HEADER CYTOKINE/CYTOKINE RECEPTOR 19-JUN-08 3DI2
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN INTERLEUKIN-7 WITH
TITLE 2 UNGLYCOSYLATED HUMAN INTERLEUKIN-7 RECEPTOR ALPHA ECTODOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-7;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 26 TO 177;
COMPND 5 SYNONYM: IL-7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-7 RECEPTOR SUBUNIT ALPHA;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 21 TO 239 (LIGAND BINDING ECTODOMAIN);
COMPND 12 SYNONYM: IL-7R-ALPHA, CD127 ANTIGEN, CDW127;
COMPND 13 ENGINEERED: YES;
COMPND 14 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: IL7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RP;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: IL7R;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RP;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS INTERLEUKIN, CYTOKINE, CYTOKINE RECEPTOR, ECTODOMAIN, GLYCOPROTEIN,
KEYWDS 2 GROWTH FACTOR, SECRETED, ALTERNATIVE SPLICING, DISEASE MUTATION,
KEYWDS 3 MEMBRANE, PHOSPHOPROTEIN, POLYMORPHISM, RECEPTOR, SCID,
KEYWDS 4 TRANSMEMBRANE, CYTOKINE-CYTOKINE RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.MCELROY,J.A.DOHM,S.T.R.WALSH
REVDAT 2 20-OCT-21 3DI2 1 REMARK SEQADV
REVDAT 1 27-JAN-09 3DI2 0
JRNL AUTH C.A.MCELROY,J.A.DOHM,S.T.WALSH
JRNL TITL STRUCTURAL AND BIOPHYSICAL STUDIES OF THE HUMAN
JRNL TITL 2 IL-7/IL-7RALPHA COMPLEX.
JRNL REF STRUCTURE V. 17 54 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19141282
JRNL DOI 10.1016/J.STR.2008.10.019
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 69.6
REMARK 3 NUMBER OF REFLECTIONS : 16902
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 SET) : 0.212
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1335
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.03600
REMARK 3 B22 (A**2) : -5.38600
REMARK 3 B33 (A**2) : 1.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.33200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.416 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.534 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.879 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 34.18
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : 1PE_XPLOR.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : 1PE_XPLOR.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 7 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DI2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000048063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97932
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21610
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 52.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG 8000, 0.1M MES, 0.2 M
REMARK 280 CALCIUM ACETATE, PH 6.0, SITTING DROP, TEMPERATURE 292K, PH 6.00
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 56.51050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 MET A -1
REMARK 465 GLY A 0
REMARK 465 ASP A 1
REMARK 465 CYS A 2
REMARK 465 ASP A 3
REMARK 465 ILE A 4
REMARK 465 GLU A 5
REMARK 465 GLY A 6
REMARK 465 LYS A 7
REMARK 465 CYS A 92
REMARK 465 THR A 93
REMARK 465 GLY A 94
REMARK 465 GLN A 95
REMARK 465 VAL A 96
REMARK 465 LYS A 97
REMARK 465 GLY A 98
REMARK 465 ARG A 99
REMARK 465 LYS A 100
REMARK 465 PRO A 101
REMARK 465 ALA A 102
REMARK 465 ALA A 103
REMARK 465 LEU A 104
REMARK 465 GLY A 105
REMARK 465 ALA A 106
REMARK 465 ALA A 107
REMARK 465 GLN A 108
REMARK 465 PRO A 109
REMARK 465 THR A 110
REMARK 465 LYS A 111
REMARK 465 SER A 112
REMARK 465 LEU A 113
REMARK 465 GLU A 114
REMARK 465 GLU A 115
REMARK 465 ASN A 116
REMARK 465 LYS A 117
REMARK 465 SER A 118
REMARK 465 LEU A 119
REMARK 465 LYS A 120
REMARK 465 GLU A 121
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 GLU B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 TYR B 4
REMARK 465 ALA B 5
REMARK 465 GLN B 6
REMARK 465 ASN B 7
REMARK 465 GLY B 8
REMARK 465 ASP B 9
REMARK 465 LEU B 10
REMARK 465 GLU B 11
REMARK 465 ASP B 12
REMARK 465 ALA B 13
REMARK 465 GLU B 14
REMARK 465 LEU B 15
REMARK 465 ASP B 16
REMARK 465 ASN B 212
REMARK 465 ASN B 213
REMARK 465 SER B 214
REMARK 465 SER B 215
REMARK 465 GLY B 216
REMARK 465 GLU B 217
REMARK 465 MET B 218
REMARK 465 ASP B 219
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 ASP C 1
REMARK 465 CYS C 2
REMARK 465 ASP C 3
REMARK 465 ILE C 4
REMARK 465 GLU C 5
REMARK 465 GLY C 6
REMARK 465 LYS C 7
REMARK 465 ASN C 91
REMARK 465 CYS C 92
REMARK 465 THR C 93
REMARK 465 GLY C 94
REMARK 465 GLN C 95
REMARK 465 VAL C 96
REMARK 465 LYS C 97
REMARK 465 GLY C 98
REMARK 465 ARG C 99
REMARK 465 LYS C 100
REMARK 465 PRO C 101
REMARK 465 ALA C 102
REMARK 465 ALA C 103
REMARK 465 LEU C 104
REMARK 465 GLY C 105
REMARK 465 ALA C 106
REMARK 465 ALA C 107
REMARK 465 GLN C 108
REMARK 465 PRO C 109
REMARK 465 THR C 110
REMARK 465 LYS C 111
REMARK 465 SER C 112
REMARK 465 LEU C 113
REMARK 465 GLU C 114
REMARK 465 GLU C 115
REMARK 465 ASN C 116
REMARK 465 LYS C 117
REMARK 465 SER C 118
REMARK 465 LEU C 119
REMARK 465 LYS C 120
REMARK 465 GLU C 121
REMARK 465 GLN C 122
REMARK 465 LYS C 150
REMARK 465 GLU C 151
REMARK 465 HIS C 152
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 GLU D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 TYR D 4
REMARK 465 ALA D 5
REMARK 465 GLN D 6
REMARK 465 ASN D 7
REMARK 465 GLY D 8
REMARK 465 ASP D 9
REMARK 465 LEU D 10
REMARK 465 GLU D 11
REMARK 465 ASP D 12
REMARK 465 ALA D 13
REMARK 465 GLU D 210
REMARK 465 ILE D 211
REMARK 465 ASN D 212
REMARK 465 ASN D 213
REMARK 465 SER D 214
REMARK 465 SER D 215
REMARK 465 GLY D 216
REMARK 465 GLU D 217
REMARK 465 MET D 218
REMARK 465 ASP D 219
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 LYS A 10 CG CD CE NZ
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 28 CD CE NZ
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 ILE A 30 CG1 CD1
REMARK 470 SER A 32 OG
REMARK 470 LEU A 35 CD1 CD2
REMARK 470 ASN A 37 OD1 ND2
REMARK 470 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 MET A 54 CG SD CE
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 MET A 69 CG SD CE
REMARK 470 ASN A 70 CG OD1 ND2
REMARK 470 THR A 72 OG1 CG2
REMARK 470 ASN A 91 CG OD1 ND2
REMARK 470 GLN A 122 CD OE1 NE2
REMARK 470 LYS A 124 CD CE NZ
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 HIS A 152 ND1 CD2 CE1 NE2
REMARK 470 ASN B 29 OD1 ND2
REMARK 470 ASN B 48 CG OD1 ND2
REMARK 470 LYS B 61 CD CE NZ
REMARK 470 GLU B 70 CG CD OE1 OE2
REMARK 470 VAL B 91 CG1 CG2
REMARK 470 GLU B 93 CD OE1 OE2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 SER B 95 OG
REMARK 470 LYS B 153 CG CD CE NZ
REMARK 470 ASN B 156 CG OD1 ND2
REMARK 470 LYS B 157 CG CD CE NZ
REMARK 470 GLN B 176 CD OE1 NE2
REMARK 470 ILE B 211 CG1 CG2 CD1
REMARK 470 LYS C 10 CG CD CE NZ
REMARK 470 GLU C 13 CG CD OE1 OE2
REMARK 470 LYS C 28 CD CE NZ
REMARK 470 GLU C 29 CG CD OE1 OE2
REMARK 470 ILE C 30 CG1 CD1
REMARK 470 SER C 32 OG
REMARK 470 ASN C 33 CG OD1 ND2
REMARK 470 LEU C 35 CG CD1 CD2
REMARK 470 ASN C 37 OD1 ND2
REMARK 470 GLU C 38 CD OE1 OE2
REMARK 470 ARG C 44 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 51 CG CD CE NZ
REMARK 470 MET C 54 CG SD CE
REMARK 470 ARG C 58 CD NE CZ NH1 NH2
REMARK 470 ARG C 61 CD NE CZ NH1 NH2
REMARK 470 LYS C 68 CG CD CE NZ
REMARK 470 MET C 69 CG SD CE
REMARK 470 ASN C 70 CG OD1 ND2
REMARK 470 LYS C 123 CG CD CE NZ
REMARK 470 LYS C 124 CG CD CE NZ
REMARK 470 LYS C 144 CD CE NZ
REMARK 470 ILE C 145 CG2 CD1
REMARK 470 MET C 147 CG SD CE
REMARK 470 THR C 149 OG1 CG2
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 LEU D 15 CG CD1 CD2
REMARK 470 ASP D 16 CG OD1 OD2
REMARK 470 ASN D 29 OD1 ND2
REMARK 470 ASN D 48 CG OD1 ND2
REMARK 470 LYS D 61 CD CE NZ
REMARK 470 GLU D 70 CG CD OE1 OE2
REMARK 470 ASN D 86 CG OD1 ND2
REMARK 470 LYS D 90 CG CD CE NZ
REMARK 470 VAL D 91 CG1 CG2
REMARK 470 GLU D 93 CD OE1 OE2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 SER D 95 OG
REMARK 470 LYS D 100 CG CD CE NZ
REMARK 470 TYR D 119 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 121 CG CD OE1 OE2
REMARK 470 PHE D 126 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 141 CD CE NZ
REMARK 470 LYS D 153 CG CD CE NZ
REMARK 470 ASN D 156 CG OD1 ND2
REMARK 470 LYS D 157 CG CD CE NZ
REMARK 470 GLN D 172 CD OE1 NE2
REMARK 470 LYS D 174 CD CE NZ
REMARK 470 GLN D 176 CD OE1 NE2
REMARK 470 MET D 180 CG SD CE
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 SER A 32 34.99 -64.81
REMARK 500 ASN A 33 -11.93 -149.23
REMARK 500 LEU A 35 102.67 -54.56
REMARK 500 ASN A 37 102.04 -32.91
REMARK 500 GLU A 38 144.77 -33.92
REMARK 500 ALA A 49 126.54 -32.39
REMARK 500 LYS A 51 15.22 -178.59
REMARK 500 GLN A 65 -3.97 -58.50
REMARK 500 SER A 71 56.35 -62.98
REMARK 500 LEU A 90 -72.21 -109.41
REMARK 500 LEU A 146 -72.28 -73.39
REMARK 500 MET A 147 24.02 -62.50
REMARK 500 GLU A 151 -70.90 -112.75
REMARK 500 THR B 46 58.82 -110.14
REMARK 500 ASN B 48 -13.90 -145.68
REMARK 500 VAL B 58 -80.38 -116.07
REMARK 500 GLN B 69 -109.58 90.20
REMARK 500 GLU B 93 1.04 -161.94
REMARK 500 LEU B 103 -14.95 -41.16
REMARK 500 SER B 116 116.17 -170.68
REMARK 500 TYR B 139 -78.55 -96.88
REMARK 500 LYS B 157 78.43 -109.19
REMARK 500 ALA B 178 75.38 34.13
REMARK 500 ASP B 190 -5.13 -140.98
REMARK 500 HIS B 191 -109.29 -106.20
REMARK 500 SER C 32 42.71 -65.28
REMARK 500 ASN C 33 -6.61 -161.47
REMARK 500 LEU C 35 102.81 -53.69
REMARK 500 ASN C 37 105.56 -31.25
REMARK 500 GLU C 38 128.55 -35.72
REMARK 500 ALA C 49 127.22 -37.45
REMARK 500 ASN C 50 69.28 39.92
REMARK 500 LYS C 51 13.79 -179.81
REMARK 500 SER C 71 57.97 -65.19
REMARK 500 LEU C 146 -74.71 -72.82
REMARK 500 MET C 147 18.47 -59.96
REMARK 500 LEU D 15 29.78 -61.44
REMARK 500 THR D 46 57.94 -110.07
REMARK 500 ASN D 48 -11.54 -146.14
REMARK 500 VAL D 58 -82.43 -116.28
REMARK 500 GLN D 69 -107.25 86.95
REMARK 500 GLU D 93 1.03 -162.96
REMARK 500 LEU D 103 -17.85 -38.26
REMARK 500 SER D 116 115.37 -172.51
REMARK 500 TYR D 139 -81.32 -94.64
REMARK 500 ASN D 156 1.92 57.52
REMARK 500 LYS D 157 77.35 -108.24
REMARK 500 ALA D 178 75.60 37.58
REMARK 500 HIS D 191 -110.29 -107.90
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 1PE A 340
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DI3 RELATED DB: PDB
DBREF 3DI2 A 1 152 UNP P13232 IL7_HUMAN 26 177
DBREF 3DI2 B 1 219 UNP P16871 IL7RA_HUMAN 21 239
DBREF 3DI2 C 1 152 UNP P13232 IL7_HUMAN 26 177
DBREF 3DI2 D 1 219 UNP P16871 IL7RA_HUMAN 21 239
SEQADV 3DI2 MET A -1 UNP P13232 EXPRESSION TAG
SEQADV 3DI2 GLY A 0 UNP P13232 EXPRESSION TAG
SEQADV 3DI2 ALA A 106 UNP P13232 GLU 131 ENGINEERED MUTATION
SEQADV 3DI2 GLY B -3 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 SER B -2 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 HIS B -1 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 MET B 0 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 VAL B 118 UNP P16871 ILE 138 ENGINEERED MUTATION
SEQADV 3DI2 MET C -1 UNP P13232 EXPRESSION TAG
SEQADV 3DI2 GLY C 0 UNP P13232 EXPRESSION TAG
SEQADV 3DI2 ALA C 106 UNP P13232 GLU 131 ENGINEERED MUTATION
SEQADV 3DI2 GLY D -3 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 SER D -2 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 HIS D -1 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 MET D 0 UNP P16871 EXPRESSION TAG
SEQADV 3DI2 VAL D 118 UNP P16871 ILE 138 ENGINEERED MUTATION
SEQRES 1 A 154 MET GLY ASP CYS ASP ILE GLU GLY LYS ASP GLY LYS GLN
SEQRES 2 A 154 TYR GLU SER VAL LEU MET VAL SER ILE ASP GLN LEU LEU
SEQRES 3 A 154 ASP SER MET LYS GLU ILE GLY SER ASN CYS LEU ASN ASN
SEQRES 4 A 154 GLU PHE ASN PHE PHE LYS ARG HIS ILE CYS ASP ALA ASN
SEQRES 5 A 154 LYS GLU GLY MET PHE LEU PHE ARG ALA ALA ARG LYS LEU
SEQRES 6 A 154 ARG GLN PHE LEU LYS MET ASN SER THR GLY ASP PHE ASP
SEQRES 7 A 154 LEU HIS LEU LEU LYS VAL SER GLU GLY THR THR ILE LEU
SEQRES 8 A 154 LEU ASN CYS THR GLY GLN VAL LYS GLY ARG LYS PRO ALA
SEQRES 9 A 154 ALA LEU GLY ALA ALA GLN PRO THR LYS SER LEU GLU GLU
SEQRES 10 A 154 ASN LYS SER LEU LYS GLU GLN LYS LYS LEU ASN ASP LEU
SEQRES 11 A 154 CYS PHE LEU LYS ARG LEU LEU GLN GLU ILE LYS THR CYS
SEQRES 12 A 154 TRP ASN LYS ILE LEU MET GLY THR LYS GLU HIS
SEQRES 1 B 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 B 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 B 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 B 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 B 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 B 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 B 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 B 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 B 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 B 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 B 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 B 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 B 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 B 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 B 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 B 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 B 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 B 223 MET ASP
SEQRES 1 C 154 MET GLY ASP CYS ASP ILE GLU GLY LYS ASP GLY LYS GLN
SEQRES 2 C 154 TYR GLU SER VAL LEU MET VAL SER ILE ASP GLN LEU LEU
SEQRES 3 C 154 ASP SER MET LYS GLU ILE GLY SER ASN CYS LEU ASN ASN
SEQRES 4 C 154 GLU PHE ASN PHE PHE LYS ARG HIS ILE CYS ASP ALA ASN
SEQRES 5 C 154 LYS GLU GLY MET PHE LEU PHE ARG ALA ALA ARG LYS LEU
SEQRES 6 C 154 ARG GLN PHE LEU LYS MET ASN SER THR GLY ASP PHE ASP
SEQRES 7 C 154 LEU HIS LEU LEU LYS VAL SER GLU GLY THR THR ILE LEU
SEQRES 8 C 154 LEU ASN CYS THR GLY GLN VAL LYS GLY ARG LYS PRO ALA
SEQRES 9 C 154 ALA LEU GLY ALA ALA GLN PRO THR LYS SER LEU GLU GLU
SEQRES 10 C 154 ASN LYS SER LEU LYS GLU GLN LYS LYS LEU ASN ASP LEU
SEQRES 11 C 154 CYS PHE LEU LYS ARG LEU LEU GLN GLU ILE LYS THR CYS
SEQRES 12 C 154 TRP ASN LYS ILE LEU MET GLY THR LYS GLU HIS
SEQRES 1 D 223 GLY SER HIS MET GLU SER GLY TYR ALA GLN ASN GLY ASP
SEQRES 2 D 223 LEU GLU ASP ALA GLU LEU ASP ASP TYR SER PHE SER CYS
SEQRES 3 D 223 TYR SER GLN LEU GLU VAL ASN GLY SER GLN HIS SER LEU
SEQRES 4 D 223 THR CYS ALA PHE GLU ASP PRO ASP VAL ASN THR THR ASN
SEQRES 5 D 223 LEU GLU PHE GLU ILE CYS GLY ALA LEU VAL GLU VAL LYS
SEQRES 6 D 223 CYS LEU ASN PHE ARG LYS LEU GLN GLU ILE TYR PHE ILE
SEQRES 7 D 223 GLU THR LYS LYS PHE LEU LEU ILE GLY LYS SER ASN ILE
SEQRES 8 D 223 CYS VAL LYS VAL GLY GLU LYS SER LEU THR CYS LYS LYS
SEQRES 9 D 223 ILE ASP LEU THR THR ILE VAL LYS PRO GLU ALA PRO PHE
SEQRES 10 D 223 ASP LEU SER VAL VAL TYR ARG GLU GLY ALA ASN ASP PHE
SEQRES 11 D 223 VAL VAL THR PHE ASN THR SER HIS LEU GLN LYS LYS TYR
SEQRES 12 D 223 VAL LYS VAL LEU MET HIS ASP VAL ALA TYR ARG GLN GLU
SEQRES 13 D 223 LYS ASP GLU ASN LYS TRP THR HIS VAL ASN LEU SER SER
SEQRES 14 D 223 THR LYS LEU THR LEU LEU GLN ARG LYS LEU GLN PRO ALA
SEQRES 15 D 223 ALA MET TYR GLU ILE LYS VAL ARG SER ILE PRO ASP HIS
SEQRES 16 D 223 TYR PHE LYS GLY PHE TRP SER GLU TRP SER PRO SER TYR
SEQRES 17 D 223 TYR PHE ARG THR PRO GLU ILE ASN ASN SER SER GLY GLU
SEQRES 18 D 223 MET ASP
HET 1PE A 340 16
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 5 1PE C10 H22 O6
FORMUL 6 HOH *28(H2 O)
HELIX 1 1 ASP A 8 VAL A 15 1 8
HELIX 2 2 VAL A 15 SER A 26 1 12
HELIX 3 3 PHE A 39 HIS A 45 1 7
HELIX 4 4 LYS A 51 GLN A 65 1 15
HELIX 5 5 GLY A 73 ASN A 91 1 19
HELIX 6 6 ASP A 127 MET A 147 1 21
HELIX 7 7 THR B 132 LYS B 137 5 6
HELIX 8 8 ARG B 173 LEU B 175 5 3
HELIX 9 9 ASP C 8 VAL C 15 1 8
HELIX 10 10 VAL C 15 SER C 26 1 12
HELIX 11 11 PHE C 39 HIS C 45 1 7
HELIX 12 12 LYS C 51 GLN C 65 1 15
HELIX 13 13 GLY C 73 LEU C 90 1 18
HELIX 14 14 ASP C 127 MET C 147 1 21
HELIX 15 15 THR D 132 LYS D 137 5 6
HELIX 16 16 ARG D 173 LEU D 175 5 3
SHEET 1 A 4 PHE B 20 ASN B 29 0
SHEET 2 A 4 GLN B 32 PHE B 39 -1 O SER B 34 N GLN B 25
SHEET 3 A 4 ILE B 71 THR B 76 -1 O THR B 76 N HIS B 33
SHEET 4 A 4 ARG B 66 LEU B 68 -1 N LEU B 68 O ILE B 71
SHEET 1 B 4 CYS B 62 ASN B 64 0
SHEET 2 B 4 LEU B 49 CYS B 54 -1 N ILE B 53 O LEU B 63
SHEET 3 B 4 SER B 85 VAL B 91 -1 O LYS B 90 N GLU B 50
SHEET 4 B 4 LYS B 94 ILE B 101 -1 O ILE B 101 N SER B 85
SHEET 1 C 3 PHE B 113 SER B 116 0
SHEET 2 C 3 ASP B 125 ASN B 131 -1 O ASN B 131 N PHE B 113
SHEET 3 C 3 TYR B 119 ARG B 120 -1 N ARG B 120 O ASP B 125
SHEET 1 D 3 PHE B 113 SER B 116 0
SHEET 2 D 3 ASP B 125 ASN B 131 -1 O ASN B 131 N PHE B 113
SHEET 3 D 3 LYS B 167 LEU B 171 -1 O LEU B 168 N VAL B 128
SHEET 1 E 4 THR B 159 LEU B 163 0
SHEET 2 E 4 LEU B 143 GLN B 151 -1 N TYR B 149 O THR B 159
SHEET 3 E 4 ALA B 179 PRO B 189 -1 O LYS B 184 N ALA B 148
SHEET 4 E 4 TYR B 204 THR B 208 -1 O PHE B 206 N TYR B 181
SHEET 1 F 4 PHE D 20 ASN D 29 0
SHEET 2 F 4 GLN D 32 PHE D 39 -1 O SER D 34 N GLN D 25
SHEET 3 F 4 ILE D 71 THR D 76 -1 O THR D 76 N HIS D 33
SHEET 4 F 4 ARG D 66 LEU D 68 -1 N LEU D 68 O ILE D 71
SHEET 1 G 4 CYS D 62 ASN D 64 0
SHEET 2 G 4 LEU D 49 CYS D 54 -1 N ILE D 53 O LEU D 63
SHEET 3 G 4 SER D 85 VAL D 91 -1 O LYS D 90 N GLU D 50
SHEET 4 G 4 SER D 95 ILE D 101 -1 O ILE D 101 N SER D 85
SHEET 1 H 3 PHE D 113 SER D 116 0
SHEET 2 H 3 ASP D 125 ASN D 131 -1 O ASN D 131 N PHE D 113
SHEET 3 H 3 TYR D 119 ARG D 120 -1 N ARG D 120 O ASP D 125
SHEET 1 I 3 PHE D 113 SER D 116 0
SHEET 2 I 3 ASP D 125 ASN D 131 -1 O ASN D 131 N PHE D 113
SHEET 3 I 3 LYS D 167 LEU D 171 -1 O LEU D 168 N VAL D 128
SHEET 1 J 3 THR D 159 LEU D 163 0
SHEET 2 J 3 LEU D 143 GLN D 151 -1 N TYR D 149 O THR D 159
SHEET 3 J 3 SER D 187 PRO D 189 -1 O ILE D 188 N MET D 144
SHEET 1 K 4 THR D 159 LEU D 163 0
SHEET 2 K 4 LEU D 143 GLN D 151 -1 N TYR D 149 O THR D 159
SHEET 3 K 4 ALA D 179 LYS D 184 -1 O LYS D 184 N ALA D 148
SHEET 4 K 4 TYR D 204 THR D 208 -1 O PHE D 206 N TYR D 181
SSBOND 1 CYS A 34 CYS A 129 1555 1555 2.03
SSBOND 2 CYS A 47 CYS A 141 1555 1555 2.03
SSBOND 3 CYS B 22 CYS B 37 1555 1555 2.04
SSBOND 4 CYS B 54 CYS B 62 1555 1555 2.04
SSBOND 5 CYS B 88 CYS B 98 1555 1555 2.04
SSBOND 6 CYS C 34 CYS C 129 1555 1555 2.03
SSBOND 7 CYS C 47 CYS C 141 1555 1555 2.03
SSBOND 8 CYS D 22 CYS D 37 1555 1555 2.04
SSBOND 9 CYS D 54 CYS D 62 1555 1555 2.04
SSBOND 10 CYS D 88 CYS D 98 1555 1555 2.04
SITE 1 AC1 2 ASP A 8 ASN A 91
CRYST1 47.202 113.021 87.534 90.00 105.10 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 0.021186 0.000000 0.005716 0.00000
SCALE2 0.000000 0.008848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011833 0.00000
(ATOM LINES ARE NOT SHOWN.)
END