HEADER CYTOKINE 22-APR-24 8Z8L TITLE STRUCTURE OF IL-4RA IN COMPLEX WITH AN NANOBODY 4E9 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-4 RECEPTOR SUBUNIT ALPHA; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: IL-4 RECEPTOR SUBUNIT ALPHA,IL-4R SUBUNIT ALPHA,IL-4R-ALPHA, COMPND 5 IL-4RA; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NANOBODY DAB1; COMPND 10 CHAIN: A; COMPND 11 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: IL4R, IL4RA, 582J2.1; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS INFLAMMATION, CYTOKINE, ANTIBODY, IMMUNE DISORDER EXPDTA X-RAY DIFFRACTION AUTHOR G.SONG,W.QIU REVDAT 1 30-APR-25 8Z8L 0 JRNL AUTH G.SONG,W.QIU JRNL TITL STRUCTURE OF IL-4RA IN COMPLEX WITH AN NANOBODY 4E9 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.2 REMARK 3 NUMBER OF REFLECTIONS : 4488 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.303 REMARK 3 R VALUE (WORKING SET) : 0.301 REMARK 3 FREE R VALUE : 0.334 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 225 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 19.8200 - 4.9800 1.00 2502 132 0.2809 0.3297 REMARK 3 2 4.9800 - 3.9600 0.72 1761 93 0.3833 0.3514 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 : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.622 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.996 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 191.3 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 208.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.003 2443 REMARK 3 ANGLE : 0.672 3341 REMARK 3 CHIRALITY : 0.057 374 REMARK 3 PLANARITY : 0.006 425 REMARK 3 DIHEDRAL : 5.432 347 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:96 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.511 -35.126 -6.051 REMARK 3 T TENSOR REMARK 3 T11: 2.2651 T22: 1.3851 REMARK 3 T33: 1.8735 T12: -0.2044 REMARK 3 T13: -0.5378 T23: 0.1182 REMARK 3 L TENSOR REMARK 3 L11: 8.4387 L22: 0.9265 REMARK 3 L33: 4.8508 L12: 1.9826 REMARK 3 L13: -2.8112 L23: 1.3473 REMARK 3 S TENSOR REMARK 3 S11: -1.3032 S12: 0.4441 S13: 0.2887 REMARK 3 S21: -1.7516 S22: 0.4522 S23: 2.1645 REMARK 3 S31: 1.0427 S32: -1.2825 S33: 0.7423 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 1:115 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.099 -56.626 15.581 REMARK 3 T TENSOR REMARK 3 T11: 1.5081 T22: 1.4132 REMARK 3 T33: 1.4300 T12: -0.2185 REMARK 3 T13: -0.0943 T23: -0.0634 REMARK 3 L TENSOR REMARK 3 L11: 11.3605 L22: 8.0845 REMARK 3 L33: 6.2996 L12: -5.4693 REMARK 3 L13: -0.9308 L23: -3.5880 REMARK 3 S TENSOR REMARK 3 S11: 0.4467 S12: -0.1163 S13: -1.4379 REMARK 3 S21: 0.1856 S22: 0.4965 S23: -0.7437 REMARK 3 S31: 0.7028 S32: -0.2053 S33: -1.0539 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN B AND RESID 97:197 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.370 -10.498 11.740 REMARK 3 T TENSOR REMARK 3 T11: 1.5590 T22: 1.9303 REMARK 3 T33: 2.1311 T12: -0.2209 REMARK 3 T13: -0.2111 T23: 0.3555 REMARK 3 L TENSOR REMARK 3 L11: 10.6805 L22: 9.1120 REMARK 3 L33: 9.1947 L12: 1.4118 REMARK 3 L13: -2.6741 L23: 3.2228 REMARK 3 S TENSOR REMARK 3 S11: -0.0362 S12: 1.0688 S13: 1.4340 REMARK 3 S21: 0.2796 S22: -0.4406 S23: -0.3399 REMARK 3 S31: -0.0925 S32: 0.3391 S33: 0.6216 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 8Z8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-24. REMARK 100 THE DEPOSITION ID IS D_1300044135. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-JAN-23 REMARK 200 TEMPERATURE (KELVIN) : 99 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4534 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.960 REMARK 200 RESOLUTION RANGE LOW (A) : 95.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 12.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.21 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 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: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM MALONATE DIBASIC REMARK 280 MONOHYDRATE PH 6.0, VAPOR DIFFUSION, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 0.00000 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 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 71.46800 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.26207 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 49.69567 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 71.46800 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 41.26207 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 49.69567 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 71.46800 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 41.26207 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 49.69567 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 71.46800 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 41.26207 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 49.69567 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 71.46800 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 41.26207 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 49.69567 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 71.46800 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 41.26207 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 49.69567 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 82.52414 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 99.39133 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 82.52414 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 99.39133 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 82.52414 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 99.39133 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 82.52414 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 99.39133 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 82.52414 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 99.39133 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 82.52414 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 99.39133 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: 1760 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C 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 THR B 108 REMARK 465 ASN B 109 REMARK 465 VAL B 110 REMARK 465 SER B 111 REMARK 465 SER B 164 REMARK 465 THR B 165 REMARK 465 LEU B 166 REMARK 465 LYS B 167 REMARK 465 SER B 168 REMARK 465 ASN B 198 REMARK 465 SER B 199 REMARK 465 TYR B 200 REMARK 465 ARG B 201 REMARK 465 GLU B 202 REMARK 465 PRO B 203 REMARK 465 PHE B 204 REMARK 465 GLU B 205 REMARK 465 GLN B 206 REMARK 465 HIS B 207 REMARK 465 HIS B 208 REMARK 465 HIS B 209 REMARK 465 HIS B 210 REMARK 465 HIS B 211 REMARK 465 HIS B 212 REMARK 465 HIS B 213 REMARK 465 ALA B 214 REMARK 465 GLU A 116 REMARK 465 SER A 117 REMARK 465 HIS A 118 REMARK 465 HIS A 119 REMARK 465 HIS A 120 REMARK 465 HIS A 121 REMARK 465 HIS A 122 REMARK 465 HIS A 123 REMARK 465 ALA A 124 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 B 2 CG CD CE NZ REMARK 470 LYS B 22 CG CD CE NZ REMARK 470 ARG A 19 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 40 CG CD CE NZ REMARK 470 ARG A 42 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 73 CG CD CE NZ REMARK 470 LYS A 84 CG CD CE NZ REMARK 470 ARG A 102 CG CD NE CZ NH1 NH2 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 MET B 14 -42.11 -134.56 REMARK 500 SER B 15 -31.90 -148.17 REMARK 500 GLU B 32 -50.98 -139.63 REMARK 500 VAL B 40 76.85 -115.03 REMARK 500 PHE B 41 -161.24 -127.81 REMARK 500 LEU B 43 49.90 -105.57 REMARK 500 PRO B 98 -178.68 -65.76 REMARK 500 PRO B 121 5.60 -69.25 REMARK 500 THR B 153 0.39 -159.69 REMARK 500 ALA B 162 48.00 -146.54 REMARK 500 LEU A 18 119.61 -165.93 REMARK 500 SER A 50 -74.17 -66.34 REMARK 500 SER A 54 108.65 -168.02 REMARK 500 ARG A 64 -65.74 -94.75 REMARK 500 SER A 72 -109.39 55.88 REMARK 500 CYS A 101 68.83 -68.10 REMARK 500 TRP A 105 -51.19 -141.50 REMARK 500 GLN A 107 -141.24 64.01 REMARK 500 REMARK 500 REMARK: NULL DBREF 8Z8L B 1 207 UNP P24394 IL4RA_HUMAN 26 232 DBREF 8Z8L A 1 124 PDB 8Z8L 8Z8L 1 124 SEQADV 8Z8L ALA B 182 UNP P24394 CYS 207 ENGINEERED MUTATION SEQADV 8Z8L HIS B 208 UNP P24394 EXPRESSION TAG SEQADV 8Z8L HIS B 209 UNP P24394 EXPRESSION TAG SEQADV 8Z8L HIS B 210 UNP P24394 EXPRESSION TAG SEQADV 8Z8L HIS B 211 UNP P24394 EXPRESSION TAG SEQADV 8Z8L HIS B 212 UNP P24394 EXPRESSION TAG SEQADV 8Z8L HIS B 213 UNP P24394 EXPRESSION TAG SEQADV 8Z8L ALA B 214 UNP P24394 EXPRESSION TAG SEQRES 1 B 214 MET LYS VAL LEU GLN GLU PRO THR CYS VAL SER ASP TYR SEQRES 2 B 214 MET SER ILE SER THR CYS GLU TRP LYS MET ASN GLY PRO SEQRES 3 B 214 THR ASN CYS SER THR GLU LEU ARG LEU LEU TYR GLN LEU SEQRES 4 B 214 VAL PHE LEU LEU SER GLU ALA HIS THR CYS ILE PRO GLU SEQRES 5 B 214 ASN ASN GLY GLY ALA GLY CYS VAL CYS HIS LEU LEU MET SEQRES 6 B 214 ASP ASP VAL VAL SER ALA ASP ASN TYR THR LEU ASP LEU SEQRES 7 B 214 TRP ALA GLY GLN GLN LEU LEU TRP LYS GLY SER PHE LYS SEQRES 8 B 214 PRO SER GLU HIS VAL LYS PRO ARG ALA PRO GLY ASN LEU SEQRES 9 B 214 THR VAL HIS THR ASN VAL SER ASP THR LEU LEU LEU THR SEQRES 10 B 214 TRP SER ASN PRO TYR PRO PRO ASP ASN TYR LEU TYR ASN SEQRES 11 B 214 HIS LEU THR TYR ALA VAL ASN ILE TRP SER GLU ASN ASP SEQRES 12 B 214 PRO ALA ASP PHE ARG ILE TYR ASN VAL THR TYR LEU GLU SEQRES 13 B 214 PRO SER LEU ARG ILE ALA ALA SER THR LEU LYS SER GLY SEQRES 14 B 214 ILE SER TYR ARG ALA ARG VAL ARG ALA TRP ALA GLN ALA SEQRES 15 B 214 TYR ASN THR THR TRP SER GLU TRP SER PRO SER THR LYS SEQRES 16 B 214 TRP HIS ASN SER TYR ARG GLU PRO PHE GLU GLN HIS HIS SEQRES 17 B 214 HIS HIS HIS HIS HIS ALA SEQRES 1 A 124 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 124 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 124 ASP PHE TYR CYS MET ALA TRP PHE ARG GLN ALA PRO GLY SEQRES 4 A 124 LYS GLU ARG GLU ALA VAL ALA ALA ILE ARG SER GLY GLY SEQRES 5 A 124 ARG SER THR TYR TYR ALA ASP SER VAL LYS GLY ARG PHE SEQRES 6 A 124 THR ILE SER ARG ASP ASN SER LYS ASN THR LEU TYR LEU SEQRES 7 A 124 GLN MET ASN SER LEU LYS ALA GLU ASP THR ALA VAL TYR SEQRES 8 A 124 TYR CYS ALA VAL GLY VAL ASP GLY ASN CYS ARG ASN TYR SEQRES 9 A 124 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER GLU SER SEQRES 10 A 124 HIS HIS HIS HIS HIS HIS ALA HET NAG C 1 14 HET NAG C 2 14 HET NAG B 301 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 3 NAG 3(C8 H15 N O6) HELIX 1 AA1 TYR B 127 LEU B 132 1 6 HELIX 2 AA2 LYS A 84 THR A 88 5 5 SHEET 1 AA1 4 VAL B 3 SER B 11 0 SHEET 2 AA1 4 ILE B 16 MET B 23 -1 O LYS B 22 N GLN B 5 SHEET 3 AA1 4 GLY B 58 LEU B 64 -1 O CYS B 61 N CYS B 19 SHEET 4 AA1 4 GLU B 52 ASN B 53 -1 N GLU B 52 O VAL B 60 SHEET 1 AA2 4 HIS B 47 CYS B 49 0 SHEET 2 AA2 4 LEU B 33 GLN B 38 -1 N TYR B 37 O HIS B 47 SHEET 3 AA2 4 TYR B 74 ALA B 80 -1 O TRP B 79 N ARG B 34 SHEET 4 AA2 4 GLN B 83 PHE B 90 -1 O GLN B 83 N ALA B 80 SHEET 1 AA3 3 GLY B 102 HIS B 107 0 SHEET 2 AA3 3 LEU B 114 SER B 119 -1 O SER B 119 N GLY B 102 SHEET 3 AA3 3 SER B 158 ILE B 161 -1 O ILE B 161 N LEU B 114 SHEET 1 AA4 4 PHE B 147 ASN B 151 0 SHEET 2 AA4 4 ALA B 135 TRP B 139 -1 N ILE B 138 O ARG B 148 SHEET 3 AA4 4 ARG B 173 ARG B 177 -1 O ARG B 173 N TRP B 139 SHEET 4 AA4 4 THR B 194 LYS B 195 -1 O THR B 194 N ALA B 174 SHEET 1 AA5 4 LEU A 4 SER A 7 0 SHEET 2 AA5 4 SER A 17 ALA A 24 -1 O SER A 21 N SER A 7 SHEET 3 AA5 4 THR A 75 ASN A 81 -1 O MET A 80 N LEU A 18 SHEET 4 AA5 4 THR A 66 ARG A 69 -1 N SER A 68 O TYR A 77 SHEET 1 AA6 6 GLY A 10 VAL A 12 0 SHEET 2 AA6 6 THR A 109 VAL A 113 1 O LEU A 110 N GLY A 10 SHEET 3 AA6 6 ALA A 89 GLY A 96 -1 N ALA A 89 O VAL A 111 SHEET 4 AA6 6 CYS A 30 ALA A 37 -1 N CYS A 30 O GLY A 96 SHEET 5 AA6 6 LYS A 40 ILE A 48 -1 O GLU A 43 N ARG A 35 SHEET 6 AA6 6 THR A 55 TYR A 57 -1 O TYR A 56 N ALA A 47 SSBOND 1 CYS B 9 CYS B 19 1555 1555 2.03 SSBOND 2 CYS B 29 CYS B 59 1555 1555 2.03 SSBOND 3 CYS B 49 CYS B 61 1555 1555 2.03 SSBOND 4 CYS A 22 CYS A 93 1555 1555 2.03 SSBOND 5 CYS A 30 CYS A 101 1555 1555 2.03 LINK ND2 ASN B 73 C1 NAG B 301 1555 1555 1.45 LINK ND2 ASN B 151 C1 NAG C 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 CRYST1 142.936 142.936 149.087 90.00 90.00 120.00 H 3 2 18 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 0.006996 0.004039 0.000000 0.00000 SCALE2 0.000000 0.008078 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006707 0.00000