HEADER HYDROLASE/IMMUNE SYSTEM 28-MAR-11 3RAJ
TITLE CRYSTAL STRUCTURE OF HUMAN CD38 IN COMPLEX WITH THE FAB FRAGMENT OF
TITLE 2 ANTIBODY HB7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 46-300;
COMPND 5 SYNONYM: CYCLIC ADP-RIBOSE HYDROLASE 1, CADPR HYDROLASE 1, T10;
COMPND 6 EC: 3.2.2.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: HEAVY CHAIN OF THE FAB FRAGMENT OF ANTIBODY HB7;
COMPND 11 CHAIN: H;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: LIGHT CHAIN OF THE FAB FRAGMENT OF ANTIBODY HB7;
COMPND 15 CHAIN: L;
COMPND 16 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: CD38;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: MOUSE;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 18 EXPRESSION_SYSTEM_CELL: HYBRIDOMA CELL;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 21 ORGANISM_COMMON: MOUSE;
SOURCE 22 ORGANISM_TAXID: 10090;
SOURCE 23 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 24 EXPRESSION_SYSTEM_COMMON: MOUSE;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 26 EXPRESSION_SYSTEM_CELL: HYBRIDOMA CELL
KEYWDS CD38, ADP-RIBOSYL CYCLASE, CYCLIC ADP-RIBOSE, X-CRYSTALLOGRAPHY,
KEYWDS 2 CALCIUM SIGNALING, AGONISTIC ANTIBODY, HB7, HYDROLASE-IMMUNE SYSTEM
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,H.C.LEE,Q.HAO
REVDAT 3 01-NOV-23 3RAJ 1 SEQADV
REVDAT 2 08-NOV-17 3RAJ 1 REMARK
REVDAT 1 27-APR-11 3RAJ 0
JRNL AUTH H.ZHANG,Y.J.ZHAO,Q.HAO,H.C.LEE
JRNL TITL ENGINEERING A NOVEL CYTOSOLIC FORM OF CD38 FOR CYCLIC
JRNL TITL 2 ADP-RIBOSE DEPENDENT SIGNALING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_378
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.570
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 19773
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1001
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 48.1630 - 5.8196 0.99 3096 159 0.2014 0.2475
REMARK 3 2 5.8196 - 4.6204 0.99 2977 145 0.1882 0.2485
REMARK 3 3 4.6204 - 4.0367 0.98 2908 159 0.1781 0.2750
REMARK 3 4 4.0367 - 3.6678 0.94 2752 153 0.1925 0.2823
REMARK 3 5 3.6678 - 3.4049 0.90 2628 144 0.2397 0.3103
REMARK 3 6 3.4049 - 3.2042 0.84 2455 139 0.2774 0.3622
REMARK 3 7 3.2042 - 3.0438 0.67 1956 102 0.2859 0.3720
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 80.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 98.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.68050
REMARK 3 B22 (A**2) : -10.45690
REMARK 3 B33 (A**2) : 32.89160
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 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 : 0.010 5164
REMARK 3 ANGLE : 1.355 7015
REMARK 3 CHIRALITY : 0.087 793
REMARK 3 PLANARITY : 0.006 889
REMARK 3 DIHEDRAL : 16.555 1833
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 3RAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19878
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.044
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.44500
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
REMARK 200 STARTING MODEL: 1YH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.6M SODIUM FORMATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 68.33050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.33050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.83200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 135.76050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.83200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 135.76050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.33050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.83200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 135.76050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.33050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.83200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 135.76050
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L
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 GLU A 44
REMARK 465 PHE A 45
REMARK 465 TRP A 46
REMARK 465 ARG A 47
REMARK 465 GLN A 48
REMARK 465 THR A 49
REMARK 465 ARG A 280
REMARK 465 PRO A 281
REMARK 465 ASP A 282
REMARK 465 LYS A 283
REMARK 465 PHE A 284
REMARK 465 LEU A 285
REMARK 465 GLN A 286
REMARK 465 CYS A 287
REMARK 465 VAL A 288
REMARK 465 LYS A 289
REMARK 465 ASN A 290
REMARK 465 PRO A 291
REMARK 465 GLU A 292
REMARK 465 ASP A 293
REMARK 465 SER A 294
REMARK 465 SER A 295
REMARK 465 CYS A 296
REMARK 465 THR A 297
REMARK 465 SER A 298
REMARK 465 GLU A 299
REMARK 465 ILE A 300
REMARK 465 THR H 1
REMARK 465 ALA H 137
REMARK 465 GLN H 138
REMARK 465 THR H 139
REMARK 465 ASN H 140
REMARK 465 ARG L 209
REMARK 465 ASN L 210
REMARK 465 GLU L 211
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 LEU A 131 CG CD1 CD2
REMARK 470 HIS A 133 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 134 CG CD OE1 NE2
REMARK 470 LEU H 2 CD1 CD2
REMARK 470 GLN H 4 CD OE1 NE2
REMARK 470 LYS H 6 CD CE NZ
REMARK 470 ARG H 18 CD NE CZ NH1 NH2
REMARK 470 ARG H 54 CD NE CZ NH1 NH2
REMARK 470 MET H 65 SD CE
REMARK 470 THR H 71 CG2
REMARK 470 LYS H 98 CD CE NZ
REMARK 470 LEU H 100 CD1 CD2
REMARK 470 LYS H 122 CG CD CE NZ
REMARK 470 GLN H 178 CG CD OE1 NE2
REMARK 470 SER H 179 OG
REMARK 470 GLU H 218 CD OE1 OE2
REMARK 470 ASN H 219 OD1 ND2
REMARK 470 ARG L 106 CG CD NE CZ NH1 NH2
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 LEU H 100 CA - CB - CG ANGL. DEV. = 15.4 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 THR A 55 126.46 -37.47
REMARK 500 LYS A 57 158.20 -45.54
REMARK 500 ARG A 58 42.87 34.98
REMARK 500 GLU A 72 -74.20 -66.15
REMARK 500 HIS A 74 79.30 -111.42
REMARK 500 GLU A 76 12.39 -67.81
REMARK 500 MET A 77 -89.19 -101.58
REMARK 500 ARG A 78 -44.00 53.67
REMARK 500 HIS A 79 9.22 -65.74
REMARK 500 CYS A 82 -37.58 -30.57
REMARK 500 SER A 95 -23.72 86.84
REMARK 500 PRO A 98 13.69 -60.69
REMARK 500 PRO A 108 -66.06 -27.22
REMARK 500 THR A 114 129.77 -24.75
REMARK 500 PRO A 118 78.50 -60.47
REMARK 500 HIS A 133 0.80 -55.98
REMARK 500 LEU A 145 -9.08 -55.38
REMARK 500 THR A 165 -129.85 -115.37
REMARK 500 SER A 166 45.88 176.48
REMARK 500 ILE A 168 156.36 -43.39
REMARK 500 CYS A 180 151.66 -40.32
REMARK 500 ASP A 202 -121.79 67.00
REMARK 500 ARG A 212 151.43 -39.33
REMARK 500 VAL A 225 -63.95 -102.05
REMARK 500 LYS A 234 -43.15 -134.93
REMARK 500 GLU A 248 -52.68 91.99
REMARK 500 SER A 250 175.17 -53.43
REMARK 500 ARG A 251 98.27 121.83
REMARK 500 ASP A 252 103.66 -58.32
REMARK 500 CYS A 254 4.48 -63.12
REMARK 500 ASP A 256 134.64 -27.12
REMARK 500 ASN A 270 5.68 91.05
REMARK 500 SER H 8 159.55 170.90
REMARK 500 PRO H 10 -97.47 -88.44
REMARK 500 SER H 11 -56.35 112.90
REMARK 500 GLN H 17 -167.29 -115.78
REMARK 500 PHE H 28 -179.53 177.44
REMARK 500 TRP H 53 172.30 -59.99
REMARK 500 ALA H 62 -45.03 -25.21
REMARK 500 SER H 69 87.39 -158.12
REMARK 500 SER H 85 69.31 35.94
REMARK 500 LEU H 86 -175.29 -64.02
REMARK 500 ASP H 90 18.05 -64.39
REMARK 500 ALA H 92 178.37 171.89
REMARK 500 ILE H 101 157.51 63.59
REMARK 500 ALA H 121 90.76 156.03
REMARK 500 LYS H 122 162.57 -43.67
REMARK 500 SER H 135 -74.10 -31.83
REMARK 500 MET H 142 -157.49 -144.36
REMARK 500 PRO H 154 -151.32 -104.59
REMARK 500
REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS.
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 TYR L 70 THR L 71 -149.36
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3RAJ A 46 300 UNP P28907 CD38_HUMAN 46 300
DBREF 3RAJ H 1 220 PDB 3RAJ 3RAJ 1 220
DBREF 3RAJ L 1 211 PDB 3RAJ 3RAJ 1 211
SEQADV 3RAJ GLU A 44 UNP P28907 EXPRESSION TAG
SEQADV 3RAJ PHE A 45 UNP P28907 EXPRESSION TAG
SEQADV 3RAJ THR A 49 UNP P28907 GLN 49 ENGINEERED MUTATION
SEQADV 3RAJ ASP A 100 UNP P28907 ASN 100 ENGINEERED MUTATION
SEQADV 3RAJ ASP A 164 UNP P28907 ASN 164 ENGINEERED MUTATION
SEQADV 3RAJ ASP A 209 UNP P28907 ASN 209 ENGINEERED MUTATION
SEQADV 3RAJ ASP A 219 UNP P28907 ASN 219 ENGINEERED MUTATION
SEQRES 1 A 257 GLU PHE TRP ARG GLN THR TRP SER GLY PRO GLY THR THR
SEQRES 2 A 257 LYS ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS
SEQRES 3 A 257 TYR THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS
SEQRES 4 A 257 GLN SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER
SEQRES 5 A 257 LYS HIS PRO CYS ASP ILE THR GLU GLU ASP TYR GLN PRO
SEQRES 6 A 257 LEU MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS
SEQRES 7 A 257 ILE LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN
SEQRES 8 A 257 PHE THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP
SEQRES 9 A 257 THR LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS
SEQRES 10 A 257 GLY GLU PHE ASP THR SER LYS ILE ASN TYR GLN SER CYS
SEQRES 11 A 257 PRO ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER
SEQRES 12 A 257 VAL PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA
SEQRES 13 A 257 ALA CYS ASP VAL VAL HIS VAL MET LEU ASP GLY SER ARG
SEQRES 14 A 257 SER LYS ILE PHE ASP LYS ASP SER THR PHE GLY SER VAL
SEQRES 15 A 257 GLU VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU
SEQRES 16 A 257 GLU ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG
SEQRES 17 A 257 ASP LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER
SEQRES 18 A 257 ILE ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN
SEQRES 19 A 257 ILE TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN
SEQRES 20 A 257 PRO GLU ASP SER SER CYS THR SER GLU ILE
SEQRES 1 H 220 THR LEU VAL GLN LEU LYS GLN SER GLY PRO SER LEU VAL
SEQRES 2 H 220 GLN PRO SER GLN ARG LEU SER ILE THR CYS THR VAL SER
SEQRES 3 H 220 GLY PHE SER LEU ILE SER TYR GLY VAL HIS TRP VAL ARG
SEQRES 4 H 220 GLN SER PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE
SEQRES 5 H 220 TRP ARG GLY GLY SER THR ASP TYR ASN ALA ALA PHE MET
SEQRES 6 H 220 SER ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN
SEQRES 7 H 220 VAL PHE PHE LYS MET ASN SER LEU GLN ALA ASP ASP THR
SEQRES 8 H 220 ALA ILE TYR PHE CYS ALA LYS THR LEU ILE THR THR GLY
SEQRES 9 H 220 TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 H 220 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 H 220 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL
SEQRES 12 H 220 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 H 220 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES 14 H 220 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES 15 H 220 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 H 220 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 H 220 SER SER THR LYS VAL ASP LYS LYS ILE GLU ASN ARG
SEQRES 1 L 211 ILE GLN MET THR GLN SER SER SER SER PHE SER VAL SER
SEQRES 2 L 211 LEU GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER GLU
SEQRES 3 L 211 ASP ILE TYR ASN ARG LEU ALA TRP TYR GLN GLN LYS PRO
SEQRES 4 L 211 GLY ASN ALA PRO ARG LEU LEU ILE SER GLY ALA THR SER
SEQRES 5 L 211 LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER GLY
SEQRES 6 L 211 SER GLY LYS ASP TYR THR LEU SER ILE THR SER LEU GLN
SEQRES 7 L 211 THR GLU ASP VAL ALA THR TYR TYR CYS GLN GLN TYR TRP
SEQRES 8 L 211 SER THR PRO THR PHE GLY GLY GLY THR LYS LEU GLU ILE
SEQRES 9 L 211 LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO
SEQRES 10 L 211 PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL
SEQRES 11 L 211 VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN
SEQRES 12 L 211 VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY
SEQRES 13 L 211 VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER
SEQRES 14 L 211 THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP
SEQRES 15 L 211 GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR
SEQRES 16 L 211 HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN
SEQRES 17 L 211 ARG ASN GLU
HELIX 1 1 ARG A 58 HIS A 74 1 17
HELIX 2 2 ASP A 81 GLY A 91 1 11
HELIX 3 3 TYR A 106 THR A 114 1 9
HELIX 4 4 ILE A 128 HIS A 133 1 6
HELIX 5 5 PHE A 135 MET A 142 1 8
HELIX 6 6 THR A 148 ASP A 155 1 8
HELIX 7 7 ASN A 183 ALA A 199 1 17
HELIX 8 8 SER A 220 VAL A 225 1 6
HELIX 9 9 GLU A 226 LEU A 230 5 5
HELIX 10 10 ASP A 256 LYS A 268 1 13
HELIX 11 11 ASN H 74 LYS H 76 5 3
HELIX 12 12 SER H 193 TRP H 195 5 3
HELIX 13 13 SER L 119 THR L 124 1 6
HELIX 14 14 LYS L 181 GLU L 185 1 5
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 2 ILE A 122 LEU A 123 0
SHEET 2 B 2 PHE A 143 THR A 144 1 O PHE A 143 N LEU A 123
SHEET 1 C 3 ASP A 202 GLY A 210 0
SHEET 2 C 3 VAL A 235 HIS A 244 1 O TRP A 241 N VAL A 206
SHEET 3 C 3 GLN A 272 ILE A 278 1 O GLN A 272 N LEU A 238
SHEET 1 D 4 GLN H 4 LEU H 5 0
SHEET 2 D 4 THR H 22 SER H 26 -1 O SER H 26 N GLN H 4
SHEET 3 D 4 GLN H 78 PHE H 80 -1 O VAL H 79 N CYS H 23
SHEET 4 D 4 THR H 71 ASP H 73 -1 N THR H 71 O PHE H 80
SHEET 1 E 6 LEU H 12 VAL H 13 0
SHEET 2 E 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 13
SHEET 3 E 6 ALA H 92 THR H 99 -1 N ALA H 92 O VAL H 116
SHEET 4 E 6 VAL H 35 SER H 41 -1 N VAL H 38 O PHE H 95
SHEET 5 E 6 GLY H 45 ILE H 52 -1 O GLY H 50 N TRP H 37
SHEET 6 E 6 THR H 58 TYR H 60 -1 O ASP H 59 N VAL H 51
SHEET 1 F 4 LEU H 12 VAL H 13 0
SHEET 2 F 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 13
SHEET 3 F 4 ALA H 92 THR H 99 -1 N ALA H 92 O VAL H 116
SHEET 4 F 4 MET H 107 TRP H 110 -1 O TYR H 109 N LYS H 98
SHEET 1 G 4 SER H 127 LEU H 131 0
SHEET 2 G 4 MET H 142 TYR H 152 -1 O LYS H 150 N SER H 127
SHEET 3 G 4 LEU H 181 SER H 185 -1 O LEU H 184 N VAL H 149
SHEET 4 G 4 VAL H 176 GLN H 178 -1 N GLN H 178 O LEU H 181
SHEET 1 H 3 SER H 127 LEU H 131 0
SHEET 2 H 3 MET H 142 TYR H 152 -1 O LYS H 150 N SER H 127
SHEET 3 H 3 VAL H 188 PRO H 191 -1 O VAL H 188 N LEU H 145
SHEET 1 I 3 THR H 158 TRP H 161 0
SHEET 2 I 3 CYS H 202 HIS H 206 -1 O ASN H 203 N THR H 160
SHEET 3 I 3 THR H 211 ASP H 214 -1 O THR H 211 N HIS H 206
SHEET 1 J 2 SER L 9 SER L 11 0
SHEET 2 J 2 LYS L 101 GLU L 103 1 O GLU L 103 N PHE L 10
SHEET 1 K 3 THR L 19 LYS L 23 0
SHEET 2 K 3 ASP L 69 ILE L 74 -1 O LEU L 72 N ILE L 20
SHEET 3 K 3 PHE L 61 SER L 66 -1 N SER L 62 O SER L 73
SHEET 1 L 4 ARG L 44 ILE L 47 0
SHEET 2 L 4 LEU L 32 GLN L 37 -1 N TRP L 34 O LEU L 46
SHEET 3 L 4 THR L 84 GLN L 89 -1 O GLN L 88 N ALA L 33
SHEET 4 L 4 THR L 95 PHE L 96 -1 O THR L 95 N GLN L 89
SHEET 1 M 3 GLY L 127 PHE L 133 0
SHEET 2 M 3 MET L 173 THR L 180 -1 O LEU L 179 N ALA L 128
SHEET 3 M 3 SER L 160 TRP L 161 -1 N SER L 160 O SER L 174
SHEET 1 N 4 SER L 151 GLU L 152 0
SHEET 2 N 4 VAL L 144 ILE L 148 -1 N ILE L 148 O SER L 151
SHEET 3 N 4 TYR L 190 ALA L 194 -1 O THR L 191 N LYS L 147
SHEET 4 N 4 ILE L 203 PHE L 207 -1 O LYS L 205 N CYS L 192
SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.05
SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.02
SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.05
SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.03
SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.04
SSBOND 6 CYS H 23 CYS H 96 1555 1555 2.05
SSBOND 7 CYS H 147 CYS H 202 1555 1555 2.03
SSBOND 8 CYS L 22 CYS L 87 1555 1555 2.03
SSBOND 9 CYS L 132 CYS L 192 1555 1555 2.03
CISPEP 1 PHE H 153 PRO H 154 0 -6.42
CISPEP 2 GLU H 155 PRO H 156 0 2.41
CISPEP 3 TRP H 195 PRO H 196 0 5.62
CISPEP 4 TYR L 138 PRO L 139 0 -3.59
CRYST1 59.664 271.521 136.661 90.00 90.00 90.00 C 2 2 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 0.016761 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003683 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007317 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
