HEADER HORMONE/GROWTH FACTOR 09-MAY-06 2GYR
TITLE CRYSTAL STRUCTURE OF HUMAN ARTEMIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTROPHIC FACTOR ARTEMIN, ISOFORM 3;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: N-TERMINAL TRUNCATED;
COMPND 5 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: ARTN;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS NEUROTROPHIC FACTOR, CYSTEIN-KNOT, HORMONE/GROWTH FACTOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.Q.WANG
REVDAT 2 24-FEB-09 2GYR 1 VERSN
REVDAT 1 27-JUN-06 2GYR 0
JRNL AUTH X.WANG,R.H.BALOH,J.MILBRANDT,K.C.GARCIA
JRNL TITL STRUCTURE OF ARTEMIN COMPLEXED WITH ITS RECEPTOR
JRNL TITL 2 GFRALPHA3: CONVERGENT RECOGNITION OF GLIAL CELL
JRNL TITL 3 LINE-DERIVED NEUROTROPHIC FACTORS.
JRNL REF STRUCTURE V. 14 1083 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16765900
JRNL DOI 10.1016/J.STR.2006.05.010
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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 : 31882
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) : 0.308
REMARK 3 FREE R VALUE : 0.353
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3169
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 : 4410
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : 0.47
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.53
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.09
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 2GYR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037713.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-
REMARK 200 ROOT I-BEAM SINGLE CRYSTAL;
REMARK 200 ASYMMETRIC CUT 4.965 DEGS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33810
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: SIRAS
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-16% PEG3350, 0.1 M HEPES (PH
REMARK 280 7.5), 0.1 M MAGNESIUM CHLORIDE, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 146.13333
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 73.06667
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 109.60000
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 36.53333
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 182.66667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 350
REMARK 350 BIOMOLECULE: 3
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: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 LEU A 101
REMARK 465 GLY A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 LEU B 101
REMARK 465 GLY B 102
REMARK 465 HIS B 103
REMARK 465 HIS B 104
REMARK 465 HIS B 105
REMARK 465 HIS B 106
REMARK 465 HIS B 107
REMARK 465 HIS B 108
REMARK 465 LEU C 101
REMARK 465 GLY C 102
REMARK 465 HIS C 103
REMARK 465 HIS C 104
REMARK 465 HIS C 105
REMARK 465 HIS C 106
REMARK 465 HIS C 107
REMARK 465 HIS C 108
REMARK 465 LEU D 101
REMARK 465 GLY D 102
REMARK 465 HIS D 103
REMARK 465 HIS D 104
REMARK 465 HIS D 105
REMARK 465 HIS D 106
REMARK 465 HIS D 107
REMARK 465 HIS D 108
REMARK 465 LEU E 101
REMARK 465 GLY E 102
REMARK 465 HIS E 103
REMARK 465 HIS E 104
REMARK 465 HIS E 105
REMARK 465 HIS E 106
REMARK 465 HIS E 107
REMARK 465 HIS E 108
REMARK 465 LEU F 101
REMARK 465 GLY F 102
REMARK 465 HIS F 103
REMARK 465 HIS F 104
REMARK 465 HIS F 105
REMARK 465 HIS F 106
REMARK 465 HIS F 107
REMARK 465 HIS F 108
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 OG SER A 79 OE1 GLU B 76 5555 2.15
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 ARG A 15 3.30 -65.87
REMARK 500 LEU A 19 20.79 -76.77
REMARK 500 SER A 23 139.42 171.62
REMARK 500 GLU A 25 116.39 -163.96
REMARK 500 ARG A 37 -14.44 -47.52
REMARK 500 ASP A 82 -162.77 -75.26
REMARK 500 ALA A 97 147.71 -171.92
REMARK 500 LEU B 19 19.10 -144.03
REMARK 500 SER B 23 135.71 -176.56
REMARK 500 PRO B 58 108.98 -42.92
REMARK 500 ASP C 24 32.55 -91.14
REMARK 500 SER C 66 32.66 -99.99
REMARK 500 ASP D 24 49.26 -73.93
REMARK 500 SER D 33 148.17 -172.89
REMARK 500 PRO D 58 115.71 -28.35
REMARK 500 GLN D 67 161.80 178.63
REMARK 500 ARG D 92 14.18 56.80
REMARK 500 CYS E 5 103.50 30.79
REMARK 500 SER E 23 134.67 158.86
REMARK 500 ARG E 74 155.70 178.88
REMARK 500 ARG E 92 21.94 43.96
REMARK 500 ASP F 24 38.19 -98.53
REMARK 500 ARG F 37 -8.89 -46.81
REMARK 500 PRO F 60 99.49 -58.10
REMARK 500 ARG F 74 146.56 158.60
REMARK 500 ASP F 82 -168.46 -70.63
REMARK 500 VAL F 83 -70.07 -50.63
REMARK 500 ASN F 84 32.64 -71.91
REMARK 500 ARG F 92 87.00 36.21
REMARK 500 LEU F 93 -26.36 -140.71
REMARK 500 ALA F 97 144.43 -178.22
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GYR A 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
DBREF 2GYR B 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
DBREF 2GYR C 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
DBREF 2GYR D 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
DBREF 2GYR E 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
DBREF 2GYR F 4 102 UNP Q5T4W7 ARTN_HUMAN 122 220
SEQADV 2GYR HIS A 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS A 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS A 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS A 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS A 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS A 108 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS B 108 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS C 108 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS D 108 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS E 108 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 103 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 104 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 105 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 106 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 107 UNP Q5T4W7 EXPRESSION TAG
SEQADV 2GYR HIS F 108 UNP Q5T4W7 EXPRESSION TAG
SEQRES 1 A 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 A 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 A 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 A 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 A 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 A 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 A 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 A 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 A 105 HIS
SEQRES 1 B 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 B 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 B 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 B 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 B 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 B 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 B 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 B 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 B 105 HIS
SEQRES 1 C 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 C 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 C 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 C 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 C 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 C 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 C 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 C 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 C 105 HIS
SEQRES 1 D 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 D 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 D 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 D 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 D 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 D 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 D 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 D 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 D 105 HIS
SEQRES 1 E 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 E 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 E 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 E 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 E 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 E 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 E 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 E 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 E 105 HIS
SEQRES 1 F 105 GLY CYS ARG LEU ARG SER GLN LEU VAL PRO VAL ARG ALA
SEQRES 2 F 105 LEU GLY LEU GLY HIS ARG SER ASP GLU LEU VAL ARG PHE
SEQRES 3 F 105 ARG PHE CYS SER GLY SER CYS ARG ARG ALA ARG SER PRO
SEQRES 4 F 105 HIS ASP LEU SER LEU ALA SER LEU LEU GLY ALA GLY ALA
SEQRES 5 F 105 LEU ARG PRO PRO PRO GLY SER ARG PRO VAL SER GLN PRO
SEQRES 6 F 105 CYS CYS ARG PRO THR ARG TYR GLU ALA VAL SER PHE MET
SEQRES 7 F 105 ASP VAL ASN SER THR TRP ARG THR VAL ASP ARG LEU SER
SEQRES 8 F 105 ALA THR ALA CYS GLY CYS LEU GLY HIS HIS HIS HIS HIS
SEQRES 9 F 105 HIS
HELIX 1 1 ARG A 15 LEU A 17 5 3
HELIX 2 2 CYS A 36 ARG A 40 5 5
HELIX 3 3 SER A 41 GLY A 52 1 12
HELIX 4 4 ARG B 15 GLY B 18 5 4
HELIX 5 5 SER B 41 ALA B 53 1 13
HELIX 6 6 ARG C 15 LEU C 17 5 3
HELIX 7 7 CYS C 36 ARG C 40 5 5
HELIX 8 8 SER C 41 ALA C 53 1 13
HELIX 9 9 ARG D 15 GLY D 18 5 4
HELIX 10 10 SER D 41 ALA D 53 1 13
HELIX 11 11 ARG E 15 LEU E 17 5 3
HELIX 12 12 CYS E 36 ARG E 40 5 5
HELIX 13 13 SER E 41 GLY E 52 1 12
HELIX 14 14 SER F 41 ALA F 53 1 13
SHEET 1 A 2 ARG A 6 PRO A 13 0
SHEET 2 A 2 LEU A 26 SER A 33 -1 O PHE A 31 N ARG A 8
SHEET 1 B 2 ARG A 71 MET A 81 0
SHEET 2 B 2 TRP A 87 GLY A 99 -1 O SER A 94 N GLU A 76
SHEET 1 C 2 ARG B 6 PRO B 13 0
SHEET 2 C 2 LEU B 26 SER B 33 -1 O PHE B 31 N ARG B 8
SHEET 1 D 2 ARG B 71 MET B 81 0
SHEET 2 D 2 TRP B 87 GLY B 99 -1 O ALA B 97 N THR B 73
SHEET 1 E 2 ARG C 6 PRO C 13 0
SHEET 2 E 2 LEU C 26 SER C 33 -1 O PHE C 31 N ARG C 8
SHEET 1 F 2 ARG C 71 SER C 79 0
SHEET 2 F 2 THR C 89 GLY C 99 -1 O ALA C 97 N THR C 73
SHEET 1 G 2 ARG D 6 PRO D 13 0
SHEET 2 G 2 LEU D 26 SER D 33 -1 O PHE D 31 N ARG D 8
SHEET 1 H 2 ARG D 71 MET D 81 0
SHEET 2 H 2 TRP D 87 GLY D 99 -1 O VAL D 90 N VAL D 78
SHEET 1 I 2 ARG E 6 PRO E 13 0
SHEET 2 I 2 LEU E 26 SER E 33 -1 O PHE E 31 N ARG E 8
SHEET 1 J 2 ARG E 71 PRO E 72 0
SHEET 2 J 2 CYS E 98 GLY E 99 -1 O GLY E 99 N ARG E 71
SHEET 1 K 2 TYR E 75 MET E 81 0
SHEET 2 K 2 TRP E 87 ALA E 95 -1 O ARG E 88 N PHE E 80
SHEET 1 L 2 ARG F 6 PRO F 13 0
SHEET 2 L 2 LEU F 26 SER F 33 -1 O PHE F 31 N ARG F 8
SHEET 1 M 2 ARG F 71 PRO F 72 0
SHEET 2 M 2 CYS F 98 GLY F 99 -1 O GLY F 99 N ARG F 71
SHEET 1 N 2 TYR F 75 MET F 81 0
SHEET 2 N 2 TRP F 87 ALA F 95 -1 O SER F 94 N GLU F 76
SSBOND 1 CYS A 5 CYS A 70 1555 1555 2.04
SSBOND 2 CYS A 32 CYS A 98 1555 1555 2.02
SSBOND 3 CYS A 36 CYS A 100 1555 1555 2.04
SSBOND 4 CYS A 69 CYS B 69 1555 1555 2.03
SSBOND 5 CYS B 5 CYS B 70 1555 1555 2.05
SSBOND 6 CYS B 32 CYS B 98 1555 1555 2.02
SSBOND 7 CYS B 36 CYS B 100 1555 1555 2.04
SSBOND 8 CYS C 5 CYS C 70 1555 1555 2.04
SSBOND 9 CYS C 32 CYS C 98 1555 1555 2.03
SSBOND 10 CYS C 36 CYS C 100 1555 1555 2.05
SSBOND 11 CYS C 69 CYS D 69 1555 1555 2.03
SSBOND 12 CYS D 5 CYS D 70 1555 1555 2.04
SSBOND 13 CYS D 32 CYS D 98 1555 1555 2.03
SSBOND 14 CYS D 36 CYS D 100 1555 1555 2.04
SSBOND 15 CYS E 5 CYS E 70 1555 1555 2.04
SSBOND 16 CYS E 32 CYS E 98 1555 1555 2.02
SSBOND 17 CYS E 36 CYS E 100 1555 1555 2.03
SSBOND 18 CYS E 69 CYS F 69 1555 1555 2.02
SSBOND 19 CYS F 5 CYS F 70 1555 1555 2.04
SSBOND 20 CYS F 32 CYS F 98 1555 1555 2.03
SSBOND 21 CYS F 36 CYS F 100 1555 1555 2.05
CRYST1 94.200 94.200 219.200 90.00 90.00 120.00 P 65 36
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 0.010616 0.006129 0.000000 0.00000
SCALE2 0.000000 0.012258 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004562 0.00000
(ATOM LINES ARE NOT SHOWN.)
END