139 0.2018 0.2496
REMARK 3 7 3.0252 - 2.8737 1.00 2646 136 0.2066 0.2697
REMARK 3 8 2.8737 - 2.7486 1.00 2642 143 0.2085 0.2614
REMARK 3 9 2.7486 - 2.6427 1.00 2638 133 0.2024 0.2659
REMARK 3 10 2.6427 - 2.5515 1.00 2631 121 0.2128 0.2712
REMARK 3 11 2.5515 - 2.4718 1.00 2601 140 0.2185 0.2796
REMARK 3 12 2.4718 - 2.4011 1.00 2622 137 0.2176 0.3141
REMARK 3 13 2.4011 - 2.3379 0.99 2621 137 0.2224 0.2537
REMARK 3 14 2.3379 - 2.2808 1.00 2589 163 0.2261 0.2618
REMARK 3 15 2.2808 - 2.2290 1.00 2645 118 0.2255 0.2569
REMARK 3 16 2.2290 - 2.1816 1.00 2532 151 0.2416 0.2647
REMARK 3 17 2.1816 - 2.1379 1.00 2631 141 0.2356 0.2952
REMARK 3 18 2.1379 - 2.0976 1.00 2611 134 0.2505 0.2903
REMARK 3 19 2.0976 - 2.0601 1.00 2617 140 0.2358 0.2906
REMARK 3 20 2.0601 - 2.0252 1.00 2592 127 0.2571 0.3282
REMARK 3 21 2.0252 - 1.9925 1.00 2646 120 0.2551 0.2926
REMARK 3 22 1.9925 - 1.9618 0.99 2559 121 0.2838 0.3312
REMARK 3 23 1.9618 - 1.9330 0.99 2608 125 0.2948 0.3484
REMARK 3 24 1.9330 - 1.9058 1.00 2597 150 0.3113 0.3771
REMARK 3 25 1.9058 - 1.8800 1.00 2578 145 0.3161 0.3662
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.690
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.82
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 6670
REMARK 3 ANGLE : 1.242 9078
REMARK 3 CHIRALITY : 0.051 973
REMARK 3 PLANARITY : 0.005 1130
REMARK 3 DIHEDRAL : 14.549 2516
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 5MU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1200003008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-15
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 : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92819
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 : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 72.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.25400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 1.65400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4C2Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% (V/W) MME2K, 0.2M KBR, 100 MM
REMARK 280 SODIUM CITRATE PH 4.5, AND 5% (V/V) GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,Y+1/2,-Z
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 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 39.36500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.36500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.36500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.36500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 106
REMARK 465 PRO A 107
REMARK 465 HIS A 108
REMARK 465 MET A 109
REMARK 465 GLU A 110
REMARK 465 GLU A 111
REMARK 465 ALA A 112
REMARK 465 SER A 113
REMARK 465 LYS A 114
REMARK 465 GLY B 106
REMARK 465 PRO B 107
REMARK 465 HIS B 108
REMARK 465 MET B 109
REMARK 465 GLU B 110
REMARK 465 GLU B 111
REMARK 465 ALA B 112
REMARK 465 SER B 113
REMARK 465 LYS B 114
REMARK 465 ASN B 409
REMARK 465 HIS B 410
REMARK 465 PRO B 411
REMARK 465 THR B 412
REMARK 465 HIS B 413
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 OE2 GLU B 393 O HOH B 601 2.03
REMARK 500 NZ LYS B 240 O HOH B 602 2.15
REMARK 500 OD1 ASP B 448 O HOH B 603 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 TYR A 180 -157.33 -89.57
REMARK 500 TYR A 236 -116.98 49.13
REMARK 500 ILE A 381 -60.05 -131.57
REMARK 500 ASN A 389 -167.58 -76.34
REMARK 500 PHE A 422 -101.07 -110.83
REMARK 500 MET A 456 -128.40 49.73
REMARK 500 LYS A 466 30.35 70.15
REMARK 500 TYR B 180 -157.00 -90.34
REMARK 500 TYR B 236 -117.23 48.71
REMARK 500 ILE B 381 -60.38 -131.46
REMARK 500 PHE B 422 -100.27 -111.18
REMARK 500 MET B 456 -129.33 47.51
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 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 254 O
REMARK 620 2 MYA A 501 O4A 102.2
REMARK 620 N 1
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 MG 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 GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KFK A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MYA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KFK B 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4C2Y RELATED DB: PDB
REMARK 900 HUMAN N-MYRISTOYLTRANSFERASE (NMT1) WITH MYRISTOYL-COA CO-FACTOR
REMARK 900 RELATED ID: 4C2Z RELATED DB: PDB
REMARK 900 HUMAN N-MYRISTOYLTRANSFERASE (NMT1) WITH MYRISTOYL-COA AND
REMARK 900 INHIBITOR BOUND
DBREF 5MU6 A 109 496 UNP P30419 NMT1_HUMAN 29 416
DBREF 5MU6 B 109 496 UNP P30419 NMT1_HUMAN 29 416
SEQADV 5MU6 GLY A 106 UNP P30419 EXPRESSION TAG
SEQADV 5MU6 PRO A 107 UNP P30419 EXPRESSION TAG
SEQADV 5MU6 HIS A 108 UNP P30419 EXPRESSION TAG
SEQADV 5MU6 GLY B 106 UNP P30419 EXPRESSION TAG
SEQADV 5MU6 PRO B 107 UNP P30419 EXPRESSION TAG
SEQADV 5MU6 HIS B 108 UNP P30419 EXPRESSION TAG
SEQRES 1 A 391 GLY PRO HIS MET GLU GLU ALA SER LYS ARG SER TYR GLN
SEQRES 2 A 391 PHE TRP ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL
SEQRES 3 A 391 VAL ASN THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN
SEQRES 4 A 391 ILE ARG GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR
SEQRES 5 A 391 TRP ASP ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS
SEQRES 6 A 391 GLU LEU TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP
SEQRES 7 A 391 ASP ASP ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE
SEQRES 8 A 391 LEU LEU TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN
SEQRES 9 A 391 TRP HIS CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU
SEQRES 10 A 391 VAL GLY PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE
SEQRES 11 A 391 TYR ASP THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU
SEQRES 12 A 391 CYS VAL HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO
SEQRES 13 A 391 VAL LEU ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU
SEQRES 14 A 391 GLY ILE PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU
SEQRES 15 A 391 PRO LYS PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER
SEQRES 16 A 391 LEU ASN PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS
SEQRES 17 A 391 LEU SER ARG ASN MET THR MET GLN ARG THR MET LYS LEU
SEQRES 18 A 391 TYR ARG LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG
SEQRES 19 A 391 PRO MET GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU
SEQRES 20 A 391 LEU THR ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL
SEQRES 21 A 391 MET SER GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN
SEQRES 22 A 391 GLU ASN ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN
SEQRES 23 A 391 GLY GLU VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO
SEQRES 24 A 391 SER THR ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS
SEQRES 25 A 391 ALA ALA TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO
SEQRES 26 A 391 LEU LEU ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS
SEQRES 27 A 391 MET LYS GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET
SEQRES 28 A 391 GLU ASN LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE
SEQRES 29 A 391 GLY ASP GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS
SEQRES 30 A 391 CYS PRO SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU
SEQRES 31 A 391 GLN
SEQRES 1 B 391 GLY PRO HIS MET GLU GLU ALA SER LYS ARG SER TYR GLN
SEQRES 2 B 391 PHE TRP ASP THR GLN PRO VAL PRO LYS LEU GLY GLU VAL
SEQRES 3 B 391 VAL ASN THR HIS GLY PRO VAL GLU PRO ASP LYS ASP ASN
SEQRES 4 B 391 ILE ARG GLN GLU PRO TYR THR LEU PRO GLN GLY PHE THR
SEQRES 5 B 391 TRP ASP ALA LEU ASP LEU GLY ASP ARG GLY VAL LEU LYS
SEQRES 6 B 391 GLU LEU TYR THR LEU LEU ASN GLU ASN TYR VAL GLU ASP
SEQRES 7 B 391 ASP ASP ASN MET PHE ARG PHE ASP TYR SER PRO GLU PHE
SEQRES 8 B 391 LEU LEU TRP ALA LEU ARG PRO PRO GLY TRP LEU PRO GLN
SEQRES 9 B 391 TRP HIS CYS GLY VAL ARG VAL VAL SER SER ARG LYS LEU
SEQRES 10 B 391 VAL GLY PHE ILE SER ALA ILE PRO ALA ASN ILE HIS ILE
SEQRES 11 B 391 TYR ASP THR GLU LYS LYS MET VAL GLU ILE ASN PHE LEU
SEQRES 12 B 391 CYS VAL HIS LYS LYS LEU ARG SER LYS ARG VAL ALA PRO
SEQRES 13 B 391 VAL LEU ILE ARG GLU ILE THR ARG ARG VAL HIS LEU GLU
SEQRES 14 B 391 GLY ILE PHE GLN ALA VAL TYR THR ALA GLY VAL VAL LEU
SEQRES 15 B 391 PRO LYS PRO VAL GLY THR CYS ARG TYR TRP HIS ARG SER
SEQRES 16 B 391 LEU ASN PRO ARG LYS LEU ILE GLU VAL LYS PHE SER HIS
SEQRES 17 B 391 LEU SER ARG ASN MET THR MET GLN ARG THR MET LYS LEU
SEQRES 18 B 391 TYR ARG LEU PRO GLU THR PRO LYS THR ALA GLY LEU ARG
SEQRES 19 B 391 PRO MET GLU THR LYS ASP ILE PRO VAL VAL HIS GLN LEU
SEQRES 20 B 391 LEU THR ARG TYR LEU LYS GLN PHE HIS LEU THR PRO VAL
SEQRES 21 B 391 MET SER GLN GLU GLU VAL GLU HIS TRP PHE TYR PRO GLN
SEQRES 22 B 391 GLU ASN ILE ILE ASP THR PHE VAL VAL GLU ASN ALA ASN
SEQRES 23 B 391 GLY GLU VAL THR ASP PHE LEU SER PHE TYR THR LEU PRO
SEQRES 24 B 391 SER THR ILE MET ASN HIS PRO THR HIS LYS SER LEU LYS
SEQRES 25 B 391 ALA ALA TYR SER PHE TYR ASN VAL HIS THR GLN THR PRO
SEQRES 26 B 391 LEU LEU ASP LEU MET SER ASP ALA LEU VAL LEU ALA LYS
SEQRES 27 B 391 MET LYS GLY PHE ASP VAL PHE ASN ALA LEU ASP LEU MET
SEQRES 28 B 391 GLU ASN LYS THR PHE LEU GLU LYS LEU LYS PHE GLY ILE
SEQRES 29 B 391 GLY ASP GLY ASN LEU GLN TYR TYR LEU TYR ASN TRP LYS
SEQRES 30 B 391 CYS PRO SER MET GLY ALA GLU LYS VAL GLY LEU VAL LEU
SEQRES 31 B 391 GLN
HET MYA A 501 63
HET MG A 502 1
HET GOL A 503 6
HET GOL A 504 6
HET KFK A 505 33
HET MYA B 501 63
HET MG B 502 1
HET GOL B 503 6
HET GOL B 504 6
HET KFK B 505 33
HETNAM MYA TETRADECANOYL-COA
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM KFK 1-[5-[3,4-BIS(FLUORANYL)-2-[2-(1,3,5-TRIMETHYLPYRAZOL-
HETNAM 2 KFK 4-YL)ETHOXY]PHENYL]-1-METHYL-INDAZOL-3-YL]-~{N},~{N}-
HETNAM 3 KFK DIMETHYL-METHANAMINE
HETSYN MYA MYRISTOYL-COA
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MYA 2(C35 H62 N7 O17 P3 S)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 7 KFK 2(C25 H29 F2 N5 O)
FORMUL 13 HOH *456(H2 O)
HELIX 1 AA1 PHE A 119 GLN A 123 5 5
HELIX 2 AA2 ASP A 165 TYR A 180 1 16
HELIX 3 AA3 SER A 193 ARG A 202 1 10
HELIX 4 AA4 LEU A 207 GLN A 209 5 3
HELIX 5 AA5 LYS A 252 ARG A 255 5 4
HELIX 6 AA6 VAL A 259 LEU A 273 1 15
HELIX 7 AA7 ASN A 302 VAL A 309 1 8
HELIX 8 AA8 THR A 319 TYR A 327 1 9
HELIX 9 AA9 GLU A 342 LYS A 344 5 3
HELIX 10 AB1 ASP A 345 LYS A 358 1 14
HELIX 11 AB2 SER A 367 TYR A 376 1 10
HELIX 12 AB3 PRO A 430 LYS A 445 1 16
HELIX 13 AB4 GLU A 457 PHE A 461 5 5
HELIX 14 AB5 GLY A 487 VAL A 491 5 5
HELIX 15 AB6 PHE B 119 GLN B 123 5 5
HELIX 16 AB7 ASP B 165 TYR B 180 1 16
HELIX 17 AB8 SER B 193 ARG B 202 1 10
HELIX 18 AB9 LEU B 207 GLN B 209 5 3
HELIX 19 AC1 LYS B 252 ARG B 255 5 4
HELIX 20 AC2 VAL B 259 LEU B 273 1 15
HELIX 21 AC3 ASN B 302 VAL B 309 1 8
HELIX 22 AC4 THR B 319 TYR B 327 1 9
HELIX 23 AC5 GLU B 342 LYS B 344 5 3
HELIX 24 AC6 ASP B 345 LEU B 357 1 13
HELIX 25 AC7 LYS B 358 PHE B 360 5 3
HELIX 26 AC8 SER B 367 TYR B 376 1 10
HELIX 27 AC9 PRO B 430 LYS B 445 1 16
HELIX 28 AD1 GLU B 457 PHE B 461 5 5
HELIX 29 AD2 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 CYS A 294 O LEU A 474
SHEET 8 AA111 VAL A 449 LEU A 453 -1 O PHE A 450 N ARG A 299
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 LEU A 398 N PHE A 385
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 ARG A 299 O PHE A 450
SHEET 7 AA211 GLY A 468 TYR A 479 -1 O LEU A 474 N CYS A 294
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 LYS B 240 N ILE B 233
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 GLN B 475 N ALA B 283
SHEET 7 AA411 GLY B 292 SER B 300 -1 N HIS B 298 O GLY B 468
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 LEU B 398 N PHE B 385
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 GLY B 468 N HIS B 298
SHEET 8 AA511 ALA B 279 ALA B 283 -1 N ALA B 283 O GLN B 475
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 ILE B 233 O LYS B 240
SHEET 11 AA511 VAL B 425 HIS B 426 0
SHEET 1 AA6 3 PHE B 188 PHE B 190 0
SHEET 2 AA6 3 SER B 405 ILE B 407 -1 O THR B 406 N ARG B 189
SHEET 3 AA6 3 SER B 415 LEU B 416 -1 O LEU B 416 N SER B 405
LINK O LEU A 254 MG MG A 502 1555 1555 2.52
LINK O4A MYA A 501 MG MG A 502 1555 1555 2.92
LINK O LEU B 254 MG MG B 502 1555 1555 2.56
CISPEP 1 PRO A 288 LYS A 289 0 -10.78
CISPEP 2 PRO B 288 LYS B 289 0 -10.64
SITE 1 AC1 28 TYR A 117 GLN A 118 PHE A 119 TRP A 120
SITE 2 AC1 28 TYR A 180 VAL A 181 PHE A 247 LEU A 248
SITE 3 AC1 28 CYS A 249 VAL A 250 ARG A 255 SER A 256
SITE 4 AC1 28 ARG A 258 VAL A 259 ALA A 260 PRO A 261
SITE 5 AC1 28 THR A 268 PHE A 277 THR A 282 LEU A 287
SITE 6 AC1 28 TYR A 479 MG A 502 HOH A 622 HOH A 665
SITE 7 AC1 28 HOH A 693 HOH A 726 HOH A 756 HOH A 758
SITE 1 AC2 7 LEU A 254 ARG A 255 SER A 256 LYS A 257
SITE 2 AC2 7 ARG A 258 VAL A 259 MYA A 501
SITE 1 AC3 7 LYS A 289 PRO A 290 VAL A 291 LEU A 478
SITE 2 AC3 7 TRP A 481 LYS A 482 CYS A 483
SITE 1 AC4 5 GLU A 244 TRP A 374 TYR A 423 VAL A 494
SITE 2 AC4 5 GLN A 496
SITE 1 AC5 13 VAL A 181 PHE A 188 PHE A 190 ASN A 246
SITE 2 AC5 13 THR A 282 TYR A 296 HIS A 298 SER A 405
SITE 3 AC5 13 TYR A 420 ASN A 451 ALA A 452 LEU A 495
SITE 4 AC5 13 GLN A 496
SITE 1 AC6 31 ARG B 115 TYR B 117 GLN B 118 PHE B 119
SITE 2 AC6 31 TRP B 120 TYR B 180 VAL B 181 ILE B 245
SITE 3 AC6 31 PHE B 247 LEU B 248 CYS B 249 VAL B 250
SITE 4 AC6 31 ARG B 255 SER B 256 LYS B 257 ARG B 258
SITE 5 AC6 31 VAL B 259 ALA B 260 PRO B 261 THR B 268
SITE 6 AC6 31 PHE B 277 ALA B 279 TYR B 281 THR B 282
SITE 7 AC6 31 LEU B 287 MG B 502 HOH B 642 HOH B 661
SITE 8 AC6 31 HOH B 695 HOH B 723 HOH B 729
SITE 1 AC7 6 LEU B 254 SER B 256 LYS B 257 ARG B 258
SITE 2 AC7 6 VAL B 259 MYA B 501
SITE 1 AC8 7 PRO B 126 LYS B 289 LEU B 478 TRP B 481
SITE 2 AC8 7 LYS B 482 CYS B 483 HOH B 614
SITE 1 AC9 6 GLU B 244 TRP B 374 TYR B 423 VAL B 494
SITE 2 AC9 6 GLN B 496 HOH B 635
SITE 1 AD1 14 VAL B 181 PHE B 188 ARG B 189 PHE B 190
SITE 2 AD1 14 ASN B 246 THR B 282 TYR B 296 HIS B 298
SITE 3 AD1 14 SER B 405 TYR B 420 ASN B 451 ALA B 452
SITE 4 AD1 14 LEU B 495 GLN B 496
CRYST1 78.730 180.730 58.990 90.00 90.00 90.00 P 21 21 2 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 0.012702 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016952 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
