HEADER RNA BINDING 02-JAN-03 1OA8
TITLE AXH DOMAIN OF HUMAN SPINOCEREBELLAR ATAXIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATAXIN-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: AXH DOMAIN, RESIDUES 562-694;
COMPND 5 SYNONYM: SPINOCEREBELLAR ATAXIA TYPE 1 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS RNA BINDING, HIGH MOBILITY GROUP HOMOLOGY, HMG, RNA-BINDING,
KEYWDS 2 DIMERIZATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.ALLEN,Y.W.CHEN,M.BYCROFT
REVDAT 6 09-OCT-19 1OA8 1 REMARK
REVDAT 5 06-FEB-19 1OA8 1 JRNL REMARK
REVDAT 4 24-JAN-18 1OA8 1 SOURCE
REVDAT 3 24-FEB-09 1OA8 1 VERSN
REVDAT 2 29-JAN-04 1OA8 1 JRNL
REVDAT 1 06-NOV-03 1OA8 0
JRNL AUTH Y.W.CHEN,M.D.ALLEN,D.B.VEPRINTSEV,J.LOWE,M.BYCROFT
JRNL TITL THE STRUCTURE OF THE AXH DOMAIN OF SPINOCEREBELLAR ATAXIN-1.
JRNL REF J. BIOL. CHEM. V. 279 3758 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14583607
JRNL DOI 10.1074/JBC.M309817200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.DE CHIARA,C.GIANNINI,S.ADINOLFI,J.DE BOER,S.GUIDA,A.RAMOS,
REMARK 1 AUTH 2 C.JODICE,D.KIOUSSIS,A.PASTORE
REMARK 1 TITL THE AXH MODULE: AN INDEPENDENTLY FOLDED DOMAIN COMMON TO
REMARK 1 TITL 2 ATAXIN-1 AND HBP1.
REMARK 1 REF FEBS LETT. V. 551 107 2003
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 12965213
REMARK 1 DOI 10.1016/S0014-5793(03)00818-4
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.27
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 58574
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 + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3125
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4211
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 378
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.39000
REMARK 3 B22 (A**2) : -1.09000
REMARK 3 B33 (A**2) : -0.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.118
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.883
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4018 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5458 ; 1.780 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 514 ; 6.668 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 628 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3020 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1747 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 347 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 11 ; 0.176 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 61 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.239 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2585 ; 1.292 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4201 ; 2.253 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1433 ; 3.333 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 5.640 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGION IN B CHAIN (RESIDUES
REMARK 3 39 - 51) MODELED BUILT FROM SE-METHONINE DATA.
REMARK 4
REMARK 4 1OA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1290011915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.960,0.97916,0.97966
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62044
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 70.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 0.1M
REMARK 280 TRIS/HCL, PH 7.0, 0.2M AMMONIUM SULPHATE, 5 MM DTT, 15% PEG 4000,
REMARK 280 20% GLYCEROL, AT 290K, PH 7.00, VAPOR DIFFUSION, SITTING DROP
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 24.39150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.89050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.22050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.89050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.39150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.22050
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: DIMERIC
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 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 400
REMARK 400 COMPOUND
REMARK 400 ATAXIN-1 BINDS TO RNA IN VITRO.
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 ASN A 690
REMARK 465 LEU A 691
REMARK 465 LYS A 692
REMARK 465 ASN A 693
REMARK 465 GLY A 694
REMARK 465 ASN B 690
REMARK 465 LEU B 691
REMARK 465 LYS B 692
REMARK 465 ASN B 693
REMARK 465 GLY B 694
REMARK 465 LEU C 691
REMARK 465 LYS C 692
REMARK 465 ASN C 693
REMARK 465 GLY C 694
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B 689 C O CB CG CD CE NZ
REMARK 470 ASN C 690 O CB CG OD1 ND2
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 O HOH D 2017 O HOH D 2021 1.99
REMARK 500 O HOH A 2065 O HOH A 2091 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 2091 O HOH D 2031 1545 2.06
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 598 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP D 598 CB - CG - OD2 ANGL. DEV. = 6.7 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 ALA A 584 2.35 -56.31
REMARK 500 GLN A 656 -56.30 -132.42
REMARK 500 LEU B 609 106.92 -42.33
REMARK 500 GLN B 656 -39.11 -147.01
REMARK 500 CYS B 662 81.20 -152.19
REMARK 500 ARG C 638 67.59 27.04
REMARK 500 GLN C 656 -36.65 -142.47
REMARK 500 ASN D 585 0.48 -61.15
REMARK 500 GLN D 656 -33.48 -136.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2098 DISTANCE = 5.82 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1690 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2096 O
REMARK 620 2 LEU A 609 O 101.4
REMARK 620 3 ALA A 603 O 104.9 83.3
REMARK 620 4 SER A 606 O 164.5 93.6 80.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C1691 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2049 O
REMARK 620 2 SER C 606 O 172.6
REMARK 620 3 LEU C 609 O 90.2 96.4
REMARK 620 4 ALA C 603 O 91.9 90.1 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D1695 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 603 O
REMARK 620 2 HOH A2066 O 91.0
REMARK 620 3 SER D 606 O 94.2 168.8
REMARK 620 4 HOH D2115 O 108.6 81.5 87.5
REMARK 620 5 LEU D 609 O 104.7 95.6 92.6 146.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1690
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C1691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D1695
DBREF 1OA8 A 562 562 PDB 1OA8 1OA8 562 562
DBREF 1OA8 A 563 694 UNP P54253 ATX1_HUMAN 563 694
DBREF 1OA8 B 562 562 PDB 1OA8 1OA8 562 562
DBREF 1OA8 B 563 694 UNP P54253 ATX1_HUMAN 563 694
DBREF 1OA8 C 562 562 PDB 1OA8 1OA8 562 562
DBREF 1OA8 C 563 694 UNP P54253 ATX1_HUMAN 563 694
DBREF 1OA8 D 562 562 PDB 1OA8 1OA8 562 562
DBREF 1OA8 D 563 694 UNP P54253 ATX1_HUMAN 563 694
SEQRES 1 A 133 GLY SER PRO ALA ALA ALA PRO PRO THR LEU PRO PRO TYR
SEQRES 2 A 133 PHE MET LYS GLY SER ILE ILE GLN LEU ALA ASN GLY GLU
SEQRES 3 A 133 LEU LYS LYS VAL GLU ASP LEU LYS THR GLU ASP PHE ILE
SEQRES 4 A 133 GLN SER ALA GLU ILE SER ASN ASP LEU LYS ILE ASP SER
SEQRES 5 A 133 SER THR VAL GLU ARG ILE GLU ASP SER HIS SER PRO GLY
SEQRES 6 A 133 VAL ALA VAL ILE GLN PHE ALA VAL GLY GLU HIS ARG ALA
SEQRES 7 A 133 GLN VAL SER VAL GLU VAL LEU VAL GLU TYR PRO PHE PHE
SEQRES 8 A 133 VAL PHE GLY GLN GLY TRP SER SER CYS CYS PRO GLU ARG
SEQRES 9 A 133 THR SER GLN LEU PHE ASP LEU PRO CYS SER LYS LEU SER
SEQRES 10 A 133 VAL GLY ASP VAL CYS ILE SER LEU THR LEU LYS ASN LEU
SEQRES 11 A 133 LYS ASN GLY
SEQRES 1 B 133 GLY SER PRO ALA ALA ALA PRO PRO THR LEU PRO PRO TYR
SEQRES 2 B 133 PHE MET LYS GLY SER ILE ILE GLN LEU ALA ASN GLY GLU
SEQRES 3 B 133 LEU LYS LYS VAL GLU ASP LEU LYS THR GLU ASP PHE ILE
SEQRES 4 B 133 GLN SER ALA GLU ILE SER ASN ASP LEU LYS ILE ASP SER
SEQRES 5 B 133 SER THR VAL GLU ARG ILE GLU ASP SER HIS SER PRO GLY
SEQRES 6 B 133 VAL ALA VAL ILE GLN PHE ALA VAL GLY GLU HIS ARG ALA
SEQRES 7 B 133 GLN VAL SER VAL GLU VAL LEU VAL GLU TYR PRO PHE PHE
SEQRES 8 B 133 VAL PHE GLY GLN GLY TRP SER SER CYS CYS PRO GLU ARG
SEQRES 9 B 133 THR SER GLN LEU PHE ASP LEU PRO CYS SER LYS LEU SER
SEQRES 10 B 133 VAL GLY ASP VAL CYS ILE SER LEU THR LEU LYS ASN LEU
SEQRES 11 B 133 LYS ASN GLY
SEQRES 1 C 133 GLY SER PRO ALA ALA ALA PRO PRO THR LEU PRO PRO TYR
SEQRES 2 C 133 PHE MET LYS GLY SER ILE ILE GLN LEU ALA ASN GLY GLU
SEQRES 3 C 133 LEU LYS LYS VAL GLU ASP LEU LYS THR GLU ASP PHE ILE
SEQRES 4 C 133 GLN SER ALA GLU ILE SER ASN ASP LEU LYS ILE ASP SER
SEQRES 5 C 133 SER THR VAL GLU ARG ILE GLU ASP SER HIS SER PRO GLY
SEQRES 6 C 133 VAL ALA VAL ILE GLN PHE ALA VAL GLY GLU HIS ARG ALA
SEQRES 7 C 133 GLN VAL SER VAL GLU VAL LEU VAL GLU TYR PRO PHE PHE
SEQRES 8 C 133 VAL PHE GLY GLN GLY TRP SER SER CYS CYS PRO GLU ARG
SEQRES 9 C 133 THR SER GLN LEU PHE ASP LEU PRO CYS SER LYS LEU SER
SEQRES 10 C 133 VAL GLY ASP VAL CYS ILE SER LEU THR LEU LYS ASN LEU
SEQRES 11 C 133 LYS ASN GLY
SEQRES 1 D 133 GLY SER PRO ALA ALA ALA PRO PRO THR LEU PRO PRO TYR
SEQRES 2 D 133 PHE MET LYS GLY SER ILE ILE GLN LEU ALA ASN GLY GLU
SEQRES 3 D 133 LEU LYS LYS VAL GLU ASP LEU LYS THR GLU ASP PHE ILE
SEQRES 4 D 133 GLN SER ALA GLU ILE SER ASN ASP LEU LYS ILE ASP SER
SEQRES 5 D 133 SER THR VAL GLU ARG ILE GLU ASP SER HIS SER PRO GLY
SEQRES 6 D 133 VAL ALA VAL ILE GLN PHE ALA VAL GLY GLU HIS ARG ALA
SEQRES 7 D 133 GLN VAL SER VAL GLU VAL LEU VAL GLU TYR PRO PHE PHE
SEQRES 8 D 133 VAL PHE GLY GLN GLY TRP SER SER CYS CYS PRO GLU ARG
SEQRES 9 D 133 THR SER GLN LEU PHE ASP LEU PRO CYS SER LYS LEU SER
SEQRES 10 D 133 VAL GLY ASP VAL CYS ILE SER LEU THR LEU LYS ASN LEU
SEQRES 11 D 133 LYS ASN GLY
HET NA A1690 1
HET NA C1691 1
HET NA D1695 1
HETNAM NA SODIUM ION
FORMUL 5 NA 3(NA 1+)
FORMUL 8 HOH *378(H2 O)
HELIX 1 1 PRO A 572 MET A 576 5 5
HELIX 2 2 GLU A 592 LEU A 594 5 3
HELIX 3 3 LYS A 595 SER A 606 1 12
HELIX 4 4 CYS A 662 ASP A 671 1 10
HELIX 5 5 ALA B 567 LEU B 571 5 5
HELIX 6 6 PRO B 573 LYS B 577 5 5
HELIX 7 7 GLU B 592 LEU B 594 5 3
HELIX 8 8 LYS B 595 PHE B 599 5 5
HELIX 9 9 CYS B 662 ASP B 671 1 10
HELIX 10 10 PRO C 572 MET C 576 5 5
HELIX 11 11 GLU C 592 LEU C 594 5 3
HELIX 12 12 LYS C 595 SER C 606 1 12
HELIX 13 13 GLU C 636 ARG C 638 5 3
HELIX 14 14 CYS C 662 ASP C 671 1 10
HELIX 15 15 SER D 563 ALA D 567 5 5
HELIX 16 16 PRO D 573 LYS D 577 5 5
HELIX 17 17 GLU D 592 LEU D 594 5 3
HELIX 18 18 LYS D 595 SER D 606 1 12
HELIX 19 19 CYS D 662 ASP D 671 1 10
SHEET 1 AA 5 ALA A 565 ALA A 566 0
SHEET 2 AA 5 ALA A 639 LEU A 646 1 O SER A 642 N ALA A 565
SHEET 3 AA 5 VAL A 627 VAL A 634 -1 O ALA A 628 N VAL A 645
SHEET 4 AA 5 LEU A 609 ASP A 621 -1 O THR A 615 N ALA A 633
SHEET 5 AA 5 VAL A 682 LEU A 688 -1 O CYS A 683 N SER A 614
SHEET 1 AB 2 ILE A 580 GLN A 582 0
SHEET 2 AB 2 LEU A 588 LYS A 590 -1 O LYS A 589 N ILE A 581
SHEET 1 AC 3 PHE A 651 VAL A 653 0
SHEET 2 AC 3 GLY A 657 SER A 660 -1 O GLY A 657 N VAL A 653
SHEET 3 AC 3 SER A 675 LYS A 676 1 O SER A 675 N SER A 660
SHEET 1 BA 2 ILE B 580 GLN B 582 0
SHEET 2 BA 2 LEU B 588 LYS B 590 -1 O LYS B 589 N ILE B 581
SHEET 1 BB 7 ALA B 639 LEU B 646 0
SHEET 2 BB 7 VAL B 627 VAL B 634 -1 O ALA B 628 N VAL B 645
SHEET 3 BB 7 SER B 613 ASP B 621 -1 O THR B 615 N ALA B 633
SHEET 4 BB 7 VAL B 682 ILE B 684 -1 O CYS B 683 N SER B 614
SHEET 5 BB 7 PHE B 651 VAL B 653 -1 O PHE B 652 N ILE B 684
SHEET 6 BB 7 GLY B 657 SER B 660 -1 O GLY B 657 N VAL B 653
SHEET 7 BB 7 SER B 675 LYS B 676 1 O SER B 675 N SER B 660
SHEET 1 CA 5 ALA C 565 ALA C 566 0
SHEET 2 CA 5 ALA C 639 LEU C 646 1 O SER C 642 N ALA C 565
SHEET 3 CA 5 VAL C 627 VAL C 634 -1 O ALA C 628 N VAL C 645
SHEET 4 CA 5 LEU C 609 ASP C 621 -1 O THR C 615 N ALA C 633
SHEET 5 CA 5 VAL C 682 LEU C 688 -1 O CYS C 683 N SER C 614
SHEET 1 CB 2 ILE C 580 GLN C 582 0
SHEET 2 CB 2 LEU C 588 LYS C 590 -1 O LYS C 589 N ILE C 581
SHEET 1 CC 3 PHE C 651 VAL C 653 0
SHEET 2 CC 3 GLY C 657 SER C 660 -1 O GLY C 657 N VAL C 653
SHEET 3 CC 3 SER C 675 LYS C 676 1 O SER C 675 N SER C 660
SHEET 1 DA 2 ILE D 580 GLN D 582 0
SHEET 2 DA 2 LEU D 588 LYS D 590 -1 O LYS D 589 N ILE D 581
SHEET 1 DB 4 ALA D 639 LEU D 646 0
SHEET 2 DB 4 VAL D 627 VAL D 634 -1 O ALA D 628 N VAL D 645
SHEET 3 DB 4 LEU D 609 ASP D 621 -1 O THR D 615 N ALA D 633
SHEET 4 DB 4 VAL D 682 LEU D 688 -1 O CYS D 683 N SER D 614
SHEET 1 DC 3 PHE D 651 VAL D 653 0
SHEET 2 DC 3 GLY D 657 SER D 660 -1 O GLY D 657 N VAL D 653
SHEET 3 DC 3 SER D 675 LYS D 676 1 O SER D 675 N SER D 660
LINK NA NA A1690 O HOH A2096 1555 1555 2.11
LINK NA NA A1690 O LEU A 609 1555 1555 2.60
LINK NA NA A1690 O ALA A 603 1555 1555 2.37
LINK NA NA A1690 O SER A 606 1555 1555 2.56
LINK NA NA C1691 O HOH B2049 1555 1555 2.38
LINK NA NA C1691 O SER C 606 1555 1555 2.27
LINK NA NA C1691 O LEU C 609 1555 1555 2.26
LINK NA NA C1691 O ALA C 603 1555 1555 2.08
LINK NA NA D1695 O ALA D 603 1555 1555 2.26
LINK NA NA D1695 O HOH A2066 1555 1565 2.25
LINK NA NA D1695 O SER D 606 1555 1555 2.33
LINK NA NA D1695 O HOH D2115 1555 1555 2.34
LINK NA NA D1695 O LEU D 609 1555 1555 2.24
SITE 1 AC1 5 ALA A 603 SER A 606 LEU A 609 LYS A 689
SITE 2 AC1 5 HOH A2096
SITE 1 AC2 5 HOH B2049 HOH B2056 ALA C 603 SER C 606
SITE 2 AC2 5 LEU C 609
SITE 1 AC3 6 HOH A2066 ALA D 603 SER D 606 LEU D 609
SITE 2 AC3 6 LYS D 689 HOH D2115
CRYST1 48.783 82.441 137.781 90.00 90.00 90.00 P 21 21 21 16
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 0.020499 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007258 0.00000
MTRIX1 1 -0.669210 -0.054970 0.741030 -27.01102 1
MTRIX2 1 0.091550 -0.995760 0.008820 -63.26282 1
MTRIX3 1 0.737410 0.073740 0.671410 14.60991 1
MTRIX1 2 0.876220 -0.481880 -0.004650 -15.61538 1
MTRIX2 2 0.470700 0.857870 -0.206140 43.61203 1
MTRIX3 2 0.103320 0.178440 0.978510 5.62488 1
MTRIX1 3 -0.665600 0.385440 0.639070 -11.01075 1
MTRIX2 3 -0.352250 -0.917180 0.186300 -27.62694 1
MTRIX3 3 0.657950 -0.101110 0.746240 5.62451 1
(ATOM LINES ARE NOT SHOWN.)
END
