HEADER HYDROLASE 20-FEB-07 2EF1
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CD38
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: CYCLIC ADP-RIBOSE HYDROLASE 1, CADPR HYDROLASE 1, LYMPHOCYTE
COMPND 6 DIFFERENTIATION ANTIGEN CD38, T10, ACUTE LYMPHOBLASTIC LEUKEMIA CELLS
COMPND 7 ANTIGEN CD38;
COMPND 8 EC: 3.2.2.5;
COMPND 9 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: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMAL-CR1
KEYWDS HYDROLASE, CELL SUEFACE ANTIGEN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUKIMOTO-NIINO,O.NUREKI,K.MURAYAMA,M.SHIROUZU,T.KATADA,M.HARA-
AUTHOR 2 YOKOYAMA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 3 25-OCT-23 2EF1 1 REMARK
REVDAT 2 24-FEB-09 2EF1 1 VERSN
REVDAT 1 27-FEB-07 2EF1 0
SPRSDE 27-FEB-07 2EF1 2DF1
JRNL AUTH M.KUKIMOTO-NIINO,O.NUREKI,K.MURAYAMA,M.SHIROUZU,T.KATADA,
JRNL AUTH 2 M.HARA-YOKOYAMA,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CD38
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1217355.380
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 21492
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) : 0.203
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2133
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2674
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 290
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3973
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.36000
REMARK 3 B22 (A**2) : -13.11000
REMARK 3 B33 (A**2) : 2.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.31000
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) : 0.25
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) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.760
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 27.74
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : EPE_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : EPE_XPLOR_TOP.TXT
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000026584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.082
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9641
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.627
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 (%): 50.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 10000, 0.1M HEPES, 0.1M SODIUM
REMARK 280 IODIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.58200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 GLY B 245
REMARK 465 GLY B 246
REMARK 465 ARG B 247
REMARK 465 GLU B 248
REMARK 465 ASP B 249
REMARK 465 SER B 250
REMARK 465 ASN B 290
REMARK 465 PRO B 291
REMARK 465 GLU B 292
REMARK 465 ASP B 293
REMARK 465 SER B 294
REMARK 465 SER B 295
REMARK 465 CYS B 296
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 PRO A 98 15.01 -64.82
REMARK 500 PRO A 118 108.64 -49.16
REMARK 500 ILE A 128 42.93 -154.48
REMARK 500 ASP A 179 -71.07 -106.58
REMARK 500 ASN A 182 53.06 -92.07
REMARK 500 ASP A 202 -113.90 59.64
REMARK 500 VAL A 225 -42.08 -135.47
REMARK 500 ASN A 290 56.20 -142.42
REMARK 500 PRO B 98 19.47 -62.98
REMARK 500 PRO B 118 108.08 -44.59
REMARK 500 ILE B 128 46.92 -161.72
REMARK 500 ARG B 140 1.06 -59.76
REMARK 500 ASN B 164 25.27 47.19
REMARK 500 ASP B 179 -68.18 -109.62
REMARK 500 ASN B 182 46.87 -84.65
REMARK 500 ASP B 202 -110.72 58.23
REMARK 500 ASN B 219 38.85 -88.35
REMARK 500 VAL B 225 -43.78 -137.36
REMARK 500 PRO B 257 -80.28 -37.00
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 EPE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SRZ001000050.1 RELATED DB: TARGETDB
DBREF 2EF1 A 45 300 UNP P28907 CD38_HUMAN 45 300
DBREF 2EF1 B 45 300 UNP P28907 CD38_HUMAN 45 300
SEQADV 2EF1 THR A 49 UNP P28907 GLN 49 SEE REMARK 999
SEQADV 2EF1 THR B 49 UNP P28907 GLN 49 SEE REMARK 999
SEQRES 1 A 256 ARG TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS
SEQRES 2 A 256 ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR
SEQRES 3 A 256 THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN
SEQRES 4 A 256 SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS
SEQRES 5 A 256 HIS PRO CYS ASN ILE THR GLU GLU ASP TYR GLN PRO LEU
SEQRES 6 A 256 MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE
SEQRES 7 A 256 LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE
SEQRES 8 A 256 THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR
SEQRES 9 A 256 LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY
SEQRES 10 A 256 GLU PHE ASN THR SER LYS ILE ASN TYR GLN SER CYS PRO
SEQRES 11 A 256 ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL
SEQRES 12 A 256 PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA
SEQRES 13 A 256 CYS ASP VAL VAL HIS VAL MET LEU ASN GLY SER ARG SER
SEQRES 14 A 256 LYS ILE PHE ASP LYS ASN SER THR PHE GLY SER VAL GLU
SEQRES 15 A 256 VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU
SEQRES 16 A 256 ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP
SEQRES 17 A 256 LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE
SEQRES 18 A 256 ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE
SEQRES 19 A 256 TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO
SEQRES 20 A 256 GLU ASP SER SER CYS THR SER GLU ILE
SEQRES 1 B 256 ARG TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS
SEQRES 2 B 256 ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR
SEQRES 3 B 256 THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN
SEQRES 4 B 256 SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS
SEQRES 5 B 256 HIS PRO CYS ASN ILE THR GLU GLU ASP TYR GLN PRO LEU
SEQRES 6 B 256 MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE
SEQRES 7 B 256 LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE
SEQRES 8 B 256 THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR
SEQRES 9 B 256 LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY
SEQRES 10 B 256 GLU PHE ASN THR SER LYS ILE ASN TYR GLN SER CYS PRO
SEQRES 11 B 256 ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL
SEQRES 12 B 256 PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA
SEQRES 13 B 256 CYS ASP VAL VAL HIS VAL MET LEU ASN GLY SER ARG SER
SEQRES 14 B 256 LYS ILE PHE ASP LYS ASN SER THR PHE GLY SER VAL GLU
SEQRES 15 B 256 VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU
SEQRES 16 B 256 ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP
SEQRES 17 B 256 LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE
SEQRES 18 B 256 ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE
SEQRES 19 B 256 TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO
SEQRES 20 B 256 GLU ASP SER SER CYS THR SER GLU ILE
HET EPE A 301 15
HET EPE B 302 15
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 EPE 2(C8 H18 N2 O4 S)
FORMUL 5 HOH *182(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 ILE A 94 1 14
HELIX 4 4 THR A 102 GLY A 113 1 12
HELIX 5 5 PRO A 118 LYS A 121 5 4
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 GLU A 226 LEU A 230 5 5
HELIX 12 12 ASP A 252 GLN A 255 5 4
HELIX 13 13 ASP A 256 ARG A 269 1 14
HELIX 14 14 ARG A 280 ASN A 290 1 11
HELIX 15 15 ARG B 58 HIS B 74 1 17
HELIX 16 16 PRO B 75 ARG B 78 5 4
HELIX 17 17 ASP B 81 ILE B 94 1 14
HELIX 18 18 THR B 102 ASP B 105 5 4
HELIX 19 19 TYR B 106 GLY B 113 1 8
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 199 1 17
HELIX 24 24 SER B 220 VAL B 225 1 6
HELIX 25 25 VAL B 225 LEU B 230 1 6
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 LYS B 289 1 10
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 ASN A 209 1 O HIS A 205 N LEU A 124
SHEET 3 B 4 VAL A 235 ILE A 243 1 O TRP A 241 N LEU A 208
SHEET 4 B 4 GLN A 272 ILE A 278 1 O SER A 274 N ALA A 240
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 ASN 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 LEU B 208
SHEET 4 D 4 GLN B 272 ILE B 278 1 O SER B 274 N ALA B 240
SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.04
SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.03
SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.04
SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.04
SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.03
SSBOND 6 CYS B 67 CYS B 82 1555 1555 2.03
SSBOND 7 CYS B 99 CYS B 180 1555 1555 2.03
SSBOND 8 CYS B 119 CYS B 201 1555 1555 2.04
SSBOND 9 CYS B 160 CYS B 173 1555 1555 2.03
SSBOND 10 CYS B 254 CYS B 275 1555 1555 2.03
SITE 1 AC1 7 ARG A 127 LEU A 157 THR A 158 SER A 220
SITE 2 AC1 7 THR A 221 HOH A 345 HOH A 355
SITE 1 AC2 6 ARG B 127 LEU B 157 SER B 220 THR B 221
SITE 2 AC2 6 HOH B 340 HOH B 347
CRYST1 57.593 51.164 101.135 90.00 97.53 90.00 P 1 21 1 4
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 0.017363 0.000000 0.002294 0.00000
SCALE2 0.000000 0.019545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009974 0.00000
(ATOM LINES ARE NOT SHOWN.)
END