HEADER HYDROLASE 05-DEC-01 1ISJ
TITLE CRYSTAL STRUCTURE ANALYSIS OF BST-1/CD157 COMPLEXED WITH NMN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BONE MARROW STROMAL CELL ANTIGEN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR REGION;
COMPND 5 SYNONYM: BST-1/CD157, ADP-RIBOSYL CYCLASE 2;
COMPND 6 EC: 3.2.2.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: AUTOGRAPHA CALIFORNICA NUCLEAR
SOURCE 11 POLYHEDROSIS VIRUS
KEYWDS ADP RIBOSYL CYCLASE, NAD GLYCOHYDROLASE, CNS, NMN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YAMAMOTO-KATAYAMA,M.ARIYOSHI,K.ISHIHARA,T.HIRANO,H.JINGAMI,
AUTHOR 2 K.MORIKAWA
REVDAT 4 13-JUL-11 1ISJ 1 VERSN
REVDAT 3 24-FEB-09 1ISJ 1 VERSN
REVDAT 2 07-JAN-03 1ISJ 1 REMARK
REVDAT 1 13-MAR-02 1ISJ 0
JRNL AUTH S.YAMAMOTO-KATAYAMA,M.ARIYOSHI,K.ISHIHARA,T.HIRANO,
JRNL AUTH 2 H.JINGAMI,K.MORIKAWA
JRNL TITL CRYSTALLOGRAPHIC STUDIES ON HUMAN BST-1/CD157 WITH
JRNL TITL 2 ADP-RIBOSYL CYCLASE AND NAD GLYCOHYDROLASE ACTIVITIES.
JRNL REF J.MOL.BIOL. V. 316 711 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11866528
JRNL DOI 10.1006/JMBI.2001.5386
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.YAMAMOTO-KATAYAMA,A.SATO,M.ARIYOSHI,M.SUYAMA,K.ISHIHARA,
REMARK 1 AUTH 2 T.HIRANO,H.NAKAMURA,K.MORIKAWA,H.JINGAMI
REMARK 1 TITL SITE-DIRECTED REMOVAL OF N-GLYCOSYLATION SITES IN
REMARK 1 TITL 2 BST-1/CD157: EFFECTS ON MOLECULAR AND FUNCTIONAL
REMARK 1 TITL 3 HETEROGENEITY.
REMARK 1 REF BIOCHEM.J. V. 357 385 2001
REMARK 1 REFN ISSN 0264-6021
REMARK 1 DOI 10.1042/0264-6021:3570385
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1756706.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 38835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2949
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5847
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 480
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 20.86000
REMARK 3 B22 (A**2) : -11.14000
REMARK 3 B33 (A**2) : -9.72000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.73
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.710 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.580 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 37.35
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NMN.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NMN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ISJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB005236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL24XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.836
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38880
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 27.700
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 33.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMMONIUM SULFATE, CITRATE, NMN, PH
REMARK 280 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.40200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.94050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.94050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.40200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.29500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 5090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 ARG A 1
REMARK 465 SER A 252
REMARK 465 ALA A 253
REMARK 465 ALA A 254
REMARK 465 ALA A 255
REMARK 465 ALA A 256
REMARK 465 THR A 257
REMARK 465 GLN A 258
REMARK 465 ARG A 259
REMARK 465 LYS A 260
REMARK 465 ALA A 261
REMARK 465 PRO A 262
REMARK 465 SER A 263
REMARK 465 LEU A 264
REMARK 465 TYR A 265
REMARK 465 ARG B 1
REMARK 465 SER B 252
REMARK 465 ALA B 253
REMARK 465 ALA B 254
REMARK 465 ALA B 255
REMARK 465 ALA B 256
REMARK 465 THR B 257
REMARK 465 GLN B 258
REMARK 465 ARG B 259
REMARK 465 LYS B 260
REMARK 465 ALA B 261
REMARK 465 PRO B 262
REMARK 465 SER B 263
REMARK 465 LEU B 264
REMARK 465 TYR B 265
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 LYS A 43 1.76 -66.32
REMARK 500 PRO A 50 2.59 -54.94
REMARK 500 SER A 80 39.38 -159.58
REMARK 500 THR A 91 -10.12 83.81
REMARK 500 PHE A 108 -1.46 69.45
REMARK 500 CYS A 112 148.42 177.66
REMARK 500 ASN A 133 54.56 -91.85
REMARK 500 HIS A 242 48.29 -143.37
REMARK 500 ASP B 47 31.22 -77.50
REMARK 500 PRO B 50 -7.60 -53.60
REMARK 500 SER B 80 40.34 -154.61
REMARK 500 THR B 91 -2.22 80.01
REMARK 500 PHE B 108 -9.82 68.28
REMARK 500 CYS B 112 151.29 179.72
REMARK 500 ALA B 116 -76.17 -103.67
REMARK 500 TYR B 231 121.00 -39.78
REMARK 500 HIS B 242 48.78 -149.70
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 NAG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NMN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NMN B 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ISF RELATED DB: PDB
REMARK 900 1ISF CONTAINS THE SAME PROTEIN (LIGAND FREE FORM).
REMARK 900 RELATED ID: 1ISG RELATED DB: PDB
REMARK 900 1ISG CONTAINS THE SAME PROTEIN COMPLEXED WITH ATPGAMMAS.
REMARK 900 RELATED ID: 1ISH RELATED DB: PDB
REMARK 900 1ISH CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHENONADP.
REMARK 900 RELATED ID: 1ISI RELATED DB: PDB
REMARK 900 1ISI CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHENONAD.
REMARK 900 RELATED ID: 1ISM RELATED DB: PDB
REMARK 900 1ISM CONTAINS THE SAME PROTEIN COMPLEXED WITH NICOTINAMIDE.
DBREF 1ISJ A 1 265 UNP Q10588 BST1_HUMAN 33 297
DBREF 1ISJ B 1 265 UNP Q10588 BST1_HUMAN 33 297
SEQADV 1ISJ ASP A 34 UNP Q10588 ASN 66 ENGINEERED
SEQADV 1ISJ THR A 63 UNP Q10588 ASN 95 ENGINEERED
SEQADV 1ISJ ALA A 116 UNP Q10588 ASN 148 ENGINEERED
SEQADV 1ISJ ASP B 34 UNP Q10588 ASN 66 ENGINEERED
SEQADV 1ISJ THR B 63 UNP Q10588 ASN 95 ENGINEERED
SEQADV 1ISJ ALA B 116 UNP Q10588 ASN 148 ENGINEERED
SEQRES 1 A 265 ARG TRP ARG ALA GLU GLY THR SER ALA HIS LEU ARG ASP
SEQRES 2 A 265 ILE PHE LEU GLY ARG CYS ALA GLU TYR ARG ALA LEU LEU
SEQRES 3 A 265 SER PRO GLU GLN ARG ASN LYS ASP CYS THR ALA ILE TRP
SEQRES 4 A 265 GLU ALA PHE LYS VAL ALA LEU ASP LYS ASP PRO CYS SER
SEQRES 5 A 265 VAL LEU PRO SER ASP TYR ASP LEU PHE ILE THR LEU SER
SEQRES 6 A 265 ARG HIS SER ILE PRO ARG ASP LYS SER LEU PHE TRP GLU
SEQRES 7 A 265 ASN SER HIS LEU LEU VAL ASN SER PHE ALA ASP ASN THR
SEQRES 8 A 265 ARG ARG PHE MET PRO LEU SER ASP VAL LEU TYR GLY ARG
SEQRES 9 A 265 VAL ALA ASP PHE LEU SER TRP CYS ARG GLN LYS ALA ASP
SEQRES 10 A 265 SER GLY LEU ASP TYR GLN SER CYS PRO THR SER GLU ASP
SEQRES 11 A 265 CYS GLU ASN ASN PRO VAL ASP SER PHE TRP LYS ARG ALA
SEQRES 12 A 265 SER ILE GLN TYR SER LYS ASP SER SER GLY VAL ILE HIS
SEQRES 13 A 265 VAL MET LEU ASN GLY SER GLU PRO THR GLY ALA TYR PRO
SEQRES 14 A 265 ILE LYS GLY PHE PHE ALA ASP TYR GLU ILE PRO ASN LEU
SEQRES 15 A 265 GLN LYS GLU LYS ILE THR ARG ILE GLU ILE TRP VAL MET
SEQRES 16 A 265 HIS GLU ILE GLY GLY PRO ASN VAL GLU SER CYS GLY GLU
SEQRES 17 A 265 GLY SER MET LYS VAL LEU GLU LYS ARG LEU LYS ASP MET
SEQRES 18 A 265 GLY PHE GLN TYR SER CYS ILE ASN ASP TYR ARG PRO VAL
SEQRES 19 A 265 LYS LEU LEU GLN CYS VAL ASP HIS SER THR HIS PRO ASP
SEQRES 20 A 265 CYS ALA LEU LYS SER ALA ALA ALA ALA THR GLN ARG LYS
SEQRES 21 A 265 ALA PRO SER LEU TYR
SEQRES 1 B 265 ARG TRP ARG ALA GLU GLY THR SER ALA HIS LEU ARG ASP
SEQRES 2 B 265 ILE PHE LEU GLY ARG CYS ALA GLU TYR ARG ALA LEU LEU
SEQRES 3 B 265 SER PRO GLU GLN ARG ASN LYS ASP CYS THR ALA ILE TRP
SEQRES 4 B 265 GLU ALA PHE LYS VAL ALA LEU ASP LYS ASP PRO CYS SER
SEQRES 5 B 265 VAL LEU PRO SER ASP TYR ASP LEU PHE ILE THR LEU SER
SEQRES 6 B 265 ARG HIS SER ILE PRO ARG ASP LYS SER LEU PHE TRP GLU
SEQRES 7 B 265 ASN SER HIS LEU LEU VAL ASN SER PHE ALA ASP ASN THR
SEQRES 8 B 265 ARG ARG PHE MET PRO LEU SER ASP VAL LEU TYR GLY ARG
SEQRES 9 B 265 VAL ALA ASP PHE LEU SER TRP CYS ARG GLN LYS ALA ASP
SEQRES 10 B 265 SER GLY LEU ASP TYR GLN SER CYS PRO THR SER GLU ASP
SEQRES 11 B 265 CYS GLU ASN ASN PRO VAL ASP SER PHE TRP LYS ARG ALA
SEQRES 12 B 265 SER ILE GLN TYR SER LYS ASP SER SER GLY VAL ILE HIS
SEQRES 13 B 265 VAL MET LEU ASN GLY SER GLU PRO THR GLY ALA TYR PRO
SEQRES 14 B 265 ILE LYS GLY PHE PHE ALA ASP TYR GLU ILE PRO ASN LEU
SEQRES 15 B 265 GLN LYS GLU LYS ILE THR ARG ILE GLU ILE TRP VAL MET
SEQRES 16 B 265 HIS GLU ILE GLY GLY PRO ASN VAL GLU SER CYS GLY GLU
SEQRES 17 B 265 GLY SER MET LYS VAL LEU GLU LYS ARG LEU LYS ASP MET
SEQRES 18 B 265 GLY PHE GLN TYR SER CYS ILE ASN ASP TYR ARG PRO VAL
SEQRES 19 B 265 LYS LEU LEU GLN CYS VAL ASP HIS SER THR HIS PRO ASP
SEQRES 20 B 265 CYS ALA LEU LYS SER ALA ALA ALA ALA THR GLN ARG LYS
SEQRES 21 B 265 ALA PRO SER LEU TYR
MODRES 1ISJ ASN A 160 ASN GLYCOSYLATION SITE
MODRES 1ISJ ASN B 160 ASN GLYCOSYLATION SITE
HET NAG A 301 14
HET NAG A 302 14
HET NAG B 303 14
HET NAG B 304 14
HET NMN A1001 22
HET NMN B1002 22
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NMN BETA-NICOTINAMIDE RIBOSE MONOPHOSPHATE
HETSYN NMN NICOTINAMIDE MONONUCLEOTIDE
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 NMN 2(C11 H16 N2 O8 P 1+)
FORMUL 7 HOH *206(H2 O)
HELIX 1 1 HIS A 10 ALA A 24 1 15
HELIX 2 2 ASP A 34 LYS A 43 1 10
HELIX 3 3 VAL A 44 LYS A 48 5 5
HELIX 4 4 LEU A 54 ASP A 57 5 4
HELIX 5 5 TYR A 58 ARG A 66 1 9
HELIX 6 6 SER A 80 ASP A 89 1 10
HELIX 7 7 PRO A 96 ASP A 99 5 4
HELIX 8 8 VAL A 100 VAL A 105 1 6
HELIX 9 9 ASN A 134 ASP A 150 1 17
HELIX 10 10 GLY A 172 TYR A 177 1 6
HELIX 11 11 GLU A 178 LEU A 182 5 5
HELIX 12 12 GLN A 183 GLU A 185 5 3
HELIX 13 13 GLY A 209 MET A 221 1 13
HELIX 14 14 TYR A 231 VAL A 240 1 10
HELIX 15 15 HIS A 245 ALA A 249 5 5
HELIX 16 16 HIS B 10 ALA B 24 1 15
HELIX 17 17 ASP B 34 ASP B 47 1 14
HELIX 18 18 LEU B 54 ASP B 57 5 4
HELIX 19 19 TYR B 58 ARG B 66 1 9
HELIX 20 20 SER B 80 ASP B 89 1 10
HELIX 21 21 PRO B 96 ASP B 99 5 4
HELIX 22 22 VAL B 100 VAL B 105 1 6
HELIX 23 23 ASN B 134 ASP B 150 1 17
HELIX 24 24 GLY B 172 GLU B 178 1 7
HELIX 25 25 ILE B 179 LEU B 182 5 4
HELIX 26 26 GLN B 183 GLU B 185 5 3
HELIX 27 27 GLY B 209 MET B 221 1 13
HELIX 28 28 TYR B 231 VAL B 240 1 10
HELIX 29 29 HIS B 245 ALA B 249 5 5
SHEET 1 A 4 LEU A 75 GLU A 78 0
SHEET 2 A 4 GLY A 153 ASN A 160 1 O HIS A 156 N PHE A 76
SHEET 3 A 4 ILE A 187 MET A 195 1 O TRP A 193 N LEU A 159
SHEET 4 A 4 TYR A 225 ASN A 229 1 O SER A 226 N ILE A 192
SHEET 1 B 2 ALA B 4 GLU B 5 0
SHEET 2 B 2 SER B 124 CYS B 125 -1 O CYS B 125 N ALA B 4
SHEET 1 C 4 LEU B 75 GLU B 78 0
SHEET 2 C 4 GLY B 153 ASN B 160 1 O HIS B 156 N PHE B 76
SHEET 3 C 4 ILE B 187 MET B 195 1 O TRP B 193 N VAL B 157
SHEET 4 C 4 TYR B 225 ASN B 229 1 O ILE B 228 N ILE B 192
SSBOND 1 CYS A 19 CYS A 35 1555 1555 2.05
SSBOND 2 CYS A 51 CYS A 131 1555 1555 2.04
SSBOND 3 CYS A 112 CYS A 125 1555 1555 2.05
SSBOND 4 CYS A 206 CYS A 227 1555 1555 2.04
SSBOND 5 CYS A 239 CYS A 248 1555 1555 2.03
SSBOND 6 CYS B 19 CYS B 35 1555 1555 2.05
SSBOND 7 CYS B 51 CYS B 131 1555 1555 2.04
SSBOND 8 CYS B 112 CYS B 125 1555 1555 2.04
SSBOND 9 CYS B 206 CYS B 227 1555 1555 2.04
SSBOND 10 CYS B 239 CYS B 248 1555 1555 2.03
LINK ND2 ASN A 160 C1 NAG A 301 1555 1555 1.45
LINK ND2 ASN B 160 C1 NAG B 303 1555 1555 1.45
LINK O4 NAG A 301 C1 NAG A 302 1555 1555 1.39
LINK O4 NAG B 303 C1 NAG B 304 1555 1555 1.39
SITE 1 AC1 11 ASN A 79 SER A 80 LEU A 83 ASN A 160
SITE 2 AC1 11 SER A 162 GLU A 163 PRO A 164 GLU A 197
SITE 3 AC1 11 NAG A 302 HOH A1036 HOH A1098
SITE 1 AC2 2 PRO A 201 NAG A 301
SITE 1 AC3 8 ASN B 79 SER B 80 LEU B 83 ASN B 160
SITE 2 AC3 8 SER B 162 GLU B 197 NAG B 304 HOH B1023
SITE 1 AC4 1 NAG B 303
SITE 1 AC5 15 PHE A 76 TRP A 77 GLU A 78 HIS A 81
SITE 2 AC5 15 LEU A 97 SER A 98 ASP A 107 TRP A 140
SITE 3 AC5 15 PHE A 173 GLU A 178 HOH A1002 HOH A1058
SITE 4 AC5 15 HOH A1064 HOH A1106 HOH A1109
SITE 1 AC6 15 PHE B 76 TRP B 77 GLU B 78 HIS B 81
SITE 2 AC6 15 LEU B 97 ASP B 107 TRP B 140 SER B 144
SITE 3 AC6 15 PHE B 173 GLU B 178 HOH B1037 HOH B1040
SITE 4 AC6 15 HOH B1046 HOH B1099 HOH B1100
CRYST1 58.804 112.590 129.881 90.00 90.00 90.00 P 21 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 0.017006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008882 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007699 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
