HEADER GROWTH FACTOR 25-MAR-97 1AGQ
TITLE GLIAL CELL-DERIVED NEUROTROPHIC FACTOR FROM RAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLIAL CELL-DERIVED NEUROTROPHIC FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GDNF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELL: GLIA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GROWTH FACTOR, NEUROTROPHIC FACTOR, CYSTINE KNOT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,N.GERBER
REVDAT 2 24-FEB-09 1AGQ 1 VERSN
REVDAT 1 05-JUN-97 1AGQ 0
JRNL AUTH C.EIGENBROT,N.GERBER
JRNL TITL X-RAY STRUCTURE OF GLIAL CELL-DERIVED NEUROTROPHIC
JRNL TITL 2 FACTOR AT 1.9 A RESOLUTION AND IMPLICATIONS FOR
JRNL TITL 3 RECEPTOR BINDING.
JRNL REF NAT.STRUCT.BIOL. V. 4 435 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9187648
JRNL DOI 10.1038/NSB0697-435
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.D.SUN,D.R.DAVIES
REMARK 1 TITL THE CYSTINE-KNOT GROWTH-FACTOR SUPERFAMILY
REMARK 1 REF ANNU.REV.BIOPHYS.BIOMOL. V. 24 269 1995
REMARK 1 REF 2 STRUCT.
REMARK 1 REFN ISSN 1056-8700
REMARK 1 REFERENCE 2
REMARK 1 AUTH L.F.LIN,D.H.DOHERTY,J.D.LILE,S.BEKTESH,F.COLLINS
REMARK 1 TITL A GLIAL CELL LINE-DERIVED NEUROTROPHIC FACTOR FOR
REMARK 1 TITL 2 MIDBRAIN DOPAMINERGIC NEURONS
REMARK 1 REF SCIENCE V. 260 1130 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 43042
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 SET) : 0.203
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 4402
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3258
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 347
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2941
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 285
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.47
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.050 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.980 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.170 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.100 ; 9.000
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESOLUTION-DEPENDENT WEIGHTING
REMARK 3 SCHEME USED. BULK SOLVENT MODEL USED. THERE ARE 139 ATOMS
REMARK 3 ASSIGNED ZERO OCCUPANCY. SOME OF THESE WERE USED WITH UNIT
REMARK 3 OCCUPANCY AT SOME STAGE OF REFINEMENT, BUT ARE NOW ASSIGNED
REMARK 3 ZERO OCCUPANCY. THE SEGMENT C 116 - C 120 IS POORLY MODELED
REMARK 3 USING A SINGLE MAIN CHAIN CONFORMATION. THERE IS RESIDUAL
REMARK 3 ELECTRON DENSITY SUGGESTING ADDITIONAL CONFORMATION(S), BUT NO
REMARK 3 ATTEMPT TO MODEL THEM HAS BEEN MADE. ALL RESIDUE NUMBERS IN
REMARK 3 THIS ENTRY ARE GREATER (BY ONE) THAN THOSE USED IN THE JOURNAL
REMARK 3 ARTICLE DESCRIBING THIS WORK (JRNL RECORD).
REMARK 4
REMARK 4 1AGQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : FEB-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46219
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: XSIGHT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.8 M LICL, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.77500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 ASP A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 ARG A 12
REMARK 465 ARG A 13
REMARK 465 GLU A 14
REMARK 465 ARG A 15
REMARK 465 ASN A 16
REMARK 465 ARG A 17
REMARK 465 GLN A 18
REMARK 465 ALA A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 SER A 23
REMARK 465 PRO A 24
REMARK 465 GLU A 25
REMARK 465 ASN A 26
REMARK 465 SER A 27
REMARK 465 ARG A 28
REMARK 465 GLY A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 ARG A 32
REMARK 465 ARG A 33
REMARK 465 GLY A 34
REMARK 465 GLN A 35
REMARK 465 ARG A 36
REMARK 465 GLY A 37
REMARK 465 LYS A 38
REMARK 465 ARG A 92
REMARK 465 LEU A 93
REMARK 465 THR A 94
REMARK 465 SER A 95
REMARK 465 ASP A 96
REMARK 465 LYS A 97
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PRO B 3
REMARK 465 ASP B 4
REMARK 465 LYS B 5
REMARK 465 GLN B 6
REMARK 465 ALA B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 LEU B 10
REMARK 465 PRO B 11
REMARK 465 ARG B 12
REMARK 465 ARG B 13
REMARK 465 GLU B 14
REMARK 465 ARG B 15
REMARK 465 ASN B 16
REMARK 465 ARG B 17
REMARK 465 GLN B 18
REMARK 465 ALA B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 SER B 23
REMARK 465 PRO B 24
REMARK 465 GLU B 25
REMARK 465 ASN B 26
REMARK 465 SER B 27
REMARK 465 ARG B 28
REMARK 465 GLY B 29
REMARK 465 LYS B 30
REMARK 465 GLY B 31
REMARK 465 ARG B 32
REMARK 465 ARG B 33
REMARK 465 GLY B 34
REMARK 465 GLN B 35
REMARK 465 ARG B 36
REMARK 465 GLY B 37
REMARK 465 ASP B 96
REMARK 465 LYS B 97
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PRO C 3
REMARK 465 ASP C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 ALA C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 LEU C 10
REMARK 465 PRO C 11
REMARK 465 ARG C 12
REMARK 465 ARG C 13
REMARK 465 GLU C 14
REMARK 465 ARG C 15
REMARK 465 ASN C 16
REMARK 465 ARG C 17
REMARK 465 GLN C 18
REMARK 465 ALA C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 ALA C 22
REMARK 465 SER C 23
REMARK 465 PRO C 24
REMARK 465 GLU C 25
REMARK 465 ASN C 26
REMARK 465 SER C 27
REMARK 465 ARG C 28
REMARK 465 GLY C 29
REMARK 465 LYS C 30
REMARK 465 GLY C 31
REMARK 465 ARG C 32
REMARK 465 ARG C 33
REMARK 465 GLY C 34
REMARK 465 GLN C 35
REMARK 465 ARG C 36
REMARK 465 GLY C 37
REMARK 465 LYS C 38
REMARK 465 ASN C 39
REMARK 465 ARG C 40
REMARK 465 THR C 94
REMARK 465 SER C 95
REMARK 465 ASP C 96
REMARK 465 LYS C 97
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 PRO D 3
REMARK 465 ASP D 4
REMARK 465 LYS D 5
REMARK 465 GLN D 6
REMARK 465 ALA D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 LEU D 10
REMARK 465 PRO D 11
REMARK 465 ARG D 12
REMARK 465 ARG D 13
REMARK 465 GLU D 14
REMARK 465 ARG D 15
REMARK 465 ASN D 16
REMARK 465 ARG D 17
REMARK 465 GLN D 18
REMARK 465 ALA D 19
REMARK 465 ALA D 20
REMARK 465 ALA D 21
REMARK 465 ALA D 22
REMARK 465 SER D 23
REMARK 465 PRO D 24
REMARK 465 GLU D 25
REMARK 465 ASN D 26
REMARK 465 SER D 27
REMARK 465 ARG D 28
REMARK 465 GLY D 29
REMARK 465 LYS D 30
REMARK 465 GLY D 31
REMARK 465 ARG D 32
REMARK 465 ARG D 33
REMARK 465 GLY D 34
REMARK 465 GLN D 35
REMARK 465 ARG D 36
REMARK 465 GLY D 37
REMARK 465 LYS D 38
REMARK 465 ASN D 39
REMARK 465 ARG D 40
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASP D 96
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 61 CG CD CE NZ
REMARK 480 SER A 72 OG
REMARK 480 GLU A 74 CG CD OE1 OE2
REMARK 480 LYS A 85 CG CD CE NZ
REMARK 480 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 480 VAL A 98 CB CG1 CG2
REMARK 480 ARG A 125 NE CZ NH1 NH2
REMARK 480 LYS A 130 NZ
REMARK 480 LYS B 38 CG CD CE NZ
REMARK 480 GLU B 59 CG CD OE1 OE2
REMARK 480 LYS B 61 CG CD CE NZ
REMARK 480 SER B 72 OG
REMARK 480 GLU B 74 CG CD OE1 OE2
REMARK 480 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 480 THR B 94 CA
REMARK 480 SER B 95 OG
REMARK 480 VAL B 98 CG1 CG2
REMARK 480 LYS B 126 CE NZ
REMARK 480 GLU C 59 CG CD OE1 OE2
REMARK 480 LYS C 61 CG CD CE NZ
REMARK 480 GLU C 74 CD OE1 OE2
REMARK 480 GLU C 77 CG CD OE1 OE2
REMARK 480 LYS C 82 CD CE NZ
REMARK 480 LYS C 85 CG CD CE NZ
REMARK 480 SER C 88 OG
REMARK 480 ARG C 89 NE CZ NH1 NH2
REMARK 480 ARG C 91 CG CD NE CZ NH1 NH2
REMARK 480 ARG C 92 CG CD NE CZ NH1 NH2
REMARK 480 GLU D 59 CG CD OE1 OE2
REMARK 480 LYS D 61 CG CD CE NZ
REMARK 480 GLU D 77 CG CD OE1 OE2
REMARK 480 LYS D 82 CG CD CE NZ
REMARK 480 LYS D 85 CG CD CE NZ
REMARK 480 ARG D 89 CG CD NE CZ NH1 NH2
REMARK 480 LYS D 97 CG CD CE NZ
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 89 -8.14 -58.29
REMARK 500 LEU B 93 94.58 -162.52
REMARK 500 ARG C 91 19.54 58.22
REMARK 500 ASP C 117 38.00 -87.89
REMARK 500 SER D 95 131.82 -39.83
REMARK 500 ASP D 96 -87.26 -19.08
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AGQ A 2 135 UNP Q07731 GDNF_RAT 78 211
DBREF 1AGQ B 2 135 UNP Q07731 GDNF_RAT 78 211
DBREF 1AGQ C 2 135 UNP Q07731 GDNF_RAT 78 211
DBREF 1AGQ D 2 135 UNP Q07731 GDNF_RAT 78 211
SEQRES 1 A 135 MET SER PRO ASP LYS GLN ALA ALA ALA LEU PRO ARG ARG
SEQRES 2 A 135 GLU ARG ASN ARG GLN ALA ALA ALA ALA SER PRO GLU ASN
SEQRES 3 A 135 SER ARG GLY LYS GLY ARG ARG GLY GLN ARG GLY LYS ASN
SEQRES 4 A 135 ARG GLY CYS VAL LEU THR ALA ILE HIS LEU ASN VAL THR
SEQRES 5 A 135 ASP LEU GLY LEU GLY TYR GLU THR LYS GLU GLU LEU ILE
SEQRES 6 A 135 PHE ARG TYR CYS SER GLY SER CYS GLU ALA ALA GLU THR
SEQRES 7 A 135 MET TYR ASP LYS ILE LEU LYS ASN LEU SER ARG SER ARG
SEQRES 8 A 135 ARG LEU THR SER ASP LYS VAL GLY GLN ALA CYS CYS ARG
SEQRES 9 A 135 PRO VAL ALA PHE ASP ASP ASP LEU SER PHE LEU ASP ASP
SEQRES 10 A 135 SER LEU VAL TYR HIS ILE LEU ARG LYS HIS SER ALA LYS
SEQRES 11 A 135 ARG CYS GLY CYS ILE
SEQRES 1 B 135 MET SER PRO ASP LYS GLN ALA ALA ALA LEU PRO ARG ARG
SEQRES 2 B 135 GLU ARG ASN ARG GLN ALA ALA ALA ALA SER PRO GLU ASN
SEQRES 3 B 135 SER ARG GLY LYS GLY ARG ARG GLY GLN ARG GLY LYS ASN
SEQRES 4 B 135 ARG GLY CYS VAL LEU THR ALA ILE HIS LEU ASN VAL THR
SEQRES 5 B 135 ASP LEU GLY LEU GLY TYR GLU THR LYS GLU GLU LEU ILE
SEQRES 6 B 135 PHE ARG TYR CYS SER GLY SER CYS GLU ALA ALA GLU THR
SEQRES 7 B 135 MET TYR ASP LYS ILE LEU LYS ASN LEU SER ARG SER ARG
SEQRES 8 B 135 ARG LEU THR SER ASP LYS VAL GLY GLN ALA CYS CYS ARG
SEQRES 9 B 135 PRO VAL ALA PHE ASP ASP ASP LEU SER PHE LEU ASP ASP
SEQRES 10 B 135 SER LEU VAL TYR HIS ILE LEU ARG LYS HIS SER ALA LYS
SEQRES 11 B 135 ARG CYS GLY CYS ILE
SEQRES 1 C 135 MET SER PRO ASP LYS GLN ALA ALA ALA LEU PRO ARG ARG
SEQRES 2 C 135 GLU ARG ASN ARG GLN ALA ALA ALA ALA SER PRO GLU ASN
SEQRES 3 C 135 SER ARG GLY LYS GLY ARG ARG GLY GLN ARG GLY LYS ASN
SEQRES 4 C 135 ARG GLY CYS VAL LEU THR ALA ILE HIS LEU ASN VAL THR
SEQRES 5 C 135 ASP LEU GLY LEU GLY TYR GLU THR LYS GLU GLU LEU ILE
SEQRES 6 C 135 PHE ARG TYR CYS SER GLY SER CYS GLU ALA ALA GLU THR
SEQRES 7 C 135 MET TYR ASP LYS ILE LEU LYS ASN LEU SER ARG SER ARG
SEQRES 8 C 135 ARG LEU THR SER ASP LYS VAL GLY GLN ALA CYS CYS ARG
SEQRES 9 C 135 PRO VAL ALA PHE ASP ASP ASP LEU SER PHE LEU ASP ASP
SEQRES 10 C 135 SER LEU VAL TYR HIS ILE LEU ARG LYS HIS SER ALA LYS
SEQRES 11 C 135 ARG CYS GLY CYS ILE
SEQRES 1 D 135 MET SER PRO ASP LYS GLN ALA ALA ALA LEU PRO ARG ARG
SEQRES 2 D 135 GLU ARG ASN ARG GLN ALA ALA ALA ALA SER PRO GLU ASN
SEQRES 3 D 135 SER ARG GLY LYS GLY ARG ARG GLY GLN ARG GLY LYS ASN
SEQRES 4 D 135 ARG GLY CYS VAL LEU THR ALA ILE HIS LEU ASN VAL THR
SEQRES 5 D 135 ASP LEU GLY LEU GLY TYR GLU THR LYS GLU GLU LEU ILE
SEQRES 6 D 135 PHE ARG TYR CYS SER GLY SER CYS GLU ALA ALA GLU THR
SEQRES 7 D 135 MET TYR ASP LYS ILE LEU LYS ASN LEU SER ARG SER ARG
SEQRES 8 D 135 ARG LEU THR SER ASP LYS VAL GLY GLN ALA CYS CYS ARG
SEQRES 9 D 135 PRO VAL ALA PHE ASP ASP ASP LEU SER PHE LEU ASP ASP
SEQRES 10 D 135 SER LEU VAL TYR HIS ILE LEU ARG LYS HIS SER ALA LYS
SEQRES 11 D 135 ARG CYS GLY CYS ILE
FORMUL 5 HOH *285(H2 O)
HELIX 1 1 VAL A 51 LEU A 54 5 4
HELIX 2 2 MET A 79 SER A 90 1 12
HELIX 3 3 VAL B 51 LEU B 54 5 4
HELIX 4 4 MET B 79 ARG B 89 1 11
HELIX 5 5 VAL C 51 LEU C 54 5 4
HELIX 6 6 MET C 79 ARG C 89 1 11
HELIX 7 7 VAL D 51 LEU D 54 5 4
HELIX 8 8 MET D 79 ARG D 89 1 11
SHEET 1 A 2 VAL A 43 ASN A 50 0
SHEET 2 A 2 GLU A 63 SER A 70 -1 N SER A 70 O VAL A 43
SHEET 1 B 2 LEU A 112 LEU A 115 0
SHEET 2 B 2 TYR A 121 LEU A 124 -1 N LEU A 124 O LEU A 112
SHEET 1 C 2 VAL B 43 ASN B 50 0
SHEET 2 C 2 GLU B 63 SER B 70 -1 N SER B 70 O VAL B 43
SHEET 1 D 2 LEU B 112 LEU B 115 0
SHEET 2 D 2 TYR B 121 LEU B 124 -1 N LEU B 124 O LEU B 112
SHEET 1 E 2 VAL C 43 ASN C 50 0
SHEET 2 E 2 GLU C 63 SER C 70 -1 N SER C 70 O VAL C 43
SHEET 1 F 2 LEU C 112 LEU C 115 0
SHEET 2 F 2 TYR C 121 LEU C 124 -1 N LEU C 124 O LEU C 112
SHEET 1 G 2 VAL D 43 ASN D 50 0
SHEET 2 G 2 GLU D 63 SER D 70 -1 N SER D 70 O VAL D 43
SHEET 1 H 2 LEU D 112 LEU D 115 0
SHEET 2 H 2 TYR D 121 LEU D 124 -1 N LEU D 124 O LEU D 112
SHEET 1 I 2 CYS A 102 ALA A 107 0
SHEET 2 I 2 ARG A 131 ILE A 135 -1 N ILE A 135 O CYS A 102
SHEET 1 J 2 CYS B 102 ALA B 107 0
SHEET 2 J 2 ARG B 131 ILE B 135 -1 N ILE B 135 O CYS B 102
SHEET 1 K 2 CYS C 102 ALA C 107 0
SHEET 2 K 2 ARG C 131 ILE C 135 -1 N ILE C 135 O CYS C 102
SHEET 1 L 2 CYS D 103 ALA D 107 0
SHEET 2 L 2 ARG D 131 CYS D 134 -1 N GLY D 133 O ARG D 104
SSBOND 1 CYS A 42 CYS A 103 1555 1555 2.02
SSBOND 2 CYS A 69 CYS A 132 1555 1555 2.04
SSBOND 3 CYS A 73 CYS A 134 1555 1555 2.03
SSBOND 4 CYS A 102 CYS B 102 1555 1555 1.99
SSBOND 5 CYS B 42 CYS B 103 1555 1555 2.03
SSBOND 6 CYS B 69 CYS B 132 1555 1555 2.04
SSBOND 7 CYS B 73 CYS B 134 1555 1555 2.02
SSBOND 8 CYS C 42 CYS C 103 1555 1555 2.03
SSBOND 9 CYS C 69 CYS C 132 1555 1555 2.04
SSBOND 10 CYS C 73 CYS C 134 1555 1555 2.02
SSBOND 11 CYS C 102 CYS D 102 1555 1555 2.04
SSBOND 12 CYS D 42 CYS D 103 1555 1555 2.02
SSBOND 13 CYS D 69 CYS D 132 1555 1555 2.03
SSBOND 14 CYS D 73 CYS D 134 1555 1555 2.03
CRYST1 67.850 67.550 71.400 90.00 115.94 90.00 P 1 21 1 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 0.014738 0.000000 0.007169 0.00000
SCALE2 0.000000 0.014804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015575 0.00000
MTRIX1 1 0.131915 0.517078 -0.845712 24.84780 1
MTRIX2 1 0.528292 -0.758579 -0.381400 38.88020 1
MTRIX3 1 -0.838753 -0.396470 -0.373237 58.13580 1
MTRIX1 2 0.559989 0.039033 0.827580 3.89620 1
MTRIX2 2 0.087061 -0.996132 -0.011928 15.99100 1
MTRIX3 2 0.823913 0.078730 -0.561221 2.57190 1
MTRIX1 3 -0.756660 -0.611477 0.231434 38.83200 1
MTRIX2 3 -0.215165 0.567151 0.795012 29.26620 1
MTRIX3 3 -0.617389 0.551757 -0.560709 44.48680 1
(ATOM LINES ARE NOT SHOWN.)
END
