HEADER METAL BINDING PROTEIN 05-AUG-13 4M2O
TITLE CRYSTAL STRUCTURE OF A NON-MYRISTOYLATED C39A RECOVERIN MUTANT WITH
TITLE 2 ONE CALCIUM ION BOUND TO EF-HAND 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECOVERIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P26;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: RCV1, RCVRN, RECOVERIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: T7 EXPRESS (NEB);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CALCIUM BINDING PROTEIN, EF HAND, NEURONAL CALCIUM SENSING (NCS)
KEYWDS 2 FAMILY PROTEIN, INHIBITS RHODOPSIN KINASE, RHODOPSIN KINASE, RETINA,
KEYWDS 3 METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.PREM KUMAR,M.J.RANAGHAN,D.D.OPRIAN
REVDAT 4 20-SEP-23 4M2O 1 REMARK SEQADV LINK
REVDAT 3 01-JAN-14 4M2O 1 JRNL
REVDAT 2 20-NOV-13 4M2O 1 REMARK
REVDAT 1 13-NOV-13 4M2O 0
JRNL AUTH M.J.RANAGHAN,R.P.KUMAR,K.S.CHAKRABARTI,V.BUOSI,D.KERN,
JRNL AUTH 2 D.D.OPRIAN
JRNL TITL A HIGHLY CONSERVED CYSTEINE OF NEURONAL CALCIUM-SENSING
JRNL TITL 2 PROTEINS CONTROLS COOPERATIVE BINDING OF CA2+ TO RECOVERIN.
JRNL REF J.BIOL.CHEM. V. 288 36160 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 24189072
JRNL DOI 10.1074/JBC.M113.524355
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 32755
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1661
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.7069 - 3.4329 1.00 2665 145 0.1911 0.1933
REMARK 3 2 3.4329 - 2.7253 1.00 2632 133 0.1785 0.1906
REMARK 3 3 2.7253 - 2.3809 1.00 2621 119 0.1728 0.1664
REMARK 3 4 2.3809 - 2.1633 1.00 2629 126 0.1710 0.1858
REMARK 3 5 2.1633 - 2.0083 1.00 2568 141 0.1736 0.1857
REMARK 3 6 2.0083 - 1.8899 0.99 2575 157 0.1825 0.1848
REMARK 3 7 1.8899 - 1.7953 0.99 2576 127 0.1920 0.2303
REMARK 3 8 1.7953 - 1.7171 0.99 2567 171 0.2035 0.2312
REMARK 3 9 1.7171 - 1.6510 0.99 2557 142 0.2142 0.2308
REMARK 3 10 1.6510 - 1.5940 0.99 2586 141 0.2126 0.2522
REMARK 3 11 1.5940 - 1.5442 0.99 2538 127 0.2233 0.2555
REMARK 3 12 1.5442 - 1.5001 0.99 2580 132 0.2309 0.2686
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.60
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1644
REMARK 3 ANGLE : 1.057 2225
REMARK 3 CHIRALITY : 0.080 239
REMARK 3 PLANARITY : 0.005 289
REMARK 3 DIHEDRAL : 15.068 631
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4M2O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081389.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-13
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32871
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 31.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OMR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM CITRATE, PH 7.0,
REMARK 280 TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 42.02500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.02500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.49500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.02500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.02500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.49500
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 42.02500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 42.02500
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 29.49500
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 42.02500
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 42.02500
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 29.49500
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: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 168.10000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 84.05000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -84.05000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 84.05000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 84.05000
REMARK 350 BIOMT3 4 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 GLY A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 SER A 6
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 NE2 GLN A 187 OE2 GLU A 189 2.00
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 8 45.87 -94.72
REMARK 500 GLN A 18 -119.00 50.18
REMARK 500 ASP A 74 5.85 -150.98
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 A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 OD1
REMARK 620 2 ASP A 112 OD1 83.9
REMARK 620 3 ASN A 114 OD1 88.8 74.6
REMARK 620 4 THR A 116 O 82.0 150.0 78.8
REMARK 620 5 GLU A 121 OE1 102.1 126.2 157.0 82.8
REMARK 620 6 GLU A 121 OE2 100.7 74.4 146.3 134.3 51.8
REMARK 620 7 HOH A 301 O 173.8 100.8 88.7 92.0 78.3 84.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OMR RELATED DB: PDB
REMARK 900 SEARCH MODEL
REMARK 900 RELATED ID: 4M2P RELATED DB: PDB
REMARK 900 RELATED ID: 4M2Q RELATED DB: PDB
REMARK 900 RELATED ID: 4MLW RELATED DB: PDB
DBREF 4M2O A 2 197 UNP P21457 RECO_BOVIN 2 197
SEQADV 4M2O ALA A 39 UNP P21457 CYS 39 ENGINEERED MUTATION
SEQRES 1 A 196 GLY ASN SER LYS SER GLY ALA LEU SER LYS GLU ILE LEU
SEQRES 2 A 196 GLU GLU LEU GLN LEU ASN THR LYS PHE THR GLU GLU GLU
SEQRES 3 A 196 LEU SER SER TRP TYR GLN SER PHE LEU LYS GLU ALA PRO
SEQRES 4 A 196 SER GLY ARG ILE THR ARG GLN GLU PHE GLN THR ILE TYR
SEQRES 5 A 196 SER LYS PHE PHE PRO GLU ALA ASP PRO LYS ALA TYR ALA
SEQRES 6 A 196 GLN HIS VAL PHE ARG SER PHE ASP ALA ASN SER ASP GLY
SEQRES 7 A 196 THR LEU ASP PHE LYS GLU TYR VAL ILE ALA LEU HIS MET
SEQRES 8 A 196 THR SER ALA GLY LYS THR ASN GLN LYS LEU GLU TRP ALA
SEQRES 9 A 196 PHE SER LEU TYR ASP VAL ASP GLY ASN GLY THR ILE SER
SEQRES 10 A 196 LYS ASN GLU VAL LEU GLU ILE VAL THR ALA ILE PHE LYS
SEQRES 11 A 196 MET ILE SER PRO GLU ASP THR LYS HIS LEU PRO GLU ASP
SEQRES 12 A 196 GLU ASN THR PRO GLU LYS ARG ALA GLU LYS ILE TRP GLY
SEQRES 13 A 196 PHE PHE GLY LYS LYS ASP ASP ASP LYS LEU THR GLU LYS
SEQRES 14 A 196 GLU PHE ILE GLU GLY THR LEU ALA ASN LYS GLU ILE LEU
SEQRES 15 A 196 ARG LEU ILE GLN PHE GLU PRO GLN LYS VAL LYS GLU LYS
SEQRES 16 A 196 LEU
HET CA A 201 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 HOH *164(H2 O)
HELIX 1 1 LEU A 9 GLN A 18 1 10
HELIX 2 2 LEU A 19 THR A 21 5 3
HELIX 3 3 THR A 24 ALA A 39 1 16
HELIX 4 4 ARG A 46 PHE A 57 1 12
HELIX 5 5 PRO A 62 SER A 72 1 11
HELIX 6 6 PHE A 83 ALA A 95 1 13
HELIX 7 7 LYS A 97 GLN A 100 5 4
HELIX 8 8 LYS A 101 ASP A 110 1 10
HELIX 9 9 SER A 118 LYS A 131 1 14
HELIX 10 10 SER A 134 LYS A 139 1 6
HELIX 11 11 HIS A 140 LEU A 141 5 2
HELIX 12 12 PRO A 142 ASN A 146 5 5
HELIX 13 13 THR A 147 PHE A 159 1 13
HELIX 14 14 THR A 168 ASN A 179 1 12
HELIX 15 15 ASN A 179 GLN A 187 1 9
SHEET 1 A 2 ARG A 43 THR A 45 0
SHEET 2 A 2 THR A 80 ASP A 82 -1 O LEU A 81 N ILE A 44
LINK OD1 ASP A 110 CA CA A 201 1555 1555 2.30
LINK OD1 ASP A 112 CA CA A 201 1555 1555 2.43
LINK OD1 ASN A 114 CA CA A 201 1555 1555 2.37
LINK O THR A 116 CA CA A 201 1555 1555 2.31
LINK OE1 GLU A 121 CA CA A 201 1555 1555 2.51
LINK OE2 GLU A 121 CA CA A 201 1555 1555 2.51
LINK CA CA A 201 O HOH A 301 1555 1555 2.38
SITE 1 AC1 6 ASP A 110 ASP A 112 ASN A 114 THR A 116
SITE 2 AC1 6 GLU A 121 HOH A 301
CRYST1 84.050 84.050 58.990 90.00 90.00 90.00 I 4 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 0.011898 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016952 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
