HEADER TRANSPORT PROTEIN 30-MAR-11 3RBX
TITLE MTHK RCK DOMAIN D184N MUTANT, CA2+-BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-GATED POTASSIUM CHANNEL MTHK;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 107-336;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 187420;
SOURCE 4 STRAIN: DELTA H;
SOURCE 5 GENE: MTHK, MTH_1520;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE80
KEYWDS K+ CHANNEL, RCK DOMAIN, ROSSMAN-FOLD, CA2+ BINDING DOMAIN, TRANSPORT
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SAMAKAI,B.S.ROTHBERG
REVDAT 2 21-FEB-24 3RBX 1 REMARK SEQADV LINK
REVDAT 1 12-OCT-11 3RBX 0
JRNL AUTH V.P.PAU,F.J.SMITH,A.B.TAYLOR,E.SAMAKAI,M.M.CALLAGHAN,
JRNL AUTH 2 K.ABARCA-HEIDEMANN,L.V.PARFENOVA,P.J.HART,B.S.ROTHBERG
JRNL TITL STRUCTURES OF MULTIPLE CA2+-BINDING SITES IN A K+ CHANNEL
JRNL TITL 2 RCK DOMAIN
JRNL REF PROC.NATL.ACAD.SCI.USA 2011
JRNL REFN ESSN 1091-6490
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 36614
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1832
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 49.4957 - 6.0292 0.99 3828 191 0.2209 0.2252
REMARK 3 2 6.0292 - 4.7868 1.00 3605 201 0.2183 0.2399
REMARK 3 3 4.7868 - 4.1821 1.00 3566 194 0.1806 0.2025
REMARK 3 4 4.1821 - 3.7999 1.00 3497 194 0.2202 0.2562
REMARK 3 5 3.7999 - 3.5276 1.00 3521 161 0.2393 0.2722
REMARK 3 6 3.5276 - 3.3197 1.00 3468 178 0.2629 0.3288
REMARK 3 7 3.3197 - 3.1535 0.99 3434 186 0.2799 0.3222
REMARK 3 8 3.1535 - 3.0162 0.98 3433 176 0.2970 0.3900
REMARK 3 9 3.0162 - 2.9001 0.96 3289 172 0.3359 0.3805
REMARK 3 10 2.9001 - 2.8000 0.91 3141 179 0.3918 0.4768
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 25.41
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.980
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) : -0.10200
REMARK 3 B22 (A**2) : -0.10200
REMARK 3 B33 (A**2) : 0.20400
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 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 : 0.009 10169
REMARK 3 ANGLE : 1.054 13760
REMARK 3 CHIRALITY : 0.071 1618
REMARK 3 PLANARITY : 0.003 1811
REMARK 3 DIHEDRAL : 15.477 3800
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1658
REMARK 3 RMSD : 0.063
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1653
REMARK 3 RMSD : 0.044
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1656
REMARK 3 RMSD : 0.065
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1668
REMARK 3 RMSD : 0.061
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 116:335 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1646
REMARK 3 RMSD : 0.053
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE SILICON(111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37176
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46800
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1 M CACL2, 0.1 M MES,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K, PH 5.7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 234.03467
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 117.01733
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 175.52600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.50867
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 292.54333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 234.03467
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 117.01733
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 58.50867
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 175.52600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 292.54333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 MET A 107
REMARK 465 GLY A 108
REMARK 465 LEU A 109
REMARK 465 ILE A 110
REMARK 465 ASP A 111
REMARK 465 VAL A 112
REMARK 465 ALA A 113
REMARK 465 LYS A 114
REMARK 465 SER A 115
REMARK 465 LEU A 337
REMARK 465 VAL A 338
REMARK 465 PRO A 339
REMARK 465 ARG A 340
REMARK 465 MET B 107
REMARK 465 GLY B 108
REMARK 465 LEU B 109
REMARK 465 ILE B 110
REMARK 465 ASP B 111
REMARK 465 VAL B 112
REMARK 465 ALA B 113
REMARK 465 LYS B 114
REMARK 465 SER B 115
REMARK 465 LEU B 337
REMARK 465 VAL B 338
REMARK 465 PRO B 339
REMARK 465 ARG B 340
REMARK 465 MET C 107
REMARK 465 GLY C 108
REMARK 465 LEU C 109
REMARK 465 ILE C 110
REMARK 465 ASP C 111
REMARK 465 VAL C 112
REMARK 465 ALA C 113
REMARK 465 LYS C 114
REMARK 465 SER C 115
REMARK 465 ALA C 336
REMARK 465 LEU C 337
REMARK 465 VAL C 338
REMARK 465 PRO C 339
REMARK 465 ARG C 340
REMARK 465 MET D 107
REMARK 465 GLY D 108
REMARK 465 LEU D 109
REMARK 465 ILE D 110
REMARK 465 ASP D 111
REMARK 465 VAL D 112
REMARK 465 ALA D 113
REMARK 465 LYS D 114
REMARK 465 SER D 115
REMARK 465 SER D 335
REMARK 465 ALA D 336
REMARK 465 LEU D 337
REMARK 465 VAL D 338
REMARK 465 PRO D 339
REMARK 465 ARG D 340
REMARK 465 MET E 107
REMARK 465 GLY E 108
REMARK 465 LEU E 109
REMARK 465 ILE E 110
REMARK 465 ASP E 111
REMARK 465 VAL E 112
REMARK 465 ALA E 113
REMARK 465 LYS E 114
REMARK 465 SER E 115
REMARK 465 ALA E 336
REMARK 465 LEU E 337
REMARK 465 VAL E 338
REMARK 465 PRO E 339
REMARK 465 ARG E 340
REMARK 465 MET F 107
REMARK 465 GLY F 108
REMARK 465 LEU F 109
REMARK 465 ILE F 110
REMARK 465 ASP F 111
REMARK 465 VAL F 112
REMARK 465 ALA F 113
REMARK 465 LYS F 114
REMARK 465 SER F 115
REMARK 465 SER F 335
REMARK 465 ALA F 336
REMARK 465 LEU F 337
REMARK 465 VAL F 338
REMARK 465 PRO F 339
REMARK 465 ARG F 340
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 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 ASP A 300 CG OD1 OD2
REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 313 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 325 CG CD OE1 OE2
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 GLU B 186 CG CD OE1 OE2
REMARK 470 GLU B 258 CG CD OE1 OE2
REMARK 470 ASP B 300 CG OD1 OD2
REMARK 470 GLU B 301 CG CD OE1 OE2
REMARK 470 LYS B 323 CG CD CE NZ
REMARK 470 ARG B 329 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 147 CG OD1 ND2
REMARK 470 ARG C 154 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 176 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 258 CG CD OE1 OE2
REMARK 470 GLU C 271 CG CD OE1 OE2
REMARK 470 LYS C 274 CG CD CE NZ
REMARK 470 VAL C 280 CG1 CG2
REMARK 470 LEU C 281 CG CD1 CD2
REMARK 470 ASP C 282 CG OD1 OD2
REMARK 470 ASP C 300 CG OD1 OD2
REMARK 470 ARG C 308 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 313 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 325 CG CD OE1 OE2
REMARK 470 ARG C 329 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 116 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 150 CG CD CE NZ
REMARK 470 GLU D 186 CG CD OE1 OE2
REMARK 470 GLU D 258 CG CD OE1 OE2
REMARK 470 GLU D 271 CG CD OE1 OE2
REMARK 470 ASP D 300 CG OD1 OD2
REMARK 470 ARG D 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 323 CG CD CE NZ
REMARK 470 ARG E 116 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 135 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 154 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 258 CG CD OE1 OE2
REMARK 470 ASP E 300 CG OD1 OD2
REMARK 470 ARG E 308 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 325 CG CD OE1 OE2
REMARK 470 ARG F 116 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 150 CG CD CE NZ
REMARK 470 GLU F 186 CG CD OE1 OE2
REMARK 470 GLU F 258 CG CD OE1 OE2
REMARK 470 GLU F 271 CG CD OE1 OE2
REMARK 470 ASP F 300 CG OD1 OD2
REMARK 470 GLU F 301 CG CD OE1 OE2
REMARK 470 ARG F 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 323 CG CD CE NZ
REMARK 470 ARG F 329 CG CD NE CZ NH1 NH2
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 ASP A 244 -71.69 -94.61
REMARK 500 GLU A 258 6.14 -69.41
REMARK 500 ASP A 284 52.47 31.99
REMARK 500 ILE A 334 -76.21 -95.11
REMARK 500 SER A 335 139.39 -5.65
REMARK 500 ASN B 174 71.28 49.93
REMARK 500 ASP B 244 -73.80 -92.25
REMARK 500 GLU B 258 8.14 -69.81
REMARK 500 ASP B 284 52.40 31.30
REMARK 500 ILE B 334 -75.60 -96.96
REMARK 500 SER B 335 138.89 -9.21
REMARK 500 ASN C 174 70.31 48.85
REMARK 500 ASP C 244 -72.43 -93.41
REMARK 500 ASP C 284 53.14 29.98
REMARK 500 ILE C 334 -75.60 -100.00
REMARK 500 ASN D 174 71.28 50.81
REMARK 500 ASP D 244 -70.77 -95.52
REMARK 500 ASP D 284 54.08 29.85
REMARK 500 ASN E 174 70.25 50.04
REMARK 500 ASP E 244 -72.44 -92.41
REMARK 500 ASP E 284 54.23 30.05
REMARK 500 ILE E 334 -73.66 -97.44
REMARK 500 ASN F 174 70.66 49.83
REMARK 500 ASP F 244 -73.21 -92.23
REMARK 500 ASP F 284 54.33 30.69
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 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 241 O
REMARK 620 2 ASP A 245 O 77.6
REMARK 620 3 GLU A 248 OE1 81.4 89.6
REMARK 620 4 GLU A 248 OE2 98.7 142.3 53.1
REMARK 620 5 GLU B 266 OE2 142.4 76.6 71.4 85.6
REMARK 620 6 GLU B 266 OE1 158.4 97.2 119.8 97.9 52.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 266 OE2
REMARK 620 2 GLU A 266 OE1 41.2
REMARK 620 3 ARG B 241 O 115.2 151.1
REMARK 620 4 ASP B 245 O 58.7 80.3 71.3
REMARK 620 5 GLU B 248 OE1 50.6 90.3 74.5 67.4
REMARK 620 6 GLU B 248 OE2 67.5 86.2 99.2 111.2 45.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 290 O
REMARK 620 2 GLU A 326 OE1 76.7
REMARK 620 3 GLU A 326 OE2 80.6 52.1
REMARK 620 4 ASP B 305 OD2 100.1 78.4 129.2
REMARK 620 5 ASP B 305 OD1 94.8 120.7 172.1 45.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 305 OD2
REMARK 620 2 ASP A 305 OD1 48.0
REMARK 620 3 GLY B 290 O 89.5 91.0
REMARK 620 4 GLU B 326 OE2 119.0 161.1 74.0
REMARK 620 5 GLU B 326 OE1 72.0 117.0 68.4 47.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 241 O
REMARK 620 2 ASP C 245 O 74.5
REMARK 620 3 GLU C 248 OE1 70.1 68.3
REMARK 620 4 GLU D 266 OE2 115.3 65.1 49.3
REMARK 620 5 GLU D 266 OE1 160.1 91.8 91.6 44.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 341 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 266 OE1
REMARK 620 2 ARG D 241 O 133.3
REMARK 620 3 ASP D 245 O 83.0 65.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 342 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 290 O
REMARK 620 2 GLU C 326 OE1 69.7
REMARK 620 3 GLU C 326 OE2 71.7 47.9
REMARK 620 4 ASP D 305 OD2 96.9 82.7 130.5
REMARK 620 5 ASP D 305 OD1 93.2 126.6 164.8 48.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 305 OD1
REMARK 620 2 ASP C 305 OD2 42.6
REMARK 620 3 GLY D 290 O 86.5 76.3
REMARK 620 4 GLU D 326 OE2 138.1 97.1 69.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG E 241 O
REMARK 620 2 GLU F 266 OE1 138.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 266 OE1
REMARK 620 2 GLU E 266 OE2 42.6
REMARK 620 3 ARG F 241 O 144.4 103.5
REMARK 620 4 ASP F 245 O 88.6 60.2 78.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 290 O
REMARK 620 2 GLU E 326 OE1 68.7
REMARK 620 3 GLU E 326 OE2 75.2 45.7
REMARK 620 4 ASP F 305 OD2 87.2 76.5 122.2
REMARK 620 5 ASP F 305 OD1 90.5 122.2 163.9 48.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 305 OD2
REMARK 620 2 ASP E 305 OD1 44.7
REMARK 620 3 GLY F 290 O 90.1 93.4
REMARK 620 4 GLU F 326 OE2 121.6 161.9 73.0
REMARK 620 5 GLU F 326 OE1 75.4 117.6 67.0 46.4
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 CA A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 342
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RBZ RELATED DB: PDB
DBREF 3RBX A 107 336 UNP O27564 MTHK_METTH 107 336
DBREF 3RBX B 107 336 UNP O27564 MTHK_METTH 107 336
DBREF 3RBX C 107 336 UNP O27564 MTHK_METTH 107 336
DBREF 3RBX D 107 336 UNP O27564 MTHK_METTH 107 336
DBREF 3RBX E 107 336 UNP O27564 MTHK_METTH 107 336
DBREF 3RBX F 107 336 UNP O27564 MTHK_METTH 107 336
SEQADV 3RBX ASN A 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU A 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL A 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO A 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG A 340 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ASN B 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU B 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL B 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO B 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG B 340 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ASN C 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU C 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL C 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO C 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG C 340 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ASN D 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU D 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL D 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO D 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG D 340 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ASN E 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU E 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL E 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO E 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG E 340 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ASN F 184 UNP O27564 ASP 184 ENGINEERED MUTATION
SEQADV 3RBX LEU F 337 UNP O27564 EXPRESSION TAG
SEQADV 3RBX VAL F 338 UNP O27564 EXPRESSION TAG
SEQADV 3RBX PRO F 339 UNP O27564 EXPRESSION TAG
SEQADV 3RBX ARG F 340 UNP O27564 EXPRESSION TAG
SEQRES 1 A 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 A 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 A 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 A 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 A 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 A 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 A 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 A 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 A 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 A 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 A 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 A 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 A 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 A 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 A 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 A 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 A 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 A 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
SEQRES 1 B 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 B 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 B 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 B 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 B 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 B 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 B 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 B 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 B 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 B 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 B 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 B 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 B 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 B 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 B 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 B 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 B 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 B 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
SEQRES 1 C 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 C 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 C 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 C 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 C 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 C 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 C 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 C 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 C 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 C 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 C 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 C 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 C 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 C 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 C 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 C 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 C 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 C 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
SEQRES 1 D 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 D 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 D 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 D 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 D 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 D 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 D 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 D 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 D 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 D 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 D 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 D 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 D 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 D 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 D 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 D 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 D 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 D 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
SEQRES 1 E 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 E 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 E 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 E 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 E 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 E 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 E 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 E 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 E 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 E 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 E 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 E 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 E 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 E 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 E 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 E 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 E 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 E 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
SEQRES 1 F 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 F 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 F 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 F 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 F 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 F 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASN
SEQRES 7 F 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 F 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 F 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 F 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 F 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 F 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 F 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 F 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 F 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 F 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 F 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 F 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
HET CA A 600 1
HET CA A 601 1
HET CA B 601 1
HET CA B 600 1
HET CA C 600 1
HET CA C 601 1
HET CA C 341 1
HET CA C 342 1
HET CA E 600 1
HET CA E 601 1
HET CA F 601 1
HET CA F 600 1
HETNAM CA CALCIUM ION
FORMUL 7 CA 12(CA 2+)
HELIX 1 1 SER A 124 LEU A 134 1 11
HELIX 2 2 ASP A 145 ASN A 147 5 3
HELIX 3 3 VAL A 148 SER A 155 1 8
HELIX 4 4 ARG A 166 ALA A 173 1 8
HELIX 5 5 SER A 187 ASP A 202 1 16
HELIX 6 6 ARG A 213 GLU A 215 5 3
HELIX 7 7 ASN A 216 GLY A 224 1 9
HELIX 8 8 SER A 230 SER A 242 1 13
HELIX 9 9 GLY A 246 LEU A 256 1 11
HELIX 10 10 SER A 279 ASP A 284 1 6
HELIX 11 11 ASP A 284 GLY A 290 1 7
HELIX 12 12 LYS A 323 SER A 335 1 13
HELIX 13 13 SER B 124 LEU B 134 1 11
HELIX 14 14 ASP B 145 ASN B 147 5 3
HELIX 15 15 VAL B 148 SER B 155 1 8
HELIX 16 16 ARG B 166 ALA B 173 1 8
HELIX 17 17 SER B 187 ASP B 202 1 16
HELIX 18 18 ARG B 213 GLU B 215 5 3
HELIX 19 19 ASN B 216 GLY B 224 1 9
HELIX 20 20 SER B 230 SER B 242 1 13
HELIX 21 21 GLY B 246 LEU B 256 1 11
HELIX 22 22 SER B 279 ASP B 284 1 6
HELIX 23 23 ASP B 284 GLY B 290 1 7
HELIX 24 24 LYS B 323 SER B 335 1 13
HELIX 25 25 SER C 124 LEU C 134 1 11
HELIX 26 26 ASP C 145 ASN C 147 5 3
HELIX 27 27 VAL C 148 SER C 155 1 8
HELIX 28 28 ARG C 166 ALA C 173 1 8
HELIX 29 29 SER C 187 ASP C 202 1 16
HELIX 30 30 ARG C 213 GLU C 215 5 3
HELIX 31 31 ASN C 216 GLY C 224 1 9
HELIX 32 32 SER C 230 SER C 242 1 13
HELIX 33 33 GLY C 246 LEU C 256 1 11
HELIX 34 34 SER C 279 ASP C 284 1 6
HELIX 35 35 ASP C 284 GLY C 290 1 7
HELIX 36 36 LYS C 323 SER C 335 1 13
HELIX 37 37 SER D 124 LEU D 134 1 11
HELIX 38 38 ASP D 145 ASN D 147 5 3
HELIX 39 39 VAL D 148 SER D 155 1 8
HELIX 40 40 ARG D 166 ALA D 173 1 8
HELIX 41 41 SER D 187 ASP D 202 1 16
HELIX 42 42 ARG D 213 GLU D 215 5 3
HELIX 43 43 ASN D 216 GLY D 224 1 9
HELIX 44 44 SER D 230 ARG D 241 1 12
HELIX 45 45 GLY D 246 LEU D 256 1 11
HELIX 46 46 SER D 279 ASP D 284 1 6
HELIX 47 47 ASP D 284 GLY D 290 1 7
HELIX 48 48 LYS D 323 ILE D 334 1 12
HELIX 49 49 SER E 124 LEU E 134 1 11
HELIX 50 50 ASP E 145 ASN E 147 5 3
HELIX 51 51 VAL E 148 SER E 155 1 8
HELIX 52 52 ARG E 166 ALA E 173 1 8
HELIX 53 53 SER E 187 ASP E 202 1 16
HELIX 54 54 ARG E 213 GLU E 215 5 3
HELIX 55 55 ASN E 216 GLY E 224 1 9
HELIX 56 56 SER E 230 SER E 242 1 13
HELIX 57 57 GLY E 246 LEU E 256 1 11
HELIX 58 58 SER E 279 ASP E 284 1 6
HELIX 59 59 ASP E 284 GLY E 290 1 7
HELIX 60 60 LYS E 323 SER E 335 1 13
HELIX 61 61 SER F 124 LEU F 134 1 11
HELIX 62 62 ASP F 145 ASN F 147 5 3
HELIX 63 63 VAL F 148 SER F 155 1 8
HELIX 64 64 ARG F 166 ALA F 173 1 8
HELIX 65 65 SER F 187 ASP F 202 1 16
HELIX 66 66 ARG F 213 GLU F 215 5 3
HELIX 67 67 ASN F 216 GLY F 224 1 9
HELIX 68 68 SER F 230 ARG F 241 1 12
HELIX 69 69 GLY F 246 LEU F 256 1 11
HELIX 70 70 SER F 279 ASP F 284 1 6
HELIX 71 71 ASP F 284 GLY F 290 1 7
HELIX 72 72 LYS F 323 ILE F 334 1 12
SHEET 1 A 6 ASN A 158 HIS A 161 0
SHEET 2 A 6 VAL A 139 ALA A 143 1 N VAL A 141 O ASN A 158
SHEET 3 A 6 VAL A 118 CYS A 121 1 N ILE A 120 O PHE A 140
SHEET 4 A 6 ALA A 180 VAL A 183 1 O ILE A 182 N CYS A 121
SHEET 5 A 6 ILE A 207 GLU A 210 1 O ILE A 208 N VAL A 183
SHEET 6 A 6 GLN A 227 ILE A 229 1 O ILE A 229 N ALA A 209
SHEET 1 B 4 ARG A 263 PRO A 268 0
SHEET 2 B 4 ILE A 317 GLY A 322 -1 O ILE A 318 N VAL A 267
SHEET 3 B 4 ILE A 292 ARG A 298 -1 N GLY A 295 O LEU A 319
SHEET 4 B 4 GLU A 301 ILE A 304 -1 O ILE A 303 N VAL A 296
SHEET 1 C 6 ASN B 158 HIS B 161 0
SHEET 2 C 6 VAL B 139 ALA B 143 1 N VAL B 141 O ASN B 158
SHEET 3 C 6 VAL B 118 CYS B 121 1 N ILE B 120 O PHE B 140
SHEET 4 C 6 ALA B 180 VAL B 183 1 O ILE B 182 N CYS B 121
SHEET 5 C 6 ARG B 206 GLU B 210 1 O ARG B 206 N VAL B 181
SHEET 6 C 6 GLN B 227 ILE B 229 1 O ILE B 229 N ALA B 209
SHEET 1 D 4 ARG B 263 PRO B 268 0
SHEET 2 D 4 ILE B 317 GLY B 322 -1 O ILE B 318 N VAL B 267
SHEET 3 D 4 ILE B 292 ARG B 298 -1 N GLY B 297 O ILE B 317
SHEET 4 D 4 GLU B 301 ILE B 304 -1 O ILE B 303 N VAL B 296
SHEET 1 E 6 ASN C 158 HIS C 161 0
SHEET 2 E 6 VAL C 139 ALA C 143 1 N VAL C 141 O ASN C 158
SHEET 3 E 6 VAL C 118 CYS C 121 1 N ILE C 120 O PHE C 140
SHEET 4 E 6 ALA C 180 VAL C 183 1 O ILE C 182 N CYS C 121
SHEET 5 E 6 ARG C 206 GLU C 210 1 O ARG C 206 N VAL C 181
SHEET 6 E 6 GLN C 227 ILE C 229 1 O ILE C 229 N ALA C 209
SHEET 1 F 4 ARG C 263 PRO C 268 0
SHEET 2 F 4 ILE C 317 GLY C 322 -1 O GLY C 320 N VAL C 265
SHEET 3 F 4 ILE C 292 ARG C 298 -1 N GLY C 295 O LEU C 319
SHEET 4 F 4 GLU C 301 ILE C 304 -1 O ILE C 303 N VAL C 296
SHEET 1 G 6 ASN D 158 HIS D 161 0
SHEET 2 G 6 VAL D 139 ALA D 143 1 N VAL D 141 O ASN D 158
SHEET 3 G 6 VAL D 118 CYS D 121 1 N ILE D 120 O PHE D 140
SHEET 4 G 6 ALA D 180 VAL D 183 1 O ILE D 182 N CYS D 121
SHEET 5 G 6 ARG D 206 GLU D 210 1 O ILE D 208 N VAL D 183
SHEET 6 G 6 GLN D 227 ILE D 229 1 O ILE D 229 N ALA D 209
SHEET 1 H 4 ARG D 263 PRO D 268 0
SHEET 2 H 4 ILE D 317 GLY D 322 -1 O ILE D 318 N VAL D 267
SHEET 3 H 4 ILE D 292 ARG D 298 -1 N GLY D 297 O ILE D 317
SHEET 4 H 4 GLU D 301 ILE D 304 -1 O ILE D 303 N VAL D 296
SHEET 1 I 6 ASN E 158 HIS E 161 0
SHEET 2 I 6 VAL E 139 ALA E 143 1 N VAL E 141 O ASN E 158
SHEET 3 I 6 VAL E 118 CYS E 121 1 N ILE E 120 O PHE E 140
SHEET 4 I 6 ALA E 180 VAL E 183 1 O ILE E 182 N CYS E 121
SHEET 5 I 6 ARG E 206 GLU E 210 1 O ILE E 208 N VAL E 183
SHEET 6 I 6 GLN E 227 ILE E 229 1 O ILE E 229 N ALA E 209
SHEET 1 J 4 ARG E 263 PRO E 268 0
SHEET 2 J 4 ILE E 317 GLY E 322 -1 O ILE E 318 N VAL E 267
SHEET 3 J 4 ILE E 292 ARG E 298 -1 N GLY E 295 O LEU E 319
SHEET 4 J 4 GLU E 301 ILE E 304 -1 O ILE E 303 N VAL E 296
SHEET 1 K 6 ASN F 158 HIS F 161 0
SHEET 2 K 6 VAL F 139 ALA F 143 1 N VAL F 141 O ASN F 158
SHEET 3 K 6 VAL F 118 CYS F 121 1 N ILE F 120 O PHE F 140
SHEET 4 K 6 ALA F 180 VAL F 183 1 O ILE F 182 N CYS F 121
SHEET 5 K 6 ILE F 207 GLU F 210 1 O ILE F 208 N VAL F 183
SHEET 6 K 6 GLN F 227 ILE F 229 1 O ILE F 229 N ALA F 209
SHEET 1 L 4 ARG F 263 PRO F 268 0
SHEET 2 L 4 ILE F 317 GLY F 322 -1 O ILE F 318 N VAL F 267
SHEET 3 L 4 ILE F 292 ARG F 298 -1 N GLY F 297 O ILE F 317
SHEET 4 L 4 GLU F 301 ILE F 304 -1 O ILE F 303 N VAL F 296
LINK O ARG A 241 CA CA A 600 1555 1555 2.53
LINK O ASP A 245 CA CA A 600 1555 1555 2.58
LINK OE1 GLU A 248 CA CA A 600 1555 1555 2.03
LINK OE2 GLU A 248 CA CA A 600 1555 1555 2.73
LINK OE2 GLU A 266 CA CA B 600 1555 1555 3.10
LINK OE1 GLU A 266 CA CA B 600 1555 1555 3.14
LINK O GLY A 290 CA CA A 601 1555 1555 2.35
LINK OD2 ASP A 305 CA CA B 601 1555 1555 2.59
LINK OD1 ASP A 305 CA CA B 601 1555 1555 2.85
LINK OE1 GLU A 326 CA CA A 601 1555 1555 2.47
LINK OE2 GLU A 326 CA CA A 601 1555 1555 2.55
LINK CA CA A 600 OE2 GLU B 266 1555 1555 2.13
LINK CA CA A 600 OE1 GLU B 266 1555 1555 2.70
LINK CA CA A 601 OD2 ASP B 305 1555 1555 2.71
LINK CA CA A 601 OD1 ASP B 305 1555 1555 3.03
LINK O ARG B 241 CA CA B 600 1555 1555 2.34
LINK O ASP B 245 CA CA B 600 1555 1555 3.12
LINK OE1 GLU B 248 CA CA B 600 1555 1555 2.75
LINK OE2 GLU B 248 CA CA B 600 1555 1555 2.95
LINK O GLY B 290 CA CA B 601 1555 1555 2.63
LINK OE2 GLU B 326 CA CA B 601 1555 1555 2.70
LINK OE1 GLU B 326 CA CA B 601 1555 1555 2.80
LINK O ARG C 241 CA CA C 600 1555 1555 2.38
LINK O ASP C 245 CA CA C 600 1555 1555 2.91
LINK OE1 GLU C 248 CA CA C 600 1555 1555 2.92
LINK OE1 GLU C 266 CA CA C 341 1555 1555 2.94
LINK O GLY C 290 CA CA C 342 1555 1555 2.67
LINK OD1 ASP C 305 CA CA C 601 1555 1555 2.91
LINK OD2 ASP C 305 CA CA C 601 1555 1555 3.18
LINK OE1 GLU C 326 CA CA C 342 1555 1555 2.60
LINK OE2 GLU C 326 CA CA C 342 1555 1555 2.79
LINK CA CA C 341 O ARG D 241 1555 1555 2.85
LINK CA CA C 341 O ASP D 245 1555 1555 3.11
LINK CA CA C 342 OD2 ASP D 305 1555 1555 2.48
LINK CA CA C 342 OD1 ASP D 305 1555 1555 2.89
LINK CA CA C 600 OE2 GLU D 266 1555 1555 2.86
LINK CA CA C 600 OE1 GLU D 266 1555 1555 2.90
LINK CA CA C 601 O GLY D 290 1555 1555 2.71
LINK CA CA C 601 OE2 GLU D 326 1555 1555 3.02
LINK O ARG E 241 CA CA E 600 1555 1555 2.74
LINK OE1 GLU E 266 CA CA F 600 1555 1555 2.93
LINK OE2 GLU E 266 CA CA F 600 1555 1555 3.13
LINK O GLY E 290 CA CA E 601 1555 1555 2.55
LINK OD2 ASP E 305 CA CA F 601 1555 1555 2.75
LINK OD1 ASP E 305 CA CA F 601 1555 1555 3.02
LINK OE1 GLU E 326 CA CA E 601 1555 1555 2.82
LINK OE2 GLU E 326 CA CA E 601 1555 1555 2.83
LINK CA CA E 600 OE1 GLU F 266 1555 1555 2.86
LINK CA CA E 601 OD2 ASP F 305 1555 1555 2.50
LINK CA CA E 601 OD1 ASP F 305 1555 1555 2.93
LINK O ARG F 241 CA CA F 600 1555 1555 2.31
LINK O ASP F 245 CA CA F 600 1555 1555 2.75
LINK O GLY F 290 CA CA F 601 1555 1555 2.52
LINK OE2 GLU F 326 CA CA F 601 1555 1555 2.78
LINK OE1 GLU F 326 CA CA F 601 1555 1555 2.81
SITE 1 AC1 4 ARG A 241 ASP A 245 GLU A 248 GLU B 266
SITE 1 AC2 3 ASP A 305 GLY B 290 GLU B 326
SITE 1 AC3 4 GLU A 266 ARG B 241 ASP B 245 GLU B 248
SITE 1 AC4 3 GLY A 290 GLU A 326 ASP B 305
SITE 1 AC5 4 ARG C 241 ASP C 245 GLU C 248 GLU D 266
SITE 1 AC6 3 ASP C 305 GLY D 290 GLU D 326
SITE 1 AC7 4 GLU C 266 ARG D 241 ASP D 245 GLU D 248
SITE 1 AC8 3 GLY C 290 GLU C 326 ASP D 305
SITE 1 AC9 4 ARG E 241 ASP E 245 GLU E 248 GLU F 266
SITE 1 BC1 3 ASP E 305 GLY F 290 GLU F 326
SITE 1 BC2 4 GLU E 266 ARG F 241 ASP F 245 GLU F 248
SITE 1 BC3 3 GLY E 290 GLU E 326 ASP F 305
CRYST1 119.120 119.120 351.052 90.00 90.00 120.00 P 65 2 2 72
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 0.008395 0.004847 0.000000 0.00000
SCALE2 0.000000 0.009694 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
