HEADER SIGNALING PROTEIN 21-FEB-17 5UWC
TITLE CYTOKINE-RECEPTOR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-3 RECEPTOR SUBUNIT ALPHA;
COMPND 3 CHAIN: G;
COMPND 4 FRAGMENT: UNP RESIDUES 20-307;
COMPND 5 SYNONYM: IL-3RA;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-3;
COMPND 10 CHAIN: I;
COMPND 11 FRAGMENT: UNP RESIDUES 31-152;
COMPND 12 SYNONYM: IL-3,HEMATOPOIETIC GROWTH FACTOR,MAST CELL GROWTH FACTOR,
COMPND 13 MCGF,MULTIPOTENTIAL COLONY-STIMULATING FACTOR,P-CELL-STIMULATING
COMPND 14 FACTOR;
COMPND 15 ENGINEERED: YES;
COMPND 16 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: IL3RA, IL3R;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: IL3;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYTOKINE, RECEPTOR, SIGNALLING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.BROUGHTON,M.W.PARKER
REVDAT 3 04-OCT-23 5UWC 1 HETSYN LINK
REVDAT 2 29-JUL-20 5UWC 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE ATOM
REVDAT 1 07-FEB-18 5UWC 0
JRNL AUTH S.E.BROUGHTON,T.R.HERCUS,T.L.NERO,W.L.KAN,E.F.BARRY,
JRNL AUTH 2 M.DOTTORE,K.S.CHEUNG TUNG SHING,C.J.MORTON,U.DHAGAT,
JRNL AUTH 3 M.P.HARDY,N.J.WILSON,M.T.DOWNTON,C.SCHIEBER,T.P.HUGHES,
JRNL AUTH 4 A.F.LOPEZ,M.W.PARKER
JRNL TITL A DUAL ROLE FOR THE N-TERMINAL DOMAIN OF THE IL-3 RECEPTOR
JRNL TITL 2 IN CELL SIGNALLING.
JRNL REF NAT COMMUN V. 9 386 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29374162
JRNL DOI 10.1038/S41467-017-02633-7
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 23081
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1242
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1650
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 84
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2958
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 103
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -1.57000
REMARK 3 B12 (A**2) : 0.24000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.286
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.867
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3126 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2905 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4241 ; 1.550 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6669 ; 0.995 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 362 ; 6.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 153 ;36.569 ;23.660
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 515 ;16.522 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.414 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 465 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3502 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 763 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; 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 ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; 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): 1460 ; 1.736 ; 5.727
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1459 ; 1.737 ; 5.724
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1818 ; 3.115 ; 8.570
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1819 ; 3.114 ; 8.574
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1666 ; 1.632 ; 6.013
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1664 ; 1.631 ; 6.014
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2423 ; 2.887 ; 8.941
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3295 ; 5.854 ;44.871
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3296 ; 5.853 ;44.874
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 27 G 293
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4046 55.1976 6.4162
REMARK 3 T TENSOR
REMARK 3 T11: 0.0294 T22: 0.0794
REMARK 3 T33: 0.0231 T12: 0.0191
REMARK 3 T13: 0.0035 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 0.9228 L22: 1.1998
REMARK 3 L33: 1.1252 L12: 0.8075
REMARK 3 L13: 0.2993 L23: 0.6958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0832 S12: -0.0288 S13: -0.1037
REMARK 3 S21: 0.0382 S22: -0.0828 S23: -0.1335
REMARK 3 S31: 0.0844 S32: 0.1376 S33: -0.0004
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5UWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6-5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23081
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 92.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 16.10
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 4JZJ, 1JLI
REMARK 200
REMARK 200 REMARK: TETRAGONAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 200 MM NACL AND 100 MM
REMARK 280 CITRATE-PHOSPHATE BUFFER PH 4.8, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.03867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.07733
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 48.05800
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 80.09667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 16.01933
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: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, 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 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 G 20
REMARK 465 GLU G 21
REMARK 465 ASP G 22
REMARK 465 PRO G 23
REMARK 465 ASN G 24
REMARK 465 PRO G 25
REMARK 465 PRO G 26
REMARK 465 ASP G 42
REMARK 465 LEU G 43
REMARK 465 ASN G 44
REMARK 465 ARG G 45
REMARK 465 ASN G 46
REMARK 465 VAL G 47
REMARK 465 THR G 48
REMARK 465 ASP G 49
REMARK 465 ILE G 50
REMARK 465 ALA G 86
REMARK 465 ASN G 87
REMARK 465 PRO G 88
REMARK 465 PRO G 89
REMARK 465 PHE G 90
REMARK 465 ASP G 294
REMARK 465 GLN G 295
REMARK 465 GLU G 296
REMARK 465 GLU G 297
REMARK 465 GLY G 298
REMARK 465 VAL G 299
REMARK 465 ASN G 300
REMARK 465 THR G 301
REMARK 465 ARG G 302
REMARK 465 ALA G 303
REMARK 465 TRP G 304
REMARK 465 ARG G 305
REMARK 465 THR G 306
REMARK 465 SER G 307
REMARK 465 GLN I 124
REMARK 465 GLN I 125
REMARK 465 THR I 126
REMARK 465 THR I 127
REMARK 465 LEU I 128
REMARK 465 SER I 129
REMARK 465 LEU I 130
REMARK 465 ALA I 131
REMARK 465 ILE I 132
REMARK 465 PHE I 133
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CZ3 TRP G 41 CG2 VAL G 83 1.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CD1 LEU I 32 CB ASN I 80 3774 2.19
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 ASN G 29 51.33 -112.96
REMARK 500 ARG G 31 143.19 -173.30
REMARK 500 THR G 40 -161.27 -111.19
REMARK 500 SER G 66 -32.07 -136.47
REMARK 500 ALA G 72 45.83 -148.09
REMARK 500 SER G 100 -58.86 -135.92
REMARK 500 VAL G 117 -54.72 71.49
REMARK 500 ARG G 146 71.79 -118.12
REMARK 500 ASN G 218 155.75 178.54
REMARK 500 ASP G 256 71.23 28.16
REMARK 500 ARG G 257 132.54 -171.35
REMARK 500 LYS I 28 43.97 -100.56
REMARK 500 LEU I 32 -115.68 61.06
REMARK 500 ASN I 39 39.11 -94.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 1
REMARK 610 NAG G 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UV8 RELATED DB: PDB
DBREF 5UWC G 20 307 UNP P26951 IL3RA_HUMAN 20 307
DBREF 5UWC I 12 133 UNP P08700 IL3_HUMAN 31 152
SEQADV 5UWC GLN G 212 UNP P26951 ASN 212 ENGINEERED MUTATION
SEQADV 5UWC VAL G 299 UNP P26951 ALA 299 ENGINEERED MUTATION
SEQADV 5UWC TYR I 13 UNP P08700 TRP 32 ENGINEERED MUTATION
SEQADV 5UWC TRP I 116 UNP P08700 LYS 135 ENGINEERED MUTATION
SEQRES 1 G 288 LYS GLU ASP PRO ASN PRO PRO ILE THR ASN LEU ARG MET
SEQRES 2 G 288 LYS ALA LYS ALA GLN GLN LEU THR TRP ASP LEU ASN ARG
SEQRES 3 G 288 ASN VAL THR ASP ILE GLU CYS VAL LYS ASP ALA ASP TYR
SEQRES 4 G 288 SER MET PRO ALA VAL ASN ASN SER TYR CYS GLN PHE GLY
SEQRES 5 G 288 ALA ILE SER LEU CYS GLU VAL THR ASN TYR THR VAL ARG
SEQRES 6 G 288 VAL ALA ASN PRO PRO PHE SER THR TRP ILE LEU PHE PRO
SEQRES 7 G 288 GLU ASN SER GLY LYS PRO TRP ALA GLY ALA GLU ASN LEU
SEQRES 8 G 288 THR CYS TRP ILE HIS ASP VAL ASP PHE LEU SER CYS SER
SEQRES 9 G 288 TRP ALA VAL GLY PRO GLY ALA PRO ALA ASP VAL GLN TYR
SEQRES 10 G 288 ASP LEU TYR LEU ASN VAL ALA ASN ARG ARG GLN GLN TYR
SEQRES 11 G 288 GLU CYS LEU HIS TYR LYS THR ASP ALA GLN GLY THR ARG
SEQRES 12 G 288 ILE GLY CYS ARG PHE ASP ASP ILE SER ARG LEU SER SER
SEQRES 13 G 288 GLY SER GLN SER SER HIS ILE LEU VAL ARG GLY ARG SER
SEQRES 14 G 288 ALA ALA PHE GLY ILE PRO CYS THR ASP LYS PHE VAL VAL
SEQRES 15 G 288 PHE SER GLN ILE GLU ILE LEU THR PRO PRO GLN MET THR
SEQRES 16 G 288 ALA LYS CYS ASN LYS THR HIS SER PHE MET HIS TRP LYS
SEQRES 17 G 288 MET ARG SER HIS PHE ASN ARG LYS PHE ARG TYR GLU LEU
SEQRES 18 G 288 GLN ILE GLN LYS ARG MET GLN PRO VAL ILE THR GLU GLN
SEQRES 19 G 288 VAL ARG ASP ARG THR SER PHE GLN LEU LEU ASN PRO GLY
SEQRES 20 G 288 THR TYR THR VAL GLN ILE ARG ALA ARG GLU ARG VAL TYR
SEQRES 21 G 288 GLU PHE LEU SER ALA TRP SER THR PRO GLN ARG PHE GLU
SEQRES 22 G 288 CYS ASP GLN GLU GLU GLY VAL ASN THR ARG ALA TRP ARG
SEQRES 23 G 288 THR SER
SEQRES 1 I 122 SER TYR VAL ASN CYS SER ASN MET ILE ASP GLU ILE ILE
SEQRES 2 I 122 THR HIS LEU LYS GLN PRO PRO LEU PRO LEU LEU ASP PHE
SEQRES 3 I 122 ASN ASN LEU ASN GLY GLU ASP GLN ASP ILE LEU MET GLU
SEQRES 4 I 122 ASN ASN LEU ARG ARG PRO ASN LEU GLU ALA PHE ASN ARG
SEQRES 5 I 122 ALA VAL LYS SER LEU GLN ASN ALA SER ALA ILE GLU SER
SEQRES 6 I 122 ILE LEU LYS ASN LEU LEU PRO CYS LEU PRO LEU ALA THR
SEQRES 7 I 122 ALA ALA PRO THR ARG HIS PRO ILE HIS ILE LYS ASP GLY
SEQRES 8 I 122 ASP TRP ASN GLU PHE ARG ARG LYS LEU THR PHE TYR LEU
SEQRES 9 I 122 TRP THR LEU GLU ASN ALA GLN ALA GLN GLN THR THR LEU
SEQRES 10 I 122 SER LEU ALA ILE PHE
HET NAG A 1 14
HET NAG A 2 14
HET FUL A 3 10
HET NAG G 401 14
HET CIT G 402 13
HET IMD G 406 5
HET EDT G 407 20
HET CIT I 201 13
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM CIT CITRIC ACID
HETNAM IMD IMIDAZOLE
HETNAM EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-
HETNAM 2 EDT AMINO}-ACETIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUL BETA-L-FUCOSE; 6-DEOXY-BETA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUL FUCOSE; FUCOSE; 6-DEOXY-BETA-L-GALACTOSE
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 3 FUL C6 H12 O5
FORMUL 5 CIT 2(C6 H8 O7)
FORMUL 6 IMD C3 H5 N2 1+
FORMUL 7 EDT C10 H16 N2 O8
FORMUL 9 HOH *64(H2 O)
HELIX 1 AA1 ASP G 169 SER G 175 1 7
HELIX 2 AA2 SER G 203 ILE G 205 5 3
HELIX 3 AA3 ASN I 15 LYS I 28 1 14
HELIX 4 AA4 ASP I 36 LEU I 40 5 5
HELIX 5 AA5 ASN I 41 GLU I 50 1 10
HELIX 6 AA6 LEU I 53 LYS I 66 1 14
HELIX 7 AA7 ALA I 71 LYS I 79 1 9
HELIX 8 AA8 ASN I 80 LEU I 85 5 6
HELIX 9 AA9 ASP I 103 GLN I 122 1 20
SHEET 1 AA1 3 MET G 32 LYS G 33 0
SHEET 2 AA1 3 GLN G 38 LEU G 39 -1 O GLN G 38 N LYS G 33
SHEET 3 AA1 3 CYS G 68 GLN G 69 -1 O CYS G 68 N LEU G 39
SHEET 1 AA2 4 TYR G 58 MET G 60 0
SHEET 2 AA2 4 CYS G 52 LYS G 54 -1 N CYS G 52 O MET G 60
SHEET 3 AA2 4 THR G 79 VAL G 83 -1 O THR G 82 N VAL G 53
SHEET 4 AA2 4 THR G 92 PHE G 96 -1 O ILE G 94 N TYR G 81
SHEET 1 AA3 4 GLU G 108 HIS G 115 0
SHEET 2 AA3 4 PHE G 119 ALA G 125 -1 O ALA G 125 N GLU G 108
SHEET 3 AA3 4 ARG G 162 PHE G 167 -1 O CYS G 165 N CYS G 122
SHEET 4 AA3 4 HIS G 153 THR G 156 -1 N LYS G 155 O GLY G 164
SHEET 1 AA4 4 GLN G 148 GLU G 150 0
SHEET 2 AA4 4 GLN G 135 VAL G 142 -1 N LEU G 140 O TYR G 149
SHEET 3 AA4 4 SER G 179 ARG G 187 -1 O HIS G 181 N ASN G 141
SHEET 4 AA4 4 THR G 196 VAL G 201 -1 O THR G 196 N VAL G 184
SHEET 1 AA5 3 GLN G 212 LYS G 216 0
SHEET 2 AA5 3 HIS G 221 LYS G 227 -1 O HIS G 225 N THR G 214
SHEET 3 AA5 3 SER G 259 LEU G 263 -1 O LEU G 262 N SER G 222
SHEET 1 AA6 4 ILE G 250 ARG G 255 0
SHEET 2 AA6 4 PHE G 236 GLN G 243 -1 N ILE G 242 O ILE G 250
SHEET 3 AA6 4 THR G 267 GLU G 276 -1 O ARG G 275 N ARG G 237
SHEET 4 AA6 4 GLN G 289 GLU G 292 -1 O PHE G 291 N TYR G 268
SSBOND 1 CYS G 52 CYS G 68 1555 1555 2.98
SSBOND 2 CYS G 76 CYS G 195 1555 1555 2.89
SSBOND 3 CYS G 112 CYS G 122 1555 1555 2.87
SSBOND 4 CYS G 151 CYS G 165 1555 1555 2.05
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.73
LINK O6 NAG A 1 C1 FUL A 3 1555 1555 1.43
CISPEP 1 ASP G 55 ALA G 56 0 -5.13
CISPEP 2 PHE G 96 PRO G 97 0 -10.21
CISPEP 3 ARG G 145 ARG G 146 0 -14.91
CISPEP 4 PRO I 31 LEU I 32 0 -13.28
CRYST1 106.461 106.461 96.116 90.00 90.00 120.00 P 61 6
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 0.009393 0.005423 0.000000 0.00000
SCALE2 0.000000 0.010846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END