HEADER SIGNALING PROTEIN 09-FEB-12 4DOH
TITLE IL20/IL201/IL20R2 TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-20;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: IL-20, CYTOKINE ZCYTO10;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INTERLEUKIN-20 RECEPTOR SUBUNIT BETA;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: IL-20 RECEPTOR SUBUNIT BETA, IL-20R-BETA, IL-20RB, IL-20R2;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: INTERLEUKIN-20 RECEPTOR SUBUNIT ALPHA;
COMPND 14 CHAIN: R, E;
COMPND 15 SYNONYM: IL-20 RECEPTOR SUBUNIT ALPHA, IL-20R-ALPHA, IL-20RA,
COMPND 16 CYTOKINE RECEPTOR CLASS-II MEMBER 8, CYTOKINE RECEPTOR FAMILY 2
COMPND 17 MEMBER 8, CRF2-8, IL-20R1, ZCYTOR7;
COMPND 18 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: IL20, ZCYTO10, UNQ852/PRO1801;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: IL20RB, DIRS1, UNQ557/PRO1114;
SOURCE 14 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7215;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: IL20RA, UNQ681/PRO1315;
SOURCE 22 EXPRESSION_SYSTEM: DROSOPHILA;
SOURCE 23 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7215
KEYWDS IL10 FAMILY CYTOKINE RECEPTOR COMPLEX, ALPHA HELICAL CYTOKINE FOLD
KEYWDS 2 BETA SANDWHICH RECEPTOR FOLD, SIGNALING COMPLEX, EXTRACELLULAR,
KEYWDS 3 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.J.LOGSDON,M.R.WALTER
REVDAT 5 29-JUL-20 4DOH 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 SITE
REVDAT 4 16-OCT-13 4DOH 1 REMARK
REVDAT 3 02-JAN-13 4DOH 1 JRNL
REVDAT 2 08-AUG-12 4DOH 1 JRNL
REVDAT 1 18-JUL-12 4DOH 0
JRNL AUTH N.J.LOGSDON,A.DESHPANDE,B.D.HARRIS,K.R.RAJASHANKAR,
JRNL AUTH 2 M.R.WALTER
JRNL TITL STRUCTURAL BASIS FOR RECEPTOR SHARING AND ACTIVATION BY
JRNL TITL 2 INTERLEUKIN-20 RECEPTOR-2 (IL-20R2) BINDING CYTOKINES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 12704 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22802649
JRNL DOI 10.1073/PNAS.1117551109
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35822
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1952
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 : 8822
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 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) : NULL
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) : 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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 38635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 90.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 6000, 0.1M ADA, 0.1M MGCL2, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 51.55750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.16700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.88200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.16700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.55750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.88200
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, R
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E
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 ALA B 29
REMARK 465 ASP B 30
REMARK 465 GLU B 31
REMARK 465 VAL B 32
REMARK 465 ALA B 33
REMARK 465 GLN B 227
REMARK 465 GLY B 228
REMARK 465 GLU B 229
REMARK 465 ALA B 230
REMARK 465 ILE B 231
REMARK 465 GLU B 232
REMARK 465 GLY B 233
REMARK 465 ARG B 234
REMARK 465 ALA R 29
REMARK 465 VAL R 30
REMARK 465 PRO R 31
REMARK 465 CYS R 32
REMARK 465 VAL R 33
REMARK 465 SER R 34
REMARK 465 GLY R 35
REMARK 465 GLY R 36
REMARK 465 LEU R 37
REMARK 465 PRO R 38
REMARK 465 GLN R 243
REMARK 465 SER R 244
REMARK 465 SER R 245
REMARK 465 ILE R 246
REMARK 465 GLU R 247
REMARK 465 GLY R 248
REMARK 465 ARG R 249
REMARK 465 ALA D 29
REMARK 465 ASP D 30
REMARK 465 GLU D 31
REMARK 465 VAL D 32
REMARK 465 ALA D 33
REMARK 465 GLN D 227
REMARK 465 GLY D 228
REMARK 465 GLU D 229
REMARK 465 ALA D 230
REMARK 465 ILE D 231
REMARK 465 GLU D 232
REMARK 465 GLY D 233
REMARK 465 ARG D 234
REMARK 465 ALA E 29
REMARK 465 VAL E 30
REMARK 465 PRO E 31
REMARK 465 CYS E 32
REMARK 465 VAL E 33
REMARK 465 SER E 34
REMARK 465 GLY E 35
REMARK 465 GLY E 36
REMARK 465 LEU E 37
REMARK 465 PRO E 38
REMARK 465 GLN E 243
REMARK 465 SER E 244
REMARK 465 SER E 245
REMARK 465 ILE E 246
REMARK 465 GLU E 247
REMARK 465 GLY E 248
REMARK 465 ARG E 249
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 ALA A 24 CB
REMARK 470 VAL B 167 CG1 CG2
REMARK 470 LYS R 39 CG CD CE NZ
REMARK 470 LYS R 241 CG CD CE NZ
REMARK 470 ALA C 24 CB
REMARK 470 VAL D 167 CG1 CG2
REMARK 470 LYS E 39 CG CD CE NZ
REMARK 470 LYS E 241 CG CD CE NZ
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 ND2 ASN E 182 C1 NAG E 301 2.14
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 LEU A 30 61.22 -118.17
REMARK 500 ARG A 67 -19.29 114.92
REMARK 500 VAL A 94 -74.57 -104.90
REMARK 500 PRO A 154 -85.32 -32.84
REMARK 500 GLU B 62 -157.81 -69.69
REMARK 500 THR B 79 59.34 -147.28
REMARK 500 CYS B 89 62.81 -116.36
REMARK 500 LEU B 91 71.19 72.96
REMARK 500 PRO B 95 45.10 -76.02
REMARK 500 SER B 122 -176.87 -68.26
REMARK 500 ARG B 172 77.64 -67.92
REMARK 500 ALA B 200 118.56 91.47
REMARK 500 PRO R 40 170.12 -58.28
REMARK 500 MET R 50 -1.84 83.95
REMARK 500 PRO R 59 -108.16 -56.04
REMARK 500 GLU R 60 -11.95 -149.60
REMARK 500 GLN R 63 -65.29 -127.69
REMARK 500 TYR R 76 125.56 -37.18
REMARK 500 GLU R 86 1.66 -65.67
REMARK 500 ASN R 89 87.77 53.00
REMARK 500 TRP R 116 -97.34 -115.78
REMARK 500 LYS R 122 -117.63 -17.06
REMARK 500 ASN R 191 18.48 58.76
REMARK 500 PRO R 231 122.00 -39.23
REMARK 500 ARG C 67 -45.00 116.19
REMARK 500 ARG C 93 18.61 -143.17
REMARK 500 ASP C 102 108.72 -45.20
REMARK 500 THR C 131 11.67 -141.15
REMARK 500 CYS C 132 58.62 -119.30
REMARK 500 PRO C 154 -72.50 -21.84
REMARK 500 LEU D 35 104.84 -51.16
REMARK 500 PRO D 38 144.88 -34.52
REMARK 500 GLN D 40 82.32 44.31
REMARK 500 SER D 80 -7.78 -56.51
REMARK 500 LEU D 91 65.80 82.99
REMARK 500 PRO D 95 34.01 -84.97
REMARK 500 ALA D 176 162.82 -48.26
REMARK 500 ALA D 200 125.56 98.75
REMARK 500 MET E 50 10.02 59.15
REMARK 500 PRO E 58 142.78 -34.68
REMARK 500 PRO E 59 -119.86 -57.07
REMARK 500 GLN E 63 -68.35 -127.36
REMARK 500 VAL E 65 -36.05 -38.89
REMARK 500 LYS E 66 70.17 -105.63
REMARK 500 GLU E 86 -8.83 -56.18
REMARK 500 ASN E 89 91.64 49.49
REMARK 500 ARG E 92 171.50 -54.48
REMARK 500 TRP E 116 -97.99 -116.55
REMARK 500 LYS E 122 -150.32 13.49
REMARK 500 ASP E 147 -119.57 -104.35
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 GLY B 198 ALA B 199 -145.98
REMARK 500 GLY D 187 ILE D 188 -149.94
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 B 301
REMARK 610 NAG R 301
REMARK 610 NAG R 302
REMARK 610 NAG D 301
REMARK 610 NAG E 301
DBREF 4DOH A 25 176 UNP Q9NYY1 IL20_HUMAN 25 176
DBREF 4DOH B 30 231 UNP Q6UXL0 I20RB_HUMAN 30 231
DBREF 4DOH R 29 245 UNP Q9UHF4 I20RA_HUMAN 29 245
DBREF 4DOH C 25 176 UNP Q9NYY1 IL20_HUMAN 25 176
DBREF 4DOH D 30 231 UNP Q6UXL0 I20RB_HUMAN 30 231
DBREF 4DOH E 29 245 UNP Q9UHF4 I20RA_HUMAN 29 245
SEQADV 4DOH ALA A 24 UNP Q9NYY1 EXPRESSION TAG
SEQADV 4DOH ALA B 29 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH GLN B 40 UNP Q6UXL0 ASN 40 ENGINEERED MUTATION
SEQADV 4DOH GLN B 134 UNP Q6UXL0 ASN 134 ENGINEERED MUTATION
SEQADV 4DOH GLU B 232 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH GLY B 233 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH ARG B 234 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH ARG R 111 UNP Q9UHF4 LYS 111 ENGINEERED MUTATION
SEQADV 4DOH ARG R 113 UNP Q9UHF4 LYS 113 ENGINEERED MUTATION
SEQADV 4DOH ILE R 246 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH GLU R 247 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH GLY R 248 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH ARG R 249 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH ALA C 24 UNP Q9NYY1 EXPRESSION TAG
SEQADV 4DOH ALA D 29 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH GLN D 40 UNP Q6UXL0 ASN 40 ENGINEERED MUTATION
SEQADV 4DOH GLN D 134 UNP Q6UXL0 ASN 134 ENGINEERED MUTATION
SEQADV 4DOH GLU D 232 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH GLY D 233 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH ARG D 234 UNP Q6UXL0 EXPRESSION TAG
SEQADV 4DOH ARG E 111 UNP Q9UHF4 LYS 111 ENGINEERED MUTATION
SEQADV 4DOH ARG E 113 UNP Q9UHF4 LYS 113 ENGINEERED MUTATION
SEQADV 4DOH ILE E 246 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH GLU E 247 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH GLY E 248 UNP Q9UHF4 EXPRESSION TAG
SEQADV 4DOH ARG E 249 UNP Q9UHF4 EXPRESSION TAG
SEQRES 1 A 153 ALA LEU LYS THR LEU ASN LEU GLY SER CYS VAL ILE ALA
SEQRES 2 A 153 THR ASN LEU GLN GLU ILE ARG ASN GLY PHE SER GLU ILE
SEQRES 3 A 153 ARG GLY SER VAL GLN ALA LYS ASP GLY ASN ILE ASP ILE
SEQRES 4 A 153 ARG ILE LEU ARG ARG THR GLU SER LEU GLN ASP THR LYS
SEQRES 5 A 153 PRO ALA ASN ARG CYS CYS LEU LEU ARG HIS LEU LEU ARG
SEQRES 6 A 153 LEU TYR LEU ASP ARG VAL PHE LYS ASN TYR GLN THR PRO
SEQRES 7 A 153 ASP HIS TYR THR LEU ARG LYS ILE SER SER LEU ALA ASN
SEQRES 8 A 153 SER PHE LEU THR ILE LYS LYS ASP LEU ARG LEU CYS HIS
SEQRES 9 A 153 ALA HIS MET THR CYS HIS CYS GLY GLU GLU ALA MET LYS
SEQRES 10 A 153 LYS TYR SER GLN ILE LEU SER HIS PHE GLU LYS LEU GLU
SEQRES 11 A 153 PRO GLN ALA ALA VAL VAL LYS ALA LEU GLY GLU LEU ASP
SEQRES 12 A 153 ILE LEU LEU GLN TRP MET GLU GLU THR GLU
SEQRES 1 B 206 ALA ASP GLU VAL ALA ILE LEU PRO ALA PRO GLN GLN LEU
SEQRES 2 B 206 SER VAL LEU SER THR ASN MET LYS HIS LEU LEU MET TRP
SEQRES 3 B 206 SER PRO VAL ILE ALA PRO GLY GLU THR VAL TYR TYR SER
SEQRES 4 B 206 VAL GLU TYR GLN GLY GLU TYR GLU SER LEU TYR THR SER
SEQRES 5 B 206 HIS ILE TRP ILE PRO SER SER TRP CYS SER LEU THR GLU
SEQRES 6 B 206 GLY PRO GLU CYS ASP VAL THR ASP ASP ILE THR ALA THR
SEQRES 7 B 206 VAL PRO TYR ASN LEU ARG VAL ARG ALA THR LEU GLY SER
SEQRES 8 B 206 GLN THR SER ALA TRP SER ILE LEU LYS HIS PRO PHE ASN
SEQRES 9 B 206 ARG GLN SER THR ILE LEU THR ARG PRO GLY MET GLU ILE
SEQRES 10 B 206 THR LYS ASP GLY PHE HIS LEU VAL ILE GLU LEU GLU ASP
SEQRES 11 B 206 LEU GLY PRO GLN PHE GLU PHE LEU VAL ALA TYR TRP ARG
SEQRES 12 B 206 ARG GLU PRO GLY ALA GLU GLU HIS VAL LYS MET VAL ARG
SEQRES 13 B 206 SER GLY GLY ILE PRO VAL HIS LEU GLU THR MET GLU PRO
SEQRES 14 B 206 GLY ALA ALA TYR CYS VAL LYS ALA GLN THR PHE VAL LYS
SEQRES 15 B 206 ALA ILE GLY ARG TYR SER ALA PHE SER GLN THR GLU CYS
SEQRES 16 B 206 VAL GLU VAL GLN GLY GLU ALA ILE GLU GLY ARG
SEQRES 1 R 221 ALA VAL PRO CYS VAL SER GLY GLY LEU PRO LYS PRO ALA
SEQRES 2 R 221 ASN ILE THR PHE LEU SER ILE ASN MET LYS ASN VAL LEU
SEQRES 3 R 221 GLN TRP THR PRO PRO GLU GLY LEU GLN GLY VAL LYS VAL
SEQRES 4 R 221 THR TYR THR VAL GLN TYR PHE ILE TYR GLY GLN LYS LYS
SEQRES 5 R 221 TRP LEU ASN LYS SER GLU CYS ARG ASN ILE ASN ARG THR
SEQRES 6 R 221 TYR CYS ASP LEU SER ALA GLU THR SER ASP TYR GLU HIS
SEQRES 7 R 221 GLN TYR TYR ALA ARG VAL ARG ALA ILE TRP GLY THR LYS
SEQRES 8 R 221 CYS SER LYS TRP ALA GLU SER GLY ARG PHE TYR PRO PHE
SEQRES 9 R 221 LEU GLU THR GLN ILE GLY PRO PRO GLU VAL ALA LEU THR
SEQRES 10 R 221 THR ASP GLU LYS SER ILE SER VAL VAL LEU THR ALA PRO
SEQRES 11 R 221 GLU LYS TRP LYS ARG ASN PRO GLU ASP LEU PRO VAL SER
SEQRES 12 R 221 MET GLN GLN ILE TYR SER ASN LEU LYS TYR ASN VAL SER
SEQRES 13 R 221 VAL LEU ASN THR LYS SER ASN ARG THR TRP SER GLN CYS
SEQRES 14 R 221 VAL THR ASN HIS THR LEU VAL LEU THR TRP LEU GLU PRO
SEQRES 15 R 221 ASN THR LEU TYR CYS VAL HIS VAL GLU SER PHE VAL PRO
SEQRES 16 R 221 GLY PRO PRO ARG ARG ALA GLN PRO SER GLU LYS GLN CYS
SEQRES 17 R 221 ALA ARG THR LEU LYS ASP GLN SER SER ILE GLU GLY ARG
SEQRES 1 C 153 ALA LEU LYS THR LEU ASN LEU GLY SER CYS VAL ILE ALA
SEQRES 2 C 153 THR ASN LEU GLN GLU ILE ARG ASN GLY PHE SER GLU ILE
SEQRES 3 C 153 ARG GLY SER VAL GLN ALA LYS ASP GLY ASN ILE ASP ILE
SEQRES 4 C 153 ARG ILE LEU ARG ARG THR GLU SER LEU GLN ASP THR LYS
SEQRES 5 C 153 PRO ALA ASN ARG CYS CYS LEU LEU ARG HIS LEU LEU ARG
SEQRES 6 C 153 LEU TYR LEU ASP ARG VAL PHE LYS ASN TYR GLN THR PRO
SEQRES 7 C 153 ASP HIS TYR THR LEU ARG LYS ILE SER SER LEU ALA ASN
SEQRES 8 C 153 SER PHE LEU THR ILE LYS LYS ASP LEU ARG LEU CYS HIS
SEQRES 9 C 153 ALA HIS MET THR CYS HIS CYS GLY GLU GLU ALA MET LYS
SEQRES 10 C 153 LYS TYR SER GLN ILE LEU SER HIS PHE GLU LYS LEU GLU
SEQRES 11 C 153 PRO GLN ALA ALA VAL VAL LYS ALA LEU GLY GLU LEU ASP
SEQRES 12 C 153 ILE LEU LEU GLN TRP MET GLU GLU THR GLU
SEQRES 1 D 206 ALA ASP GLU VAL ALA ILE LEU PRO ALA PRO GLN GLN LEU
SEQRES 2 D 206 SER VAL LEU SER THR ASN MET LYS HIS LEU LEU MET TRP
SEQRES 3 D 206 SER PRO VAL ILE ALA PRO GLY GLU THR VAL TYR TYR SER
SEQRES 4 D 206 VAL GLU TYR GLN GLY GLU TYR GLU SER LEU TYR THR SER
SEQRES 5 D 206 HIS ILE TRP ILE PRO SER SER TRP CYS SER LEU THR GLU
SEQRES 6 D 206 GLY PRO GLU CYS ASP VAL THR ASP ASP ILE THR ALA THR
SEQRES 7 D 206 VAL PRO TYR ASN LEU ARG VAL ARG ALA THR LEU GLY SER
SEQRES 8 D 206 GLN THR SER ALA TRP SER ILE LEU LYS HIS PRO PHE ASN
SEQRES 9 D 206 ARG GLN SER THR ILE LEU THR ARG PRO GLY MET GLU ILE
SEQRES 10 D 206 THR LYS ASP GLY PHE HIS LEU VAL ILE GLU LEU GLU ASP
SEQRES 11 D 206 LEU GLY PRO GLN PHE GLU PHE LEU VAL ALA TYR TRP ARG
SEQRES 12 D 206 ARG GLU PRO GLY ALA GLU GLU HIS VAL LYS MET VAL ARG
SEQRES 13 D 206 SER GLY GLY ILE PRO VAL HIS LEU GLU THR MET GLU PRO
SEQRES 14 D 206 GLY ALA ALA TYR CYS VAL LYS ALA GLN THR PHE VAL LYS
SEQRES 15 D 206 ALA ILE GLY ARG TYR SER ALA PHE SER GLN THR GLU CYS
SEQRES 16 D 206 VAL GLU VAL GLN GLY GLU ALA ILE GLU GLY ARG
SEQRES 1 E 221 ALA VAL PRO CYS VAL SER GLY GLY LEU PRO LYS PRO ALA
SEQRES 2 E 221 ASN ILE THR PHE LEU SER ILE ASN MET LYS ASN VAL LEU
SEQRES 3 E 221 GLN TRP THR PRO PRO GLU GLY LEU GLN GLY VAL LYS VAL
SEQRES 4 E 221 THR TYR THR VAL GLN TYR PHE ILE TYR GLY GLN LYS LYS
SEQRES 5 E 221 TRP LEU ASN LYS SER GLU CYS ARG ASN ILE ASN ARG THR
SEQRES 6 E 221 TYR CYS ASP LEU SER ALA GLU THR SER ASP TYR GLU HIS
SEQRES 7 E 221 GLN TYR TYR ALA ARG VAL ARG ALA ILE TRP GLY THR LYS
SEQRES 8 E 221 CYS SER LYS TRP ALA GLU SER GLY ARG PHE TYR PRO PHE
SEQRES 9 E 221 LEU GLU THR GLN ILE GLY PRO PRO GLU VAL ALA LEU THR
SEQRES 10 E 221 THR ASP GLU LYS SER ILE SER VAL VAL LEU THR ALA PRO
SEQRES 11 E 221 GLU LYS TRP LYS ARG ASN PRO GLU ASP LEU PRO VAL SER
SEQRES 12 E 221 MET GLN GLN ILE TYR SER ASN LEU LYS TYR ASN VAL SER
SEQRES 13 E 221 VAL LEU ASN THR LYS SER ASN ARG THR TRP SER GLN CYS
SEQRES 14 E 221 VAL THR ASN HIS THR LEU VAL LEU THR TRP LEU GLU PRO
SEQRES 15 E 221 ASN THR LEU TYR CYS VAL HIS VAL GLU SER PHE VAL PRO
SEQRES 16 E 221 GLY PRO PRO ARG ARG ALA GLN PRO SER GLU LYS GLN CYS
SEQRES 17 E 221 ALA ARG THR LEU LYS ASP GLN SER SER ILE GLU GLY ARG
HET NAG B 301 14
HET NAG R 301 14
HET NAG R 302 14
HET NAG D 301 14
HET NAG E 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 7 NAG 5(C8 H15 N O6)
FORMUL 12 HOH *57(H2 O)
HELIX 1 1 ASN A 38 GLU A 48 1 11
HELIX 2 2 ILE A 49 LYS A 56 1 8
HELIX 3 3 LYS A 75 VAL A 94 1 20
HELIX 4 4 PHE A 95 TYR A 98 5 4
HELIX 5 5 ASP A 102 HIS A 129 1 28
HELIX 6 6 GLY A 135 LEU A 152 1 18
HELIX 7 7 GLU A 153 GLY A 163 1 11
HELIX 8 8 GLU A 164 THR A 175 1 12
HELIX 9 9 GLU B 73 THR B 79 1 7
HELIX 10 10 ASN B 132 THR B 136 5 5
HELIX 11 11 LYS B 210 GLY B 213 5 4
HELIX 12 12 SER R 85 ARG R 88 5 4
HELIX 13 13 TYR R 130 THR R 135 1 6
HELIX 14 14 SER R 171 TYR R 176 1 6
HELIX 15 15 ASN C 38 LYS C 56 1 19
HELIX 16 16 LYS C 75 VAL C 94 1 20
HELIX 17 17 ASP C 102 HIS C 129 1 28
HELIX 18 18 GLY C 135 LEU C 152 1 18
HELIX 19 19 GLU C 153 GLU C 164 1 12
HELIX 20 20 GLU C 164 GLU C 174 1 11
HELIX 21 21 GLY D 72 THR D 79 1 8
HELIX 22 22 ASN D 132 THR D 136 5 5
HELIX 23 23 SER E 85 ARG E 88 5 4
HELIX 24 24 TYR E 130 THR E 135 1 6
HELIX 25 25 SER E 171 TYR E 176 1 6
SHEET 1 A 2 LYS A 26 LEU A 30 0
SHEET 2 A 2 CYS A 33 THR A 37 -1 O THR A 37 N LYS A 26
SHEET 1 B 3 SER B 42 THR B 46 0
SHEET 2 B 3 LYS B 49 MET B 53 -1 O LEU B 51 N LEU B 44
SHEET 3 B 3 GLU B 96 ASP B 98 -1 O CYS B 97 N LEU B 52
SHEET 1 C 4 ILE B 84 THR B 92 0
SHEET 2 C 4 TYR B 65 GLY B 72 -1 N TYR B 70 O ILE B 84
SHEET 3 C 4 TYR B 109 LEU B 117 -1 O ASN B 110 N GLN B 71
SHEET 4 C 4 GLN B 120 THR B 121 -1 O GLN B 120 N LEU B 117
SHEET 1 D 4 ILE B 84 THR B 92 0
SHEET 2 D 4 TYR B 65 GLY B 72 -1 N TYR B 70 O ILE B 84
SHEET 3 D 4 TYR B 109 LEU B 117 -1 O ASN B 110 N GLN B 71
SHEET 4 D 4 SER B 125 ILE B 126 -1 O SER B 125 N VAL B 113
SHEET 1 E 3 MET B 143 ASP B 148 0
SHEET 2 E 3 HIS B 151 LEU B 156 -1 O VAL B 153 N THR B 146
SHEET 3 E 3 PRO B 189 THR B 194 -1 O VAL B 190 N ILE B 154
SHEET 1 F 4 HIS B 179 VAL B 183 0
SHEET 2 F 4 GLU B 164 ARG B 171 -1 N VAL B 167 O LYS B 181
SHEET 3 F 4 TYR B 201 VAL B 209 -1 O GLN B 206 N LEU B 166
SHEET 4 F 4 ARG B 214 TYR B 215 -1 O ARG B 214 N VAL B 209
SHEET 1 G 4 HIS B 179 VAL B 183 0
SHEET 2 G 4 GLU B 164 ARG B 171 -1 N VAL B 167 O LYS B 181
SHEET 3 G 4 TYR B 201 VAL B 209 -1 O GLN B 206 N LEU B 166
SHEET 4 G 4 GLU B 222 VAL B 224 -1 O GLU B 222 N VAL B 203
SHEET 1 H 3 ALA R 41 ILE R 48 0
SHEET 2 H 3 LYS R 51 THR R 57 -1 O THR R 57 N ALA R 41
SHEET 3 H 3 TYR R 94 ASP R 96 -1 O CYS R 95 N LEU R 54
SHEET 1 I 4 LEU R 82 ASN R 83 0
SHEET 2 I 4 THR R 68 ILE R 75 -1 N TYR R 73 O LEU R 82
SHEET 3 I 4 TYR R 108 ILE R 115 -1 O ARG R 111 N GLN R 72
SHEET 4 I 4 ALA R 124 GLU R 125 -1 O ALA R 124 N VAL R 112
SHEET 1 J 3 GLU R 141 THR R 145 0
SHEET 2 J 3 ILE R 151 THR R 156 -1 O SER R 152 N THR R 145
SHEET 3 J 3 THR R 202 LEU R 205 -1 O LEU R 205 N ILE R 151
SHEET 1 K 4 ARG R 192 VAL R 198 0
SHEET 2 K 4 LYS R 180 ASN R 187 -1 N VAL R 183 O GLN R 196
SHEET 3 K 4 LEU R 213 PHE R 221 -1 O CYS R 215 N LEU R 186
SHEET 4 K 4 GLU R 233 ARG R 238 -1 O ALA R 237 N TYR R 214
SHEET 1 L 2 LYS C 26 LEU C 30 0
SHEET 2 L 2 CYS C 33 THR C 37 -1 O ILE C 35 N LEU C 28
SHEET 1 M 3 GLN D 39 THR D 46 0
SHEET 2 M 3 LYS D 49 SER D 55 -1 O SER D 55 N GLN D 39
SHEET 3 M 3 GLU D 96 ASP D 98 -1 O CYS D 97 N LEU D 52
SHEET 1 N 4 ILE D 84 THR D 92 0
SHEET 2 N 4 TYR D 65 GLN D 71 -1 N TYR D 70 O ILE D 84
SHEET 3 N 4 ASN D 110 LEU D 117 -1 O ARG D 112 N GLU D 69
SHEET 4 N 4 GLN D 120 THR D 121 -1 N GLN D 120 O LEU D 117
SHEET 1 O 4 ILE D 84 THR D 92 0
SHEET 2 O 4 TYR D 65 GLN D 71 -1 N TYR D 70 O ILE D 84
SHEET 3 O 4 ASN D 110 LEU D 117 -1 O ARG D 112 N GLU D 69
SHEET 4 O 4 SER D 125 ILE D 126 -1 O SER D 125 N VAL D 113
SHEET 1 P 3 MET D 143 ASP D 148 0
SHEET 2 P 3 HIS D 151 LEU D 156 -1 O HIS D 151 N ASP D 148
SHEET 3 P 3 VAL D 190 THR D 194 -1 O VAL D 190 N ILE D 154
SHEET 1 Q 4 HIS D 179 VAL D 183 0
SHEET 2 Q 4 GLU D 164 ARG D 171 -1 N VAL D 167 O LYS D 181
SHEET 3 Q 4 TYR D 201 PHE D 208 -1 O LYS D 204 N ALA D 168
SHEET 4 Q 4 GLU D 222 VAL D 224 -1 O GLU D 222 N VAL D 203
SHEET 1 R 3 ALA E 41 ILE E 48 0
SHEET 2 R 3 LYS E 51 THR E 57 -1 O THR E 57 N ALA E 41
SHEET 3 R 3 TYR E 94 ASP E 96 -1 O CYS E 95 N LEU E 54
SHEET 1 S 4 LEU E 82 ASN E 83 0
SHEET 2 S 4 THR E 68 ILE E 75 -1 N TYR E 73 O LEU E 82
SHEET 3 S 4 TYR E 108 ILE E 115 -1 O ILE E 115 N THR E 68
SHEET 4 S 4 ALA E 124 GLU E 125 -1 O ALA E 124 N VAL E 112
SHEET 1 T 3 GLU E 141 THR E 146 0
SHEET 2 T 3 ILE E 151 THR E 156 -1 O SER E 152 N THR E 145
SHEET 3 T 3 THR E 202 LEU E 205 -1 O LEU E 205 N ILE E 151
SHEET 1 U 4 ARG E 192 VAL E 198 0
SHEET 2 U 4 LYS E 180 ASN E 187 -1 N VAL E 185 O TRP E 194
SHEET 3 U 4 LEU E 213 PHE E 221 -1 O GLU E 219 N ASN E 182
SHEET 4 U 4 GLN E 235 ARG E 238 -1 O GLN E 235 N VAL E 216
SSBOND 1 CYS A 33 CYS A 126 1555 1555 2.05
SSBOND 2 CYS A 80 CYS A 132 1555 1555 2.04
SSBOND 3 CYS A 81 CYS A 134 1555 1555 2.04
SSBOND 4 CYS B 89 CYS B 97 1555 1555 2.04
SSBOND 5 CYS B 202 CYS B 223 1555 1555 2.05
SSBOND 6 CYS R 87 CYS R 95 1555 1555 2.04
SSBOND 7 CYS R 215 CYS R 236 1555 1555 2.04
SSBOND 8 CYS C 33 CYS C 126 1555 1555 2.05
SSBOND 9 CYS C 80 CYS C 132 1555 1555 2.04
SSBOND 10 CYS C 81 CYS C 134 1555 1555 2.05
SSBOND 11 CYS D 89 CYS D 97 1555 1555 2.03
SSBOND 12 CYS D 202 CYS D 223 1555 1555 2.04
SSBOND 13 CYS E 87 CYS E 95 1555 1555 2.05
SSBOND 14 CYS E 215 CYS E 236 1555 1555 2.04
CRYST1 103.115 111.764 136.334 90.00 90.00 90.00 P 21 21 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 0.009698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END