HEADER SIGNALING PROTEIN 01-NOV-05 2D5G
TITLE STRUCTURE OF UBIQUITIN FOLD PROTEIN R767E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AXIN-1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: DIX DOMAIN;
COMPND 5 SYNONYM: AXIS INHIBITION PROTEIN 1, RAXIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMALC2
KEYWDS UBIQUITIN FOLD, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SHIBATA,Y.HIGUCHI
REVDAT 3 10-NOV-21 2D5G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D5G 1 VERSN
REVDAT 1 01-NOV-06 2D5G 0
JRNL AUTH N.SHIBATA,T.HANAMURA,R.YAMAMOTO,Y.UEDA,H.YAMAMOTO,A.KIKUCHI,
JRNL AUTH 2 Y.HIGUCHI
JRNL TITL STRUCTURE OF UBIQUITIN FOLD PROTEIN R767E MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 321432.460
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 21930
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) : 0.228
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2081
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1868
REMARK 3 BIN R VALUE (WORKING SET) : 0.3810
REMARK 3 BIN FREE R VALUE : 0.4690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 210
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
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) : 76.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.43000
REMARK 3 B12 (A**2) : 3.44000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.40
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) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.62
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
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) : 7.710 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 12.320; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 16.290; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 21.350; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 66.61
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PCMB.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : PCMB.TO
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 4
REMARK 4 2D5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000025009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-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 : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21930
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
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) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, TRIS, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
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 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+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 1.000000 0.000000 0.000000 62.77500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.24316
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 38.47667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 62.77500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 36.24316
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 38.47667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 62.77500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 36.24316
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.47667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.48633
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 76.95333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 72.48633
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 76.95333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 72.48633
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 76.95333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 PRO A 748
REMARK 465 PRO A 749
REMARK 465 PRO C 748
REMARK 465 PRO C 749
REMARK 465 PRO D 748
REMARK 465 PRO D 749
REMARK 465 PRO E 748
REMARK 465 PRO E 749
REMARK 465 CYS E 750
REMARK 465 ASP E 751
REMARK 465 SER E 752
REMARK 465 PRO F 748
REMARK 465 PRO F 749
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 749 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 PRO B 749 C - N - CD ANGL. DEV. = -15.9 DEGREES
REMARK 500 GLU D 800 CA - C - N ANGL. DEV. = 17.3 DEGREES
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 CYS A 760 44.99 21.16
REMARK 500 GLU A 762 124.05 -13.56
REMARK 500 ARG A 773 -29.24 72.06
REMARK 500 SER A 798 118.59 -160.16
REMARK 500 GLU A 822 -5.12 72.61
REMARK 500 PRO B 749 127.18 11.82
REMARK 500 ASP B 751 72.10 79.76
REMARK 500 SER B 752 126.31 160.80
REMARK 500 CYS B 760 5.49 49.67
REMARK 500 ARG B 773 -28.14 63.14
REMARK 500 LYS B 796 161.62 178.71
REMARK 500 CYS B 803 22.94 34.19
REMARK 500 GLU B 822 -10.99 75.15
REMARK 500 CYS C 760 47.07 26.27
REMARK 500 ARG C 773 -17.32 50.45
REMARK 500 SER C 798 116.38 -165.62
REMARK 500 CYS C 803 16.89 -140.45
REMARK 500 GLU C 822 -5.99 74.26
REMARK 500 ASP D 751 -140.58 77.30
REMARK 500 CYS D 760 105.52 -12.87
REMARK 500 ARG D 773 1.41 57.41
REMARK 500 ALA D 774 83.90 -172.80
REMARK 500 LYS D 796 128.85 -170.74
REMARK 500 ASP D 799 88.10 0.17
REMARK 500 GLU D 800 -20.81 67.96
REMARK 500 PHE D 801 -135.58 -159.02
REMARK 500 ASP D 813 -54.15 -25.69
REMARK 500 GLU D 822 -6.02 75.80
REMARK 500 CYS E 760 18.40 54.72
REMARK 500 ARG E 773 -110.07 -71.15
REMARK 500 LYS E 796 114.39 -173.39
REMARK 500 ASP E 802 -80.68 -68.79
REMARK 500 GLU E 822 -5.69 73.37
REMARK 500 CYS F 760 15.53 42.01
REMARK 500 ARG F 773 20.86 45.94
REMARK 500 ALA F 774 95.88 -177.80
REMARK 500 GLU F 822 -6.63 75.70
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 ARG A 771 GLY A 772 149.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR C 793 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG E 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WSP RELATED DB: PDB
DBREF 2D5G A 748 832 UNP O70239 AXN1_RAT 743 827
DBREF 2D5G B 748 832 UNP O70239 AXN1_RAT 743 827
DBREF 2D5G C 748 832 UNP O70239 AXN1_RAT 743 827
DBREF 2D5G D 748 832 UNP O70239 AXN1_RAT 743 827
DBREF 2D5G E 748 832 UNP O70239 AXN1_RAT 743 827
DBREF 2D5G F 748 832 UNP O70239 AXN1_RAT 743 827
SEQADV 2D5G GLU A 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQADV 2D5G GLU B 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQADV 2D5G GLU C 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQADV 2D5G GLU D 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQADV 2D5G GLU E 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQADV 2D5G GLU F 767 UNP O70239 ARG 762 ENGINEERED MUTATION
SEQRES 1 A 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 A 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 A 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 A 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 A 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 A 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 A 85 GLY LYS VAL GLU LYS VAL ASP
SEQRES 1 B 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 B 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 B 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 B 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 B 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 B 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 B 85 GLY LYS VAL GLU LYS VAL ASP
SEQRES 1 C 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 C 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 C 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 C 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 C 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 C 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 C 85 GLY LYS VAL GLU LYS VAL ASP
SEQRES 1 D 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 D 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 D 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 D 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 D 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 D 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 D 85 GLY LYS VAL GLU LYS VAL ASP
SEQRES 1 E 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 E 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 E 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 E 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 E 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 E 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 E 85 GLY LYS VAL GLU LYS VAL ASP
SEQRES 1 F 85 PRO PRO CYS ASP SER ILE VAL VAL ALA TYR TYR PHE CYS
SEQRES 2 F 85 GLY GLU PRO ILE PRO TYR GLU THR LEU VAL ARG GLY ARG
SEQRES 3 F 85 ALA VAL THR LEU GLY GLN PHE LYS GLU LEU LEU THR LYS
SEQRES 4 F 85 LYS GLY SER TYR ARG TYR TYR PHE LYS LYS VAL SER ASP
SEQRES 5 F 85 GLU PHE ASP CYS GLY VAL VAL PHE GLU GLU VAL ARG GLU
SEQRES 6 F 85 ASP GLU ALA ILE LEU PRO VAL PHE GLU GLU LYS ILE ILE
SEQRES 7 F 85 GLY LYS VAL GLU LYS VAL ASP
HET HG A 601 1
HET HG A 602 1
HET HG B 603 1
HET HG B 604 1
HET HG C 605 1
HET HG C 606 1
HET HG D 607 1
HET HG E 608 1
HET HG F 609 1
HET HG F 610 1
HETNAM HG MERCURY (II) ION
FORMUL 7 HG 10(HG 2+)
HELIX 1 1 THR A 776 GLU A 782 1 7
HELIX 2 2 THR B 776 GLU B 782 1 7
HELIX 3 3 THR C 776 GLU C 782 1 7
HELIX 4 4 THR D 776 GLU D 782 1 7
HELIX 5 5 THR E 776 GLU E 782 1 7
HELIX 6 6 THR F 776 GLU F 782 1 7
SHEET 1 A30 TYR B 766 ARG B 771 0
SHEET 2 A30 SER B 752 PHE B 759 -1 N TYR B 757 O TYR B 766
SHEET 3 A30 LYS B 823 LYS B 830 1 O GLY B 826 N TYR B 758
SHEET 4 A30 TYR B 790 VAL B 797 -1 N LYS B 795 O ILE B 825
SHEET 5 A30 VAL B 805 GLU B 809 -1 O VAL B 806 N LYS B 796
SHEET 6 A30 TYR A 766 ARG A 771 1 N GLU A 767 O PHE B 807
SHEET 7 A30 SER A 752 PHE A 759 -1 N VAL A 755 O THR A 768
SHEET 8 A30 LYS A 823 LYS A 830 1 O GLY A 826 N TYR A 758
SHEET 9 A30 TYR A 790 VAL A 797 -1 N LYS A 795 O ILE A 825
SHEET 10 A30 VAL A 805 GLU A 809 -1 O GLU A 808 N PHE A 794
SHEET 11 A30 TYR C 766 ARG C 771 1 O GLU C 767 N GLU A 809
SHEET 12 A30 SER C 752 PHE C 759 -1 N VAL C 755 O THR C 768
SHEET 13 A30 LYS C 823 LYS C 830 1 O GLY C 826 N TYR C 758
SHEET 14 A30 TYR C 790 VAL C 797 -1 N ARG C 791 O GLU C 829
SHEET 15 A30 VAL C 805 VAL C 810 -1 O GLU C 808 N PHE C 794
SHEET 16 A30 TYR D 766 VAL D 770 1 O GLU D 767 N PHE C 807
SHEET 17 A30 ILE D 753 PHE D 759 -1 N ILE D 753 O VAL D 770
SHEET 18 A30 LYS D 823 LYS D 830 1 O GLY D 826 N TYR D 758
SHEET 19 A30 TYR D 790 SER D 798 -1 N ARG D 791 O GLU D 829
SHEET 20 A30 PHE D 801 VAL D 810 -1 O PHE D 801 N SER D 798
SHEET 21 A30 TYR E 766 LEU E 769 1 O GLU E 767 N PHE D 807
SHEET 22 A30 VAL E 754 PHE E 759 -1 N TYR E 757 O TYR E 766
SHEET 23 A30 LYS E 823 LYS E 830 1 O GLY E 826 N TYR E 758
SHEET 24 A30 TYR E 790 VAL E 797 -1 N TYR E 793 O LYS E 827
SHEET 25 A30 VAL E 805 VAL E 810 -1 O GLU E 808 N PHE E 794
SHEET 26 A30 TYR F 766 ARG F 771 1 O GLU F 767 N GLU E 809
SHEET 27 A30 SER F 752 PHE F 759 -1 N ILE F 753 O VAL F 770
SHEET 28 A30 LYS F 823 LYS F 830 1 O GLY F 826 N TYR F 758
SHEET 29 A30 TYR F 790 VAL F 797 -1 N LYS F 795 O ILE F 825
SHEET 30 A30 VAL F 805 GLU F 809 -1 O GLU F 808 N PHE F 794
CISPEP 1 CYS D 803 GLY D 804 0 5.53
SITE 1 AC1 2 CYS A 750 CYS C 803
SITE 1 AC2 3 PHE A 759 CYS A 760 TYR A 790
SITE 1 AC3 2 CYS B 750 ASP B 751
SITE 1 AC4 3 PHE B 759 CYS B 760 TYR B 790
SITE 1 AC5 1 CYS C 750
SITE 1 AC6 2 PHE C 759 CYS C 760
SITE 1 AC7 2 PHE D 759 CYS D 760
SITE 1 AC8 2 PHE E 759 CYS E 760
SITE 1 AC9 3 PHE F 759 CYS F 760 TYR F 790
SITE 1 BC1 2 CYS F 750 CYS F 803
CRYST1 125.550 125.550 115.430 90.00 90.00 120.00 H 3 54
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 0.007965 0.004599 0.000000 0.00000
SCALE2 0.000000 0.009197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008663 0.00000
(ATOM LINES ARE NOT SHOWN.)
END