HEADER METAL BINDING PROTEIN 28-JUL-03 1OKQ
TITLE LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR, CA1 SITE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMININ ALPHA 2 CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LAMININ G-LIKE DOMAIN 4-5 PAIR, RESIDUES 2729-3093;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: FVB/N;
SOURCE 6 CELL_LINE: EBNA-293;
SOURCE 7 TISSUE: EMBRYO;
SOURCE 8 CELL: EMRYONIC KIDNEY CELL;
SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: EBNA-293;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PCEP-PU
KEYWDS METAL BINDING PROTEIN, LAMININ
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WIZEMANN,J.H.O.GARBE,M.V.K.FRIEDRICH,R.TIMPL,T.SASAKI,E.HOHENESTER
REVDAT 4 13-DEC-23 1OKQ 1 LINK
REVDAT 3 22-MAY-19 1OKQ 1 REMARK
REVDAT 2 24-FEB-09 1OKQ 1 VERSN
REVDAT 1 11-SEP-03 1OKQ 0
JRNL AUTH H.WIZEMANN,J.H.O.GARBE,M.V.K.FRIEDRICH,R.TIMPL,T.SASAKI,
JRNL AUTH 2 E.HOHENESTER
JRNL TITL DISTINCT REQUIREMENTS FOR HEPARIN AND ALPHA-DYSTROGLYCAN
JRNL TITL 2 BINDING REVEALED BY STRUCTURE-BASED MUTAGENESIS OF THE
JRNL TITL 3 LAMININ ALPHA2 LG4-LG5 DOMAIN PAIR
JRNL REF J.MOL.BIOL. V. 332 635 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12963372
JRNL DOI 10.1016/S0022-2836(03)00848-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.TISI,J.F.TALTS,R.TIMPL,E.HOHENESTER
REMARK 1 TITL STRUCTURE OF THE C-TERMINAL LAMININ G-LIKE DOMAIN PAIR OF
REMARK 1 TITL 2 THE LAMININ ALPHA 2 CHAIN HARBOURING BINDIN SITES FOR
REMARK 1 TITL 3 ALPHA-DYSTROGLYCAN AND HEPARIN
REMARK 1 REF EMBO J. V. 19 1432 2000
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 10747011
REMARK 1 DOI 10.1093/EMBOJ/19.7.1432
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.F.TALTS,K.MANN,Y.YAMADA,R.TIMPL
REMARK 1 TITL STRUCTURAL ANALYSIS AND PROTEOLYTIC PROCESSING OF
REMARK 1 TITL 2 RECOMBINANT G DOMAIN OF MOUSE LAMININ ALPHA 2 CHAIN
REMARK 1 REF FEBS LETT. V. 426 71 1998
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 9598981
REMARK 1 DOI 10.1016/S0014-5793(98)00312-3
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 11805
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) : 0.220
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1199
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 : 2854
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : INDIVIDUAL RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.200 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.200 ; 4.000
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 1OKQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1290013185.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11824
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.23300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DYK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.91750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.91750
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.05500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.36700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.05500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.36700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 61.91750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.05500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.36700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 61.91750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.05500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.36700
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUES ASP 2808 ALA, ASP 2876 ALA
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 2725
REMARK 465 PRO A 2726
REMARK 465 LEU A 2727
REMARK 465 ALA A 2728
REMARK 465 SER A 2729
REMARK 465 VAL A 2730
REMARK 465 PRO A 2731
REMARK 465 THR A 2732
REMARK 465 PRO A 2733
REMARK 465 ALA A 2734
REMARK 465 PHE A 2735
REMARK 465 PRO A 2736
REMARK 465 PHE A 2737
REMARK 465 PRO A 2738
REMARK 465 VAL A 2739
REMARK 465 PRO A 2740
REMARK 465 THR A 2741
REMARK 465 MET A 2742
REMARK 465 VAL A 2743
REMARK 465 THR A 3118
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 PRO A2835 49.04 -65.46
REMARK 500 ASN A2839 50.82 -104.05
REMARK 500 LYS A2852 -106.04 59.46
REMARK 500 ASP A2860 -100.45 67.80
REMARK 500 PRO A2869 169.47 -47.93
REMARK 500 LYS A2870 -127.91 36.73
REMARK 500 ILE A2888 -84.56 -55.24
REMARK 500 ASN A2889 36.01 -78.74
REMARK 500 GLN A2920 75.99 -116.23
REMARK 500 ALA A2948 -78.43 -46.05
REMARK 500 PHE A2962 162.63 171.96
REMARK 500 ASP A2982 142.13 63.83
REMARK 500 GLU A2991 -7.05 70.44
REMARK 500 GLU A3011 -39.32 65.50
REMARK 500 LYS A3030 -107.59 64.06
REMARK 500 ASP A3055 84.34 -68.77
REMARK 500 ASN A3057 51.65 -168.65
REMARK 500 LYS A3091 -159.14 -130.28
REMARK 500 THR A3093 132.64 73.59
REMARK 500 LYS A3095 119.24 62.26
REMARK 500 PRO A3096 144.42 -39.55
REMARK 500 PHE A3101 -7.27 -50.54
REMARK 500 LYS A3103 35.23 -142.35
REMARK 500
REMARK 500 REMARK: NULL
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 CA A4002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A2861 OD2
REMARK 620 2 ASP A2982 OD2 161.7
REMARK 620 3 ASN A2999 O 94.6 95.9
REMARK 620 4 SER A3053 O 78.7 85.4 95.9
REMARK 620 5 ASP A3055 OD2 92.1 77.0 172.9 83.3
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A4002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QU0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE
REMARK 900 LAMININ ALPHA2 CHAIN
REMARK 900 RELATED ID: 1DYK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LAMININ ALPHA 2 CHAIN LG4-5 DOMAIN PAIR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 D8080A/D2876A DOUBLE MUTANT
REMARK 999 THE SWISSPROT SEQUENCE IS TAKEN FROM
REMARK 999 BERNIER S.M., UTANI A., SUGIYAMA S., DOI T., POLISTINA C.,
REMARK 999 YAMADA Y. MATRIX BIOL. 14:447-455(1995).
REMARK 999
REMARK 999 THE 21 RESIDUES OF THE C-TERMINUS DO NOT MATCH WITH
REMARK 999 THE SEQUENCE DATABASE REFERENCE PROVIDED.
REMARK 999 THE COORDINATE SECTION SHOWS COORDINATES TO RESIDUE
REMARK 999 3118 WHILE THE SEQUENCE DATABASE ENDS AT RESIDUE 3106
REMARK 999 THE CORRECTIONS TO THE SWS ENTRY Q60675 ARE DESCRIBED
REMARK 999 IN REFERENCE 1 (TALTS ET AL., 1998) OF THIS FILE
REMARK 999
REMARK 999 N-TERMINAL ALPHA RESIDUES ARE DERIVED FROM THE EXPRESSION
REMARK 999 SYSTEM VECTOR
DBREF 1OKQ A 2725 2728 PDB 1OKQ 1OKQ 2725 2728
DBREF 1OKQ A 2729 3093 UNP Q60675 LMA2_MOUSE 2729 3093
DBREF 1OKQ A 3094 3118 PDB 1OKQ 1OKQ 3094 3118
SEQADV 1OKQ ALA A 2773 UNP Q60675 VAL 2773 CONFLICT
SEQADV 1OKQ ALA A 2802 UNP Q60675 GLY 2802 CONFLICT
SEQADV 1OKQ ALA A 2808 UNP Q60675 ASP 2808 ENGINEERED MUTATION
SEQADV 1OKQ ALA A 2810 UNP Q60675 GLY 2810 CONFLICT
SEQADV 1OKQ TYR A 2820 UNP Q60675 PHE 2820 CONFLICT
SEQADV 1OKQ ASP A 2829 UNP Q60675 SER 2829 CONFLICT
SEQADV 1OKQ SER A 2831 UNP Q60675 ARG 2831 CONFLICT
SEQADV 1OKQ ALA A 2876 UNP Q60675 ASP 2876 ENGINEERED MUTATION
SEQADV 1OKQ VAL A 2878 UNP Q60675 GLY 2878 CONFLICT
SEQADV 1OKQ ALA A 2946 UNP Q60675 GLY 2946 CONFLICT
SEQADV 1OKQ LYS A 2953 UNP Q60675 ILE 2953 CONFLICT
SEQADV 1OKQ VAL A 2976 UNP Q60675 ILE 2976 CONFLICT
SEQADV 1OKQ HIS A 3022 UNP Q60675 TYR 3022 CONFLICT
SEQADV 1OKQ GLY A 3094 UNP Q60675 ALA 3094 CONFLICT
SEQRES 1 A 394 ALA PRO LEU ALA SER VAL PRO THR PRO ALA PHE PRO PHE
SEQRES 2 A 394 PRO VAL PRO THR MET VAL HIS GLY PRO CYS VAL ALA GLU
SEQRES 3 A 394 SER GLU PRO ALA LEU LEU THR GLY SER LYS GLN PHE GLY
SEQRES 4 A 394 LEU SER ARG ASN SER HIS ILE ALA ILE ALA PHE ASP ASP
SEQRES 5 A 394 THR LYS VAL LYS ASN ARG LEU THR ILE GLU LEU GLU VAL
SEQRES 6 A 394 ARG THR GLU ALA GLU SER GLY LEU LEU PHE TYR MET ALA
SEQRES 7 A 394 ARG ILE ASN HIS ALA ALA PHE ALA THR VAL GLN LEU ARG
SEQRES 8 A 394 ASN GLY PHE PRO TYR PHE SER TYR ASP LEU GLY SER GLY
SEQRES 9 A 394 ASP THR SER THR MET ILE PRO THR LYS ILE ASN ASP GLY
SEQRES 10 A 394 GLN TRP HIS LYS ILE LYS ILE VAL ARG VAL LYS GLN GLU
SEQRES 11 A 394 GLY ILE LEU TYR VAL ASP ASP ALA SER SER GLN THR ILE
SEQRES 12 A 394 SER PRO LYS LYS ALA ASP ILE LEU ALA VAL VAL GLY ILE
SEQRES 13 A 394 LEU TYR VAL GLY GLY LEU PRO ILE ASN TYR THR THR ARG
SEQRES 14 A 394 ARG ILE GLY PRO VAL THR TYR SER LEU ASP GLY CYS VAL
SEQRES 15 A 394 ARG ASN LEU HIS MET GLU GLN ALA PRO VAL ASP LEU ASP
SEQRES 16 A 394 GLN PRO THR SER SER PHE HIS VAL GLY THR CYS PHE ALA
SEQRES 17 A 394 ASN ALA GLU SER GLY THR TYR PHE ASP GLY THR GLY PHE
SEQRES 18 A 394 ALA LYS ALA VAL GLY GLY PHE LYS VAL GLY LEU ASP LEU
SEQRES 19 A 394 LEU VAL GLU PHE GLU PHE ARG THR THR ARG PRO THR GLY
SEQRES 20 A 394 VAL LEU LEU GLY VAL SER SER GLN LYS MET ASP GLY MET
SEQRES 21 A 394 GLY ILE GLU MET ILE ASP GLU LYS LEU MET PHE HIS VAL
SEQRES 22 A 394 ASP ASN GLY ALA GLY ARG PHE THR ALA ILE TYR ASP ALA
SEQRES 23 A 394 GLU ILE PRO GLY HIS MET CYS ASN GLY GLN TRP HIS LYS
SEQRES 24 A 394 VAL THR ALA LYS LYS ILE LYS ASN ARG LEU GLU LEU VAL
SEQRES 25 A 394 VAL ASP GLY ASN GLN VAL ASP ALA GLN SER PRO ASN SER
SEQRES 26 A 394 ALA SER THR SER ALA ASP THR ASN ASP PRO VAL PHE VAL
SEQRES 27 A 394 GLY GLY PHE PRO GLY GLY LEU ASN GLN PHE GLY LEU THR
SEQRES 28 A 394 THR ASN ILE ARG PHE ARG GLY CYS ILE ARG SER LEU LYS
SEQRES 29 A 394 LEU THR LYS GLY THR GLY LYS PRO LEU GLU VAL ASN PHE
SEQRES 30 A 394 ALA LYS ALA LEU GLU LEU ARG GLY VAL GLN PRO VAL SER
SEQRES 31 A 394 CYS PRO THR THR
HET CA A4002 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 HOH *38(H2 O)
HELIX 1 1 ASN A 3100 ALA A 3104 5 5
SHEET 1 AA 6 LYS A2760 PHE A2762 0
SHEET 2 AA 6 GLY A2904 MET A2911 -1 O GLY A2904 N PHE A2762
SHEET 3 AA 6 ARG A2782 THR A2791 -1 O GLU A2786 N HIS A2910
SHEET 4 AA 6 TRP A2843 VAL A2851 -1 O HIS A2844 N VAL A2789
SHEET 5 AA 6 GLU A2854 VAL A2859 -1 O GLU A2854 N VAL A2851
SHEET 6 AA 6 ALA A2862 ILE A2867 -1 O ALA A2862 N VAL A2859
SHEET 1 AB 7 ASP A2829 MET A2833 0
SHEET 2 AB 7 PHE A2818 ASP A2824 -1 O PHE A2821 N THR A2832
SHEET 3 AB 7 PHE A2809 ARG A2815 -1 O PHE A2809 N ASP A2824
SHEET 4 AB 7 GLY A2796 ALA A2802 -1 O GLY A2796 N LEU A2814
SHEET 5 AB 7 ILE A2880 VAL A2883 -1 O TYR A2882 N TYR A2800
SHEET 6 AB 7 HIS A2769 ALA A2773 -1 O ILE A2770 N VAL A2883
SHEET 7 AB 7 SER A2923 PHE A2925 -1 O SER A2923 N ALA A2771
SHEET 1 AC 2 ALA A2934 SER A2936 0
SHEET 2 AC 2 SER A3114 PRO A3116 -1 O CYS A3115 N GLU A2935
SHEET 1 AD 7 ARG A3003 TYR A3008 0
SHEET 2 AD 7 LYS A2992 ASP A2998 -1 O LEU A2993 N TYR A3008
SHEET 3 AD 7 GLY A2983 ILE A2989 -1 O GLY A2983 N ASP A2998
SHEET 4 AD 7 GLY A2971 SER A2977 -1 O GLY A2971 N MET A2988
SHEET 5 AD 7 PHE A3061 VAL A3062 -1 O PHE A3061 N GLY A2975
SHEET 6 AD 7 THR A2938 LYS A2947 -1 O ALA A2946 N VAL A3062
SHEET 7 AD 7 ARG A3081 LYS A3091 -1 O GLY A3082 N PHE A2940
SHEET 1 AE 7 ARG A3003 TYR A3008 0
SHEET 2 AE 7 LYS A2992 ASP A2998 -1 O LEU A2993 N TYR A3008
SHEET 3 AE 7 GLY A2983 ILE A2989 -1 O GLY A2983 N ASP A2998
SHEET 4 AE 7 GLY A2971 SER A2977 -1 O GLY A2971 N MET A2988
SHEET 5 AE 7 PHE A3061 VAL A3062 -1 O PHE A3061 N GLY A2975
SHEET 6 AE 7 THR A2938 LYS A2947 -1 O ALA A2946 N VAL A3062
SHEET 7 AE 7 GLU A3106 GLN A3111 -1 O GLU A3106 N LYS A2947
SSBOND 1 CYS A 2747 CYS A 3017 1555 1555 2.02
SSBOND 2 CYS A 2905 CYS A 2930 1555 1555 2.03
SSBOND 3 CYS A 3083 CYS A 3115 1555 1555 2.02
LINK OD2 ASP A2861 CA CA A4002 8456 1555 2.31
LINK OD2 ASP A2982 CA CA A4002 1555 1555 2.32
LINK O ASN A2999 CA CA A4002 1555 1555 2.25
LINK O SER A3053 CA CA A4002 1555 1555 2.19
LINK OD2 ASP A3055 CA CA A4002 1555 1555 2.35
SITE 1 AC1 5 ASP A2861 ASP A2982 ASN A2999 SER A3053
SITE 2 AC1 5 ASP A3055
CRYST1 70.110 110.734 123.835 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014263 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008075 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
