HEADER ISOMERASE 03-NOV-03 1O6C
TITLE CRYSTAL STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UDP-GLCNAC-2-EPIMERASE;
COMPND 5 EC: 5.1.3.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: MNAA, BSU35660;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURAL GENOMICS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR STRUCTURAL GENOMIX
REVDAT 7 27-DEC-23 1O6C 1 SEQADV LINK
REVDAT 6 04-OCT-17 1O6C 1 REMARK
REVDAT 5 13-JUL-11 1O6C 1 VERSN
REVDAT 4 24-FEB-09 1O6C 1 VERSN
REVDAT 3 30-AUG-05 1O6C 1 JRNL
REVDAT 2 30-DEC-03 1O6C 1 JRNL
REVDAT 1 25-NOV-03 1O6C 0
JRNL AUTH J.BADGER,J.M.SAUDER,J.M.ADAMS,S.ANTONYSAMY,K.BAIN,
JRNL AUTH 2 M.G.BERGSEID,S.G.BUCHANAN,M.D.BUCHANAN,Y.BATIYENKO,
JRNL AUTH 3 J.A.CHRISTOPHER,S.EMTAGE,A.EROSHKINA,I.FEIL,E.B.FURLONG,
JRNL AUTH 4 K.S.GAJIWALA,X.GAO,D.HE,J.HENDLE,A.HUBER,K.HODA,P.KEARINS,
JRNL AUTH 5 C.KISSINGER,B.LAUBERT,H.A.LEWIS,J.LIN,K.LOOMIS,D.LORIMER,
JRNL AUTH 6 G.LOUIE,M.MALETIC,C.D.MARSH,I.MILLER,J.MOLINARI,
JRNL AUTH 7 H.J.MULLER-DIECKMANN,J.M.NEWMAN,B.W.NOLAND,B.PAGARIGAN,
JRNL AUTH 8 F.PARK,T.S.PEAT,K.W.POST,S.RADOJICIC,A.RAMOS,R.ROMERO,
JRNL AUTH 9 M.E.RUTTER,W.E.SANDERSON,K.D.SCHWINN,J.TRESSER,J.WINHOVEN,
JRNL AUTH10 T.A.WRIGHT,L.WU,J.XU,T.J.HARRIS
JRNL TITL STRUCTURAL ANALYSIS OF A SET OF PROTEINS RESULTING FROM A
JRNL TITL 2 BACTERIAL GENOMICS PROJECT
JRNL REF PROTEINS V. 60 787 2005
JRNL REFN ISSN 0887-3585
JRNL PMID 16021622
JRNL DOI 10.1002/PROT.20541
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 4.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 21936
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.274
REMARK 3 FREE R VALUE : 0.334
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2141
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65300
REMARK 3 B22 (A**2) : -0.65300
REMARK 3 B33 (A**2) : 1.30600
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 2.120 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.013 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.135 ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.883 ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.137 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.962 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.581 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.544 ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000001850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 32-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, TRUNCATE
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21936
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SE-MET SAD PHASING
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 226.21500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.91000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.91000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 339.32250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.91000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.91000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.10750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.91000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.91000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 339.32250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.91000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.91000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 113.10750
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 226.21500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 MSE A 1
REMARK 465 ALA A 206
REMARK 465 HIS A 207
REMARK 465 ARG A 208
REMARK 465 ARG A 209
REMARK 465 GLU A 210
REMARK 465 ASN A 211
REMARK 465 LEU A 212
REMARK 465 GLY A 213
REMARK 465 GLU A 214
REMARK 465 PRO A 215
REMARK 465 VAL A 239
REMARK 465 HIS A 240
REMARK 465 LEU A 241
REMARK 465 ASN A 242
REMARK 465 PHE A 253
REMARK 465 GLY A 254
REMARK 465 SER A 284
REMARK 465 GLY A 285
REMARK 465 ARG A 307
REMARK 465 PRO A 308
REMARK 465 GLU A 309
REMARK 465 GLY A 379
REMARK 465 LYS A 380
REMARK 465 GLY A 381
REMARK 465 SER A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS B 207
REMARK 465 ARG B 208
REMARK 465 ARG B 209
REMARK 465 GLU B 210
REMARK 465 ASN B 211
REMARK 465 LEU B 212
REMARK 465 GLY B 213
REMARK 465 GLU B 214
REMARK 465 LYS B 380
REMARK 465 GLY B 381
REMARK 465 SER B 382
REMARK 465 HIS B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
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 GLN A 41 CD OE1 NE2
REMARK 470 GLN A 44 CG CD OE1 NE2
REMARK 470 MSE A 45 CB CG SE CE
REMARK 470 LEU A 46 CD1 CD2
REMARK 470 ASP A 47 CG OD1 OD2
REMARK 470 GLU A 66 CB CG CD OE1 OE2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 ASP A 87 CG OD1 OD2
REMARK 470 SER A 189 CB OG
REMARK 470 PRO A 191 CG CD
REMARK 470 LEU A 193 CG CD1 CD2
REMARK 470 GLU A 198 CG CD OE1 OE2
REMARK 470 ASP A 199 CB CG OD1 OD2
REMARK 470 LYS A 200 CD CE NZ
REMARK 470 MSE A 216 CB CG SE CE
REMARK 470 GLU A 217 CB CG CD OE1 OE2
REMARK 470 MSE A 219 CB CG SE CE
REMARK 470 LYS A 221 CG CD CE NZ
REMARK 470 GLU A 231 CB CG CD OE1 OE2
REMARK 470 ASP A 232 CG OD1 OD2
REMARK 470 VAL A 245 CB CG1 CG2
REMARK 470 ARG A 246 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 247 CG CD OE1 OE2
REMARK 470 HIS A 250 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 251 NZ
REMARK 470 ASP A 255 CG OD1 OD2
REMARK 470 ASP A 257 CG OD1 OD2
REMARK 470 ARG A 258 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 259 CG1 CG2
REMARK 470 LEU A 261 CD1 CD2
REMARK 470 ILE A 262 CG1 CG2 CD1
REMARK 470 LEU A 265 CG CD1 CD2
REMARK 470 GLU A 266 CG CD OE1 OE2
REMARK 470 ILE A 268 CG1 CG2 CD1
REMARK 470 SER A 277 CB OG
REMARK 470 GLU A 289 CG CD OE1 OE2
REMARK 470 PRO A 292 CG CD
REMARK 470 ARG A 302 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 303 CG OD1 OD2
REMARK 470 VAL A 311 CG1 CG2
REMARK 470 THR A 315 OG1 CG2
REMARK 470 LEU A 316 CB CG CD1 CD2
REMARK 470 LYS A 317 CD CE NZ
REMARK 470 GLN A 332 CG CD OE1 NE2
REMARK 470 ASP A 338 CG OD1 OD2
REMARK 470 TYR A 340 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 342 CB CG CD CE NZ
REMARK 470 SER A 344 OG
REMARK 470 LYS A 371 CD CE NZ
REMARK 470 ASP A 375 CG OD1 OD2
REMARK 470 PHE A 377 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 83 CB CG CD OE1 OE2
REMARK 470 LYS B 86 CD CE NZ
REMARK 470 ASP B 186 CG OD1 OD2
REMARK 470 PRO B 215 CG CD
REMARK 470 GLU B 231 CG CD OE1 OE2
REMARK 470 GLU B 247 CG CD OE1 OE2
REMARK 470 HIS B 250 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 251 CD CE NZ
REMARK 470 ASP B 255 CG OD1 OD2
REMARK 470 SER B 256 OG
REMARK 470 ASP B 257 CG OD1 OD2
REMARK 470 ARG B 302 CB CG CD NE CZ NH1 NH2
REMARK 470 THR B 304 OG1 CG2
REMARK 470 GLU B 306 CB CG CD OE1 OE2
REMARK 470 THR B 321 OG1 CG2
REMARK 470 ASP B 338 CB CG OD1 OD2
REMARK 470 LYS B 342 CG CD CE NZ
REMARK 470 LYS B 371 CG CD CE NZ
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 A 370 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 80 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 138 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH1 ANGL. DEV. = 3.3 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 ILE A 17 -76.34 -61.44
REMARK 500 LYS A 18 -26.50 -37.29
REMARK 500 THR A 39 54.38 -111.34
REMARK 500 GLU A 120 60.60 67.53
REMARK 500 ALA A 145 130.01 -36.83
REMARK 500 ASP A 167 2.75 -57.87
REMARK 500 ASN A 181 11.17 -64.02
REMARK 500 THR A 182 -34.50 -134.64
REMARK 500 VAL A 267 -66.15 -28.06
REMARK 500 GLN A 288 3.72 -62.76
REMARK 500 THR A 335 -74.72 -81.36
REMARK 500 ASP A 336 103.34 -47.04
REMARK 500 LYS B 27 1.57 -67.24
REMARK 500 SER B 130 107.47 -165.73
REMARK 500 LEU B 241 152.91 -44.47
REMARK 500 ASP B 283 11.23 -153.24
REMARK 500 ARG B 307 75.42 -117.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP B 58 10.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1O6C A 2 380 UNP P39131 MNAA_BACSU 2 380
DBREF 1O6C B 2 380 UNP P39131 MNAA_BACSU 2 380
SEQADV 1O6C MSE A 1 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C MSE A 7 UNP P39131 MET 7 MODIFIED RESIDUE
SEQADV 1O6C MSE A 19 UNP P39131 MET 19 MODIFIED RESIDUE
SEQADV 1O6C MSE A 45 UNP P39131 MET 45 MODIFIED RESIDUE
SEQADV 1O6C MSE A 64 UNP P39131 MET 64 MODIFIED RESIDUE
SEQADV 1O6C MSE A 140 UNP P39131 MET 140 MODIFIED RESIDUE
SEQADV 1O6C MSE A 201 UNP P39131 MET 201 MODIFIED RESIDUE
SEQADV 1O6C MSE A 216 UNP P39131 MET 216 MODIFIED RESIDUE
SEQADV 1O6C MSE A 219 UNP P39131 MET 219 MODIFIED RESIDUE
SEQADV 1O6C MSE A 343 UNP P39131 MET 343 MODIFIED RESIDUE
SEQADV 1O6C GLY A 381 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C SER A 382 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 383 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 384 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 385 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 386 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 387 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS A 388 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C MSE B 1 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C MSE B 7 UNP P39131 MET 7 MODIFIED RESIDUE
SEQADV 1O6C MSE B 19 UNP P39131 MET 19 MODIFIED RESIDUE
SEQADV 1O6C MSE B 45 UNP P39131 MET 45 MODIFIED RESIDUE
SEQADV 1O6C MSE B 64 UNP P39131 MET 64 MODIFIED RESIDUE
SEQADV 1O6C MSE B 140 UNP P39131 MET 140 MODIFIED RESIDUE
SEQADV 1O6C MSE B 201 UNP P39131 MET 201 MODIFIED RESIDUE
SEQADV 1O6C MSE B 216 UNP P39131 MET 216 MODIFIED RESIDUE
SEQADV 1O6C MSE B 219 UNP P39131 MET 219 MODIFIED RESIDUE
SEQADV 1O6C MSE B 343 UNP P39131 MET 343 MODIFIED RESIDUE
SEQADV 1O6C GLY B 381 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C SER B 382 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 383 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 384 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 385 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 386 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 387 UNP P39131 CLONING ARTIFACT
SEQADV 1O6C HIS B 388 UNP P39131 CLONING ARTIFACT
SEQRES 1 A 388 MSE LYS LYS LEU LYS VAL MSE THR VAL PHE GLY THR ARG
SEQRES 2 A 388 PRO GLU ALA ILE LYS MSE ALA PRO LEU VAL LEU GLU LEU
SEQRES 3 A 388 LYS LYS TYR PRO GLU ILE ASP SER TYR VAL THR VAL THR
SEQRES 4 A 388 ALA GLN HIS ARG GLN MSE LEU ASP GLN VAL LEU ASP ALA
SEQRES 5 A 388 PHE HIS ILE LYS PRO ASP PHE ASP LEU ASN ILE MSE LYS
SEQRES 6 A 388 GLU ARG GLN THR LEU ALA GLU ILE THR SER ASN ALA LEU
SEQRES 7 A 388 VAL ARG LEU ASP GLU LEU PHE LYS ASP ILE LYS PRO ASP
SEQRES 8 A 388 ILE VAL LEU VAL HIS GLY ASP THR THR THR THR PHE ALA
SEQRES 9 A 388 GLY SER LEU ALA ALA PHE TYR HIS GLN ILE ALA VAL GLY
SEQRES 10 A 388 HIS VAL GLU ALA GLY LEU ARG THR GLY ASN LYS TYR SER
SEQRES 11 A 388 PRO PHE PRO GLU GLU LEU ASN ARG GLN MSE THR GLY ALA
SEQRES 12 A 388 ILE ALA ASP LEU HIS PHE ALA PRO THR GLY GLN ALA LYS
SEQRES 13 A 388 ASP ASN LEU LEU LYS GLU ASN LYS LYS ALA ASP SER ILE
SEQRES 14 A 388 PHE VAL THR GLY ASN THR ALA ILE ASP ALA LEU ASN THR
SEQRES 15 A 388 THR VAL ARG ASP GLY TYR SER HIS PRO VAL LEU ASP GLN
SEQRES 16 A 388 VAL GLY GLU ASP LYS MSE ILE LEU LEU THR ALA HIS ARG
SEQRES 17 A 388 ARG GLU ASN LEU GLY GLU PRO MSE GLU ASN MSE PHE LYS
SEQRES 18 A 388 ALA ILE ARG ARG ILE VAL GLY GLU PHE GLU ASP VAL GLN
SEQRES 19 A 388 VAL VAL TYR PRO VAL HIS LEU ASN PRO VAL VAL ARG GLU
SEQRES 20 A 388 ALA ALA HIS LYS HIS PHE GLY ASP SER ASP ARG VAL HIS
SEQRES 21 A 388 LEU ILE GLU PRO LEU GLU VAL ILE ASP PHE HIS ASN PHE
SEQRES 22 A 388 ALA ALA LYS SER HIS PHE ILE LEU THR ASP SER GLY GLY
SEQRES 23 A 388 VAL GLN GLU GLU ALA PRO SER LEU GLY LYS PRO VAL LEU
SEQRES 24 A 388 VAL LEU ARG ASP THR THR GLU ARG PRO GLU GLY VAL GLU
SEQRES 25 A 388 ALA GLY THR LEU LYS LEU ALA GLY THR ASP GLU GLU ASN
SEQRES 26 A 388 ILE TYR GLN LEU ALA LYS GLN LEU LEU THR ASP PRO ASP
SEQRES 27 A 388 GLU TYR LYS LYS MSE SER GLN ALA SER ASN PRO TYR GLY
SEQRES 28 A 388 ASP GLY GLU ALA SER ARG ARG ILE VAL GLU GLU LEU LEU
SEQRES 29 A 388 PHE HIS TYR GLY TYR ARG LYS GLU GLN PRO ASP SER PHE
SEQRES 30 A 388 THR GLY LYS GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 388 MSE LYS LYS LEU LYS VAL MSE THR VAL PHE GLY THR ARG
SEQRES 2 B 388 PRO GLU ALA ILE LYS MSE ALA PRO LEU VAL LEU GLU LEU
SEQRES 3 B 388 LYS LYS TYR PRO GLU ILE ASP SER TYR VAL THR VAL THR
SEQRES 4 B 388 ALA GLN HIS ARG GLN MSE LEU ASP GLN VAL LEU ASP ALA
SEQRES 5 B 388 PHE HIS ILE LYS PRO ASP PHE ASP LEU ASN ILE MSE LYS
SEQRES 6 B 388 GLU ARG GLN THR LEU ALA GLU ILE THR SER ASN ALA LEU
SEQRES 7 B 388 VAL ARG LEU ASP GLU LEU PHE LYS ASP ILE LYS PRO ASP
SEQRES 8 B 388 ILE VAL LEU VAL HIS GLY ASP THR THR THR THR PHE ALA
SEQRES 9 B 388 GLY SER LEU ALA ALA PHE TYR HIS GLN ILE ALA VAL GLY
SEQRES 10 B 388 HIS VAL GLU ALA GLY LEU ARG THR GLY ASN LYS TYR SER
SEQRES 11 B 388 PRO PHE PRO GLU GLU LEU ASN ARG GLN MSE THR GLY ALA
SEQRES 12 B 388 ILE ALA ASP LEU HIS PHE ALA PRO THR GLY GLN ALA LYS
SEQRES 13 B 388 ASP ASN LEU LEU LYS GLU ASN LYS LYS ALA ASP SER ILE
SEQRES 14 B 388 PHE VAL THR GLY ASN THR ALA ILE ASP ALA LEU ASN THR
SEQRES 15 B 388 THR VAL ARG ASP GLY TYR SER HIS PRO VAL LEU ASP GLN
SEQRES 16 B 388 VAL GLY GLU ASP LYS MSE ILE LEU LEU THR ALA HIS ARG
SEQRES 17 B 388 ARG GLU ASN LEU GLY GLU PRO MSE GLU ASN MSE PHE LYS
SEQRES 18 B 388 ALA ILE ARG ARG ILE VAL GLY GLU PHE GLU ASP VAL GLN
SEQRES 19 B 388 VAL VAL TYR PRO VAL HIS LEU ASN PRO VAL VAL ARG GLU
SEQRES 20 B 388 ALA ALA HIS LYS HIS PHE GLY ASP SER ASP ARG VAL HIS
SEQRES 21 B 388 LEU ILE GLU PRO LEU GLU VAL ILE ASP PHE HIS ASN PHE
SEQRES 22 B 388 ALA ALA LYS SER HIS PHE ILE LEU THR ASP SER GLY GLY
SEQRES 23 B 388 VAL GLN GLU GLU ALA PRO SER LEU GLY LYS PRO VAL LEU
SEQRES 24 B 388 VAL LEU ARG ASP THR THR GLU ARG PRO GLU GLY VAL GLU
SEQRES 25 B 388 ALA GLY THR LEU LYS LEU ALA GLY THR ASP GLU GLU ASN
SEQRES 26 B 388 ILE TYR GLN LEU ALA LYS GLN LEU LEU THR ASP PRO ASP
SEQRES 27 B 388 GLU TYR LYS LYS MSE SER GLN ALA SER ASN PRO TYR GLY
SEQRES 28 B 388 ASP GLY GLU ALA SER ARG ARG ILE VAL GLU GLU LEU LEU
SEQRES 29 B 388 PHE HIS TYR GLY TYR ARG LYS GLU GLN PRO ASP SER PHE
SEQRES 30 B 388 THR GLY LYS GLY SER HIS HIS HIS HIS HIS HIS
MODRES 1O6C MSE A 7 MET SELENOMETHIONINE
MODRES 1O6C MSE A 19 MET SELENOMETHIONINE
MODRES 1O6C MSE A 45 MET SELENOMETHIONINE
MODRES 1O6C MSE A 64 MET SELENOMETHIONINE
MODRES 1O6C MSE A 140 MET SELENOMETHIONINE
MODRES 1O6C MSE A 201 MET SELENOMETHIONINE
MODRES 1O6C MSE A 216 MET SELENOMETHIONINE
MODRES 1O6C MSE A 219 MET SELENOMETHIONINE
MODRES 1O6C MSE A 343 MET SELENOMETHIONINE
MODRES 1O6C MSE B 1 MET SELENOMETHIONINE
MODRES 1O6C MSE B 7 MET SELENOMETHIONINE
MODRES 1O6C MSE B 19 MET SELENOMETHIONINE
MODRES 1O6C MSE B 45 MET SELENOMETHIONINE
MODRES 1O6C MSE B 64 MET SELENOMETHIONINE
MODRES 1O6C MSE B 140 MET SELENOMETHIONINE
MODRES 1O6C MSE B 201 MET SELENOMETHIONINE
MODRES 1O6C MSE B 216 MET SELENOMETHIONINE
MODRES 1O6C MSE B 219 MET SELENOMETHIONINE
MODRES 1O6C MSE B 343 MET SELENOMETHIONINE
HET MSE A 7 8
HET MSE A 19 8
HET MSE A 45 4
HET MSE A 64 8
HET MSE A 140 8
HET MSE A 201 8
HET MSE A 216 4
HET MSE A 219 4
HET MSE A 343 8
HET MSE B 1 8
HET MSE B 7 8
HET MSE B 19 8
HET MSE B 45 8
HET MSE B 64 8
HET MSE B 140 8
HET MSE B 201 8
HET MSE B 216 8
HET MSE B 219 8
HET MSE B 343 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 19(C5 H11 N O2 SE)
FORMUL 3 HOH *12(H2 O)
HELIX 1 1 THR A 12 LEU A 26 1 15
HELIX 2 2 LYS A 27 TYR A 29 5 3
HELIX 3 3 HIS A 42 MSE A 45 5 4
HELIX 4 4 LEU A 46 PHE A 53 1 8
HELIX 5 5 THR A 69 LYS A 89 1 21
HELIX 6 6 THR A 99 HIS A 112 1 14
HELIX 7 7 PRO A 133 ALA A 145 1 13
HELIX 8 8 THR A 152 GLU A 162 1 11
HELIX 9 9 LYS A 165 ASP A 167 5 3
HELIX 10 10 ASN A 174 VAL A 184 1 11
HELIX 11 11 MSE A 216 PHE A 230 1 15
HELIX 12 12 PRO A 243 HIS A 252 1 10
HELIX 13 13 GLU A 266 SER A 277 1 12
HELIX 14 14 GLY A 286 ALA A 291 1 6
HELIX 15 15 PRO A 292 GLY A 295 5 4
HELIX 16 16 ASP A 322 ASP A 336 1 15
HELIX 17 17 ASP A 336 ALA A 346 1 11
HELIX 18 18 GLU A 354 TYR A 367 1 14
HELIX 19 19 THR B 12 LYS B 27 1 16
HELIX 20 20 HIS B 42 MSE B 45 5 4
HELIX 21 21 LEU B 46 PHE B 53 1 8
HELIX 22 22 THR B 69 LYS B 89 1 21
HELIX 23 23 THR B 99 HIS B 112 1 14
HELIX 24 24 PRO B 133 ALA B 145 1 13
HELIX 25 25 THR B 152 LYS B 161 1 10
HELIX 26 26 LYS B 165 ASP B 167 5 3
HELIX 27 27 ASN B 174 VAL B 184 1 11
HELIX 28 28 HIS B 190 GLY B 197 1 8
HELIX 29 29 PRO B 215 PHE B 230 1 16
HELIX 30 30 ASN B 242 PHE B 253 1 12
HELIX 31 31 GLU B 266 SER B 277 1 12
HELIX 32 32 SER B 284 ALA B 291 1 8
HELIX 33 33 PRO B 292 GLY B 295 5 4
HELIX 34 34 ARG B 307 ALA B 313 1 7
HELIX 35 35 ASP B 322 ASP B 336 1 15
HELIX 36 36 ASP B 336 GLN B 345 1 10
HELIX 37 37 GLU B 354 TYR B 367 1 14
SHEET 1 A 7 PHE A 59 ASP A 60 0
SHEET 2 A 7 ILE A 32 VAL A 38 1 N VAL A 38 O PHE A 59
SHEET 3 A 7 LEU A 4 PHE A 10 1 N PHE A 10 O THR A 37
SHEET 4 A 7 ILE A 92 HIS A 96 1 O LEU A 94 N MSE A 7
SHEET 5 A 7 ALA A 115 VAL A 119 1 O ALA A 115 N VAL A 93
SHEET 6 A 7 LEU A 147 ALA A 150 1 O LEU A 147 N HIS A 118
SHEET 7 A 7 ILE A 169 VAL A 171 1 O PHE A 170 N HIS A 148
SHEET 1 B 6 VAL A 259 LEU A 261 0
SHEET 2 B 6 VAL A 233 TYR A 237 1 N TYR A 237 O HIS A 260
SHEET 3 B 6 LYS A 200 LEU A 204 1 N ILE A 202 O GLN A 234
SHEET 4 B 6 PHE A 279 THR A 282 1 O LEU A 281 N LEU A 203
SHEET 5 B 6 VAL A 298 LEU A 301 1 O LEU A 301 N THR A 282
SHEET 6 B 6 LYS A 317 ALA A 319 1 O ALA A 319 N VAL A 300
SHEET 1 C 7 PHE B 59 ASP B 60 0
SHEET 2 C 7 ILE B 32 VAL B 38 1 N VAL B 38 O PHE B 59
SHEET 3 C 7 LEU B 4 PHE B 10 1 N VAL B 6 O TYR B 35
SHEET 4 C 7 ILE B 92 HIS B 96 1 O LEU B 94 N MSE B 7
SHEET 5 C 7 ALA B 115 VAL B 119 1 O VAL B 119 N VAL B 95
SHEET 6 C 7 LEU B 147 ALA B 150 1 O LEU B 147 N HIS B 118
SHEET 7 C 7 ILE B 169 VAL B 171 1 O PHE B 170 N ALA B 150
SHEET 1 D 6 VAL B 259 ILE B 262 0
SHEET 2 D 6 VAL B 233 PRO B 238 1 N TYR B 237 O HIS B 260
SHEET 3 D 6 LYS B 200 LEU B 204 1 N ILE B 202 O GLN B 234
SHEET 4 D 6 PHE B 279 THR B 282 1 O LEU B 281 N LEU B 203
SHEET 5 D 6 VAL B 298 VAL B 300 1 O LEU B 299 N ILE B 280
SHEET 6 D 6 LEU B 316 LEU B 318 1 O LYS B 317 N VAL B 300
LINK C VAL A 6 N MSE A 7 1555 1555 1.33
LINK C MSE A 7 N THR A 8 1555 1555 1.32
LINK C LYS A 18 N MSE A 19 1555 1555 1.30
LINK C MSE A 19 N ALA A 20 1555 1555 1.34
LINK C GLN A 44 N MSE A 45 1555 1555 1.33
LINK C MSE A 45 N LEU A 46 1555 1555 1.33
LINK C ILE A 63 N MSE A 64 1555 1555 1.32
LINK C MSE A 64 N LYS A 65 1555 1555 1.33
LINK C GLN A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N THR A 141 1555 1555 1.33
LINK C LYS A 200 N MSE A 201 1555 1555 1.33
LINK C MSE A 201 N ILE A 202 1555 1555 1.32
LINK C MSE A 216 N GLU A 217 1555 1555 1.33
LINK C ASN A 218 N MSE A 219 1555 1555 1.33
LINK C MSE A 219 N PHE A 220 1555 1555 1.33
LINK C LYS A 342 N MSE A 343 1555 1555 1.33
LINK C MSE A 343 N SER A 344 1555 1555 1.32
LINK C MSE B 1 N LYS B 2 1555 1555 1.34
LINK C VAL B 6 N MSE B 7 1555 1555 1.33
LINK C MSE B 7 N THR B 8 1555 1555 1.32
LINK C LYS B 18 N MSE B 19 1555 1555 1.30
LINK C MSE B 19 N ALA B 20 1555 1555 1.33
LINK C GLN B 44 N MSE B 45 1555 1555 1.33
LINK C MSE B 45 N LEU B 46 1555 1555 1.33
LINK C ILE B 63 N MSE B 64 1555 1555 1.34
LINK C MSE B 64 N LYS B 65 1555 1555 1.33
LINK C GLN B 139 N MSE B 140 1555 1555 1.33
LINK C MSE B 140 N THR B 141 1555 1555 1.33
LINK C LYS B 200 N MSE B 201 1555 1555 1.35
LINK C MSE B 201 N ILE B 202 1555 1555 1.33
LINK C PRO B 215 N MSE B 216 1555 1555 1.34
LINK C MSE B 216 N GLU B 217 1555 1555 1.33
LINK C ASN B 218 N MSE B 219 1555 1555 1.32
LINK C MSE B 219 N PHE B 220 1555 1555 1.32
LINK C LYS B 342 N MSE B 343 1555 1555 1.33
LINK C MSE B 343 N SER B 344 1555 1555 1.32
CISPEP 1 SER A 130 PRO A 131 0 -1.24
CISPEP 2 PHE A 132 PRO A 133 0 -0.66
CISPEP 3 SER B 130 PRO B 131 0 -2.56
CISPEP 4 PHE B 132 PRO B 133 0 1.71
CRYST1 63.820 63.820 452.430 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 0.015669 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002210 0.00000
(ATOM LINES ARE NOT SHOWN.)
END