HEADER HYDROLASE 28-AUG-06 2I65
TITLE STRUCTURAL BASIS FOR THE MECHANISTIC UNDERSTANDING HUMAN
TITLE 2 CD38 CONTROLLED MULTIPLE CATALYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYCLIC ADP-RIBOSE HYDROLASE 1, CADPR HYDROLASE 1,
COMPND 5 LYMPHOCYTE DIFFERENTIATION ANTIGEN CD38, T10, ACUTE
COMPND 6 LYMPHOBLASTIC LEUKEMIA CELLS ANTIGEN CD38;
COMPND 7 EC: 3.2.2.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD38;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZAA
KEYWDS THE CATALYTIC POCKET, REACTION PRODUCT, REACTION
KEYWDS 2 INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.LIU,I.A.KRIKSUNOV,R.GRAEFF,C.MUNSHI,H.C.LEE,Q.HAO
REVDAT 3 24-FEB-09 2I65 1 VERSN
REVDAT 2 21-NOV-06 2I65 1 JRNL
REVDAT 1 05-SEP-06 2I65 0
JRNL AUTH Q.LIU,I.A.KRIKSUNOV,R.GRAEFF,C.MUNSHI,H.C.LEE,Q.HAO
JRNL TITL STRUCTURAL BASIS FOR THE MECHANISTIC UNDERSTANDING
JRNL TITL 2 OF HUMAN CD38-CONTROLLED MULTIPLE CATALYSIS.
JRNL REF J.BIOL.CHEM. V. 281 32861 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16951430
JRNL DOI 10.1074/JBC.M606365200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35626
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 + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1872
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2122
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 119
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.54000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : 1.28000
REMARK 3 B12 (A**2) : 0.85000
REMARK 3 B13 (A**2) : 0.92000
REMARK 3 B23 (A**2) : 1.13000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.185
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.923
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.009 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.246 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 6.064 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ;38.753 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;14.912 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ;16.161 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.085 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.004 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; 0.212 ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; 0.311 ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; 0.158 ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; 0.192 ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; 0.148 ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; 0.737 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 1.214 ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 1.772 ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 2.886 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2I65 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-06.
REMARK 100 THE RCSB ID CODE IS RCSB039185.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37732
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1YH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 10% PEG 4000, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: THERE ARE TWO BIOLOGICAL UNITS IN THE CRYSTALLOGRAPHIC
REMARK 300 ASYMMETRIC UNIT
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 LYS A 39
REMARK 465 ARG A 40
REMARK 465 GLU A 41
REMARK 465 ALA A 42
REMARK 465 GLU A 43
REMARK 465 ALA A 44
REMARK 465 ARG A 45
REMARK 465 TRP A 46
REMARK 465 ARG A 47
REMARK 465 THR A 297
REMARK 465 SER A 298
REMARK 465 GLU A 299
REMARK 465 ILE A 300
REMARK 465 LYS B 39
REMARK 465 ARG B 40
REMARK 465 GLU B 41
REMARK 465 ALA B 42
REMARK 465 GLU B 43
REMARK 465 ALA B 44
REMARK 465 THR B 297
REMARK 465 SER B 298
REMARK 465 GLU B 299
REMARK 465 ILE B 300
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 128 46.69 -142.52
REMARK 500 ASP A 179 -73.99 -122.88
REMARK 500 ASP A 202 -123.59 60.38
REMARK 500 SER A 213 -18.89 81.77
REMARK 500 GLU A 248 -167.78 49.91
REMARK 500 SER A 295 -16.18 98.43
REMARK 500 ILE B 128 57.89 -144.86
REMARK 500 ASP B 179 -73.46 -107.09
REMARK 500 ASN B 182 56.57 -96.52
REMARK 500 ASP B 202 -116.08 56.78
REMARK 500 LYS B 214 68.15 107.59
REMARK 500 ARG B 247 39.12 -78.67
REMARK 500 GLU B 248 114.74 78.30
REMARK 500 ASP B 249 -77.34 -122.41
REMARK 500 SER B 250 -149.66 -111.91
REMARK 500 ARG B 251 -151.33 -121.29
REMARK 500 SER B 294 -19.79 89.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 249 SER B 250 -143.61
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 NAD A 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2I66 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE MECHANISTIC UNDERSTANDING HUMAN
REMARK 900 CD38 CONTROLLED MULTIPLE CATALYSIS
REMARK 900 RELATED ID: 2I67 RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE MECHANISTIC UNDERSTANDING HUMAN
REMARK 900 CD38 CONTROLLED MULTIPLE CATALYSIS
DBREF 2I65 A 45 300 UNP P28907 CD38_HUMAN 45 300
DBREF 2I65 B 45 300 UNP P28907 CD38_HUMAN 45 300
SEQADV 2I65 LYS A 39 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ARG A 40 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 GLU A 41 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ALA A 42 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 GLU A 43 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ALA A 44 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 THR A 49 UNP P28907 GLN 49 ENGINEERED
SEQADV 2I65 ASP A 100 UNP P28907 ASN 100 ENGINEERED
SEQADV 2I65 ASP A 164 UNP P28907 ASN 164 ENGINEERED
SEQADV 2I65 ASP A 209 UNP P28907 ASN 209 ENGINEERED
SEQADV 2I65 ASP A 219 UNP P28907 ASN 219 ENGINEERED
SEQADV 2I65 GLN A 226 UNP P28907 GLU 226 ENGINEERED
SEQADV 2I65 LYS B 39 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ARG B 40 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 GLU B 41 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ALA B 42 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 GLU B 43 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 ALA B 44 UNP P28907 CLONING ARTIFACT
SEQADV 2I65 THR B 49 UNP P28907 GLN 49 ENGINEERED
SEQADV 2I65 ASP B 100 UNP P28907 ASN 100 ENGINEERED
SEQADV 2I65 ASP B 164 UNP P28907 ASN 164 ENGINEERED
SEQADV 2I65 ASP B 209 UNP P28907 ASN 209 ENGINEERED
SEQADV 2I65 ASP B 219 UNP P28907 ASN 219 ENGINEERED
SEQADV 2I65 GLN B 226 UNP P28907 GLU 226 ENGINEERED
SEQRES 1 A 262 LYS ARG GLU ALA GLU ALA ARG TRP ARG GLN THR TRP SER
SEQRES 2 A 262 GLY PRO GLY THR THR LYS ARG PHE PRO GLU THR VAL LEU
SEQRES 3 A 262 ALA ARG CYS VAL LYS TYR THR GLU ILE HIS PRO GLU MET
SEQRES 4 A 262 ARG HIS VAL ASP CYS GLN SER VAL TRP ASP ALA PHE LYS
SEQRES 5 A 262 GLY ALA PHE ILE SER LYS HIS PRO CYS ASP ILE THR GLU
SEQRES 6 A 262 GLU ASP TYR GLN PRO LEU MET LYS LEU GLY THR GLN THR
SEQRES 7 A 262 VAL PRO CYS ASN LYS ILE LEU LEU TRP SER ARG ILE LYS
SEQRES 8 A 262 ASP LEU ALA HIS GLN PHE THR GLN VAL GLN ARG ASP MET
SEQRES 9 A 262 PHE THR LEU GLU ASP THR LEU LEU GLY TYR LEU ALA ASP
SEQRES 10 A 262 ASP LEU THR TRP CYS GLY GLU PHE ASP THR SER LYS ILE
SEQRES 11 A 262 ASN TYR GLN SER CYS PRO ASP TRP ARG LYS ASP CYS SER
SEQRES 12 A 262 ASN ASN PRO VAL SER VAL PHE TRP LYS THR VAL SER ARG
SEQRES 13 A 262 ARG PHE ALA GLU ALA ALA CYS ASP VAL VAL HIS VAL MET
SEQRES 14 A 262 LEU ASP GLY SER ARG SER LYS ILE PHE ASP LYS ASP SER
SEQRES 15 A 262 THR PHE GLY SER VAL GLN VAL HIS ASN LEU GLN PRO GLU
SEQRES 16 A 262 LYS VAL GLN THR LEU GLU ALA TRP VAL ILE HIS GLY GLY
SEQRES 17 A 262 ARG GLU ASP SER ARG ASP LEU CYS GLN ASP PRO THR ILE
SEQRES 18 A 262 LYS GLU LEU GLU SER ILE ILE SER LYS ARG ASN ILE GLN
SEQRES 19 A 262 PHE SER CYS LYS ASN ILE TYR ARG PRO ASP LYS PHE LEU
SEQRES 20 A 262 GLN CYS VAL LYS ASN PRO GLU ASP SER SER CYS THR SER
SEQRES 21 A 262 GLU ILE
SEQRES 1 B 262 LYS ARG GLU ALA GLU ALA ARG TRP ARG GLN THR TRP SER
SEQRES 2 B 262 GLY PRO GLY THR THR LYS ARG PHE PRO GLU THR VAL LEU
SEQRES 3 B 262 ALA ARG CYS VAL LYS TYR THR GLU ILE HIS PRO GLU MET
SEQRES 4 B 262 ARG HIS VAL ASP CYS GLN SER VAL TRP ASP ALA PHE LYS
SEQRES 5 B 262 GLY ALA PHE ILE SER LYS HIS PRO CYS ASP ILE THR GLU
SEQRES 6 B 262 GLU ASP TYR GLN PRO LEU MET LYS LEU GLY THR GLN THR
SEQRES 7 B 262 VAL PRO CYS ASN LYS ILE LEU LEU TRP SER ARG ILE LYS
SEQRES 8 B 262 ASP LEU ALA HIS GLN PHE THR GLN VAL GLN ARG ASP MET
SEQRES 9 B 262 PHE THR LEU GLU ASP THR LEU LEU GLY TYR LEU ALA ASP
SEQRES 10 B 262 ASP LEU THR TRP CYS GLY GLU PHE ASP THR SER LYS ILE
SEQRES 11 B 262 ASN TYR GLN SER CYS PRO ASP TRP ARG LYS ASP CYS SER
SEQRES 12 B 262 ASN ASN PRO VAL SER VAL PHE TRP LYS THR VAL SER ARG
SEQRES 13 B 262 ARG PHE ALA GLU ALA ALA CYS ASP VAL VAL HIS VAL MET
SEQRES 14 B 262 LEU ASP GLY SER ARG SER LYS ILE PHE ASP LYS ASP SER
SEQRES 15 B 262 THR PHE GLY SER VAL GLN VAL HIS ASN LEU GLN PRO GLU
SEQRES 16 B 262 LYS VAL GLN THR LEU GLU ALA TRP VAL ILE HIS GLY GLY
SEQRES 17 B 262 ARG GLU ASP SER ARG ASP LEU CYS GLN ASP PRO THR ILE
SEQRES 18 B 262 LYS GLU LEU GLU SER ILE ILE SER LYS ARG ASN ILE GLN
SEQRES 19 B 262 PHE SER CYS LYS ASN ILE TYR ARG PRO ASP LYS PHE LEU
SEQRES 20 B 262 GLN CYS VAL LYS ASN PRO GLU ASP SER SER CYS THR SER
SEQRES 21 B 262 GLU ILE
HET NAD A 301 44
HET NAD B 301 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 5 HOH *215(H2 O)
HELIX 1 1 ARG A 58 HIS A 74 1 17
HELIX 2 2 PRO A 75 ARG A 78 5 4
HELIX 3 3 ASP A 81 ALA A 92 1 12
HELIX 4 4 THR A 102 ASP A 105 5 4
HELIX 5 5 TYR A 106 GLY A 113 1 8
HELIX 6 6 ILE A 128 GLN A 139 1 12
HELIX 7 7 THR A 144 ASP A 147 5 4
HELIX 8 8 THR A 148 ASP A 155 1 8
HELIX 9 9 ASN A 183 ALA A 200 1 18
HELIX 10 10 SER A 220 VAL A 225 1 6
HELIX 11 11 ASP A 252 GLN A 255 5 4
HELIX 12 12 ASP A 256 ARG A 269 1 14
HELIX 13 13 ARG A 280 ASN A 290 1 11
HELIX 14 14 ARG B 58 HIS B 74 1 17
HELIX 15 15 PRO B 75 ARG B 78 5 4
HELIX 16 16 ASP B 81 ILE B 94 1 14
HELIX 17 17 THR B 102 ASP B 105 5 4
HELIX 18 18 TYR B 106 GLY B 113 1 8
HELIX 19 19 PRO B 118 LYS B 121 5 4
HELIX 20 20 ILE B 128 GLN B 139 1 12
HELIX 21 21 THR B 144 ASP B 147 5 4
HELIX 22 22 THR B 148 ASP B 155 1 8
HELIX 23 23 ASN B 183 ALA B 200 1 18
HELIX 24 24 SER B 220 VAL B 225 1 6
HELIX 25 25 GLN B 226 LEU B 230 5 5
HELIX 26 26 ASP B 252 GLN B 255 5 4
HELIX 27 27 ASP B 256 ARG B 269 1 14
HELIX 28 28 ARG B 280 ASN B 290 1 11
SHEET 1 A 2 GLY A 52 PRO A 53 0
SHEET 2 A 2 SER A 172 CYS A 173 -1 O CYS A 173 N GLY A 52
SHEET 1 B 4 LEU A 123 SER A 126 0
SHEET 2 B 4 ASP A 202 ASP A 209 1 O HIS A 205 N LEU A 124
SHEET 3 B 4 VAL A 235 ILE A 243 1 O ILE A 243 N LEU A 208
SHEET 4 B 4 GLN A 272 ILE A 278 1 O LYS A 276 N VAL A 242
SHEET 1 C 2 GLY B 52 PRO B 53 0
SHEET 2 C 2 SER B 172 CYS B 173 -1 O CYS B 173 N GLY B 52
SHEET 1 D 4 LEU B 123 SER B 126 0
SHEET 2 D 4 ASP B 202 ASP B 209 1 O HIS B 205 N LEU B 124
SHEET 3 D 4 VAL B 235 ILE B 243 1 O TRP B 241 N VAL B 206
SHEET 4 D 4 GLN B 272 ILE B 278 1 O LYS B 276 N ALA B 240
SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.06
SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.03
SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.03
SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.06
SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.06
SSBOND 6 CYS A 287 CYS A 296 1555 1555 2.03
SSBOND 7 CYS B 67 CYS B 82 1555 1555 2.06
SSBOND 8 CYS B 99 CYS B 180 1555 1555 2.04
SSBOND 9 CYS B 119 CYS B 201 1555 1555 2.04
SSBOND 10 CYS B 160 CYS B 173 1555 1555 2.05
SSBOND 11 CYS B 254 CYS B 275 1555 1555 2.05
SSBOND 12 CYS B 287 CYS B 296 1555 1555 2.19
SITE 1 AC1 19 LEU A 124 TRP A 125 SER A 126 ARG A 127
SITE 2 AC1 19 LEU A 145 GLU A 146 ASP A 155 TRP A 176
SITE 3 AC1 19 SER A 186 TRP A 189 SER A 193 SER A 220
SITE 4 AC1 19 THR A 221 PHE A 222 GLN A 226 HOH A 303
SITE 5 AC1 19 HOH A 338 HOH A 346 HOH A 350
SITE 1 AC2 17 LEU B 124 TRP B 125 SER B 126 ARG B 127
SITE 2 AC2 17 LYS B 129 LEU B 145 GLU B 146 ASP B 155
SITE 3 AC2 17 TRP B 189 SER B 193 SER B 220 THR B 221
SITE 4 AC2 17 PHE B 222 GLN B 226 HOH B 309 HOH B 310
SITE 5 AC2 17 HOH B 357
CRYST1 41.451 50.715 65.200 108.76 92.01 96.38 P 1 2
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 0.024125 0.002696 0.001830 0.00000
SCALE2 0.000000 0.019841 0.006882 0.00000
SCALE3 0.000000 0.000000 0.016244 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
