HEADER STRUCTURAL PROTEIN 01-SEP-15 5DII
TITLE STRUCTURE OF AN ENGINEERED BACTERIAL MICROCOMPARTMENT SHELL PROTEIN
TITLE 2 BINDING A [4FE-4S] CLUSTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROCOMPARTMENTS PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALIANGIUM OCHRACEUM (STRAIN DSM 14365 / JCM
SOURCE 3 11303 / SMP-2);
SOURCE 4 ORGANISM_TAXID: 502025;
SOURCE 5 STRAIN: DSM 14365 / JCM 11303 / SMP-2;
SOURCE 6 GENE: HOCH_5812;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED PROTEIN, BACTERIAL MICROCOMPARTMENTS, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUTTER,C.AUSSIGNARGUES,A.TURMO,C.A.KERFELD
REVDAT 3 27-SEP-23 5DII 1 REMARK LINK
REVDAT 2 11-MAY-16 5DII 1 JRNL
REVDAT 1 03-FEB-16 5DII 0
JRNL AUTH C.AUSSIGNARGUES,M.E.PANDELIA,M.SUTTER,J.S.PLEGARIA,
JRNL AUTH 2 J.ZARZYCKI,A.TURMO,J.HUANG,D.C.DUCAT,E.L.HEGG,B.R.GIBNEY,
JRNL AUTH 3 C.A.KERFELD
JRNL TITL STRUCTURE AND FUNCTION OF A BACTERIAL MICROCOMPARTMENT SHELL
JRNL TITL 2 PROTEIN ENGINEERED TO BIND A [4FE-4S] CLUSTER.
JRNL REF J.AM.CHEM.SOC. V. 138 5262 2016
JRNL REFN ESSN 1520-5126
JRNL PMID 26704697
JRNL DOI 10.1021/JACS.5B11734
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1690
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 176084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1989
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 38.6336 - 5.3396 0.98 7244 159 0.1715 0.1783
REMARK 3 2 5.3396 - 4.2399 0.94 6907 151 0.1473 0.1589
REMARK 3 3 4.2399 - 3.7044 0.93 6947 146 0.1390 0.1465
REMARK 3 4 3.7044 - 3.3659 0.93 6917 145 0.1583 0.1844
REMARK 3 5 3.3659 - 3.1248 0.93 6861 154 0.1571 0.2288
REMARK 3 6 3.1248 - 2.9406 0.92 6887 144 0.1656 0.2493
REMARK 3 7 2.9406 - 2.7934 0.92 6847 146 0.1638 0.2188
REMARK 3 8 2.7934 - 2.6718 0.91 6703 125 0.1610 0.1966
REMARK 3 9 2.6718 - 2.5690 0.91 6841 137 0.1814 0.2443
REMARK 3 10 2.5690 - 2.4804 0.91 6711 168 0.1855 0.2496
REMARK 3 11 2.4804 - 2.4028 0.91 6672 134 0.1794 0.2013
REMARK 3 12 2.4028 - 2.3342 0.90 6730 159 0.1870 0.2091
REMARK 3 13 2.3342 - 2.2727 0.89 6589 136 0.1916 0.2314
REMARK 3 14 2.2727 - 2.2173 0.90 6669 142 0.1935 0.2434
REMARK 3 15 2.2173 - 2.1669 0.89 6646 148 0.2040 0.2237
REMARK 3 16 2.1669 - 2.1208 0.89 6593 126 0.2118 0.2397
REMARK 3 17 2.1208 - 2.0783 0.88 6530 174 0.2207 0.2676
REMARK 3 18 2.0783 - 2.0391 0.88 6525 112 0.2360 0.3276
REMARK 3 19 2.0391 - 2.0027 0.89 6632 136 0.2599 0.2867
REMARK 3 20 2.0027 - 1.9688 0.88 6475 160 0.2758 0.2991
REMARK 3 21 1.9688 - 1.9370 0.88 6496 115 0.2953 0.2931
REMARK 3 22 1.9370 - 1.9072 0.87 6470 156 0.3059 0.3769
REMARK 3 23 1.9072 - 1.8792 0.87 6471 133 0.3208 0.3022
REMARK 3 24 1.8792 - 1.8527 0.87 6391 132 0.3489 0.3699
REMARK 3 25 1.8527 - 1.8277 0.86 6574 137 0.3684 0.3606
REMARK 3 26 1.8277 - 1.8039 0.70 5056 125 0.3887 0.3898
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.390
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 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 : 0.010 8971
REMARK 3 ANGLE : 1.401 12183
REMARK 3 CHIRALITY : 0.050 1458
REMARK 3 PLANARITY : 0.006 1583
REMARK 3 DIHEDRAL : 12.431 3297
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 5DII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000211782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977408
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 176094
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 38.625
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 5DIH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 250MM NA ACETATE TRIHYDRATE, 100MM
REMARK 280 TRIS PH 8.5, 26% PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 TRP A 114
REMARK 465 GLU A 115
REMARK 465 GLU A 116
REMARK 465 ASP A 117
REMARK 465 THR A 118
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 GLU B 115
REMARK 465 GLU B 116
REMARK 465 ASP B 117
REMARK 465 THR B 118
REMARK 465 ALA C 14
REMARK 465 GLY C 15
REMARK 465 GLU C 115
REMARK 465 GLU C 116
REMARK 465 ASP C 117
REMARK 465 THR C 118
REMARK 465 MET D 1
REMARK 465 ASP D 2
REMARK 465 HIS D 3
REMARK 465 GLU D 198
REMARK 465 LEU D 199
REMARK 465 ARG D 200
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 HIS E 3
REMARK 465 ALA E 4
REMARK 465 PRO E 5
REMARK 465 GLU E 6
REMARK 465 GLU E 115
REMARK 465 GLU E 116
REMARK 465 ASP E 117
REMARK 465 THR E 118
REMARK 465 MET F 1
REMARK 465 ASP F 2
REMARK 465 HIS F 3
REMARK 465 ALA F 4
REMARK 465 GLU F 115
REMARK 465 GLU F 116
REMARK 465 ASP F 117
REMARK 465 THR F 118
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 CYS B 55 HG SER B 56 1.51
REMARK 500 O HOH E 345 O HOH E 354 2.07
REMARK 500 O HOH B 352 O HOH B 367 2.15
REMARK 500 O HOH E 355 O HOH E 372 2.16
REMARK 500 O HOH B 368 O HOH B 373 2.16
REMARK 500 NH1 ARG C 103 O HOH C 301 2.17
REMARK 500 O HOH D 427 O HOH D 461 2.18
REMARK 500 O HOH C 321 O HOH C 345 2.19
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 PRO A 45 43.45 -80.31
REMARK 500 SER A 56 -9.94 90.88
REMARK 500 ALA A 153 -52.20 69.84
REMARK 500 PRO B 45 43.61 -79.02
REMARK 500 SER B 56 -9.56 93.86
REMARK 500 ALA B 153 -49.31 69.05
REMARK 500 PRO C 45 47.11 -78.63
REMARK 500 SER C 56 -11.02 93.40
REMARK 500 ALA C 153 -50.52 68.98
REMARK 500 PRO D 45 43.31 -80.01
REMARK 500 SER D 56 -10.28 92.19
REMARK 500 ALA D 153 -50.90 69.00
REMARK 500 PRO E 45 42.65 -77.37
REMARK 500 SER E 56 -10.32 92.81
REMARK 500 ALA E 153 -50.69 70.41
REMARK 500 PRO F 45 45.38 -79.75
REMARK 500 SER F 56 -6.09 91.43
REMARK 500 ALA F 153 -52.08 68.46
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 C 359 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH E 380 DISTANCE = 5.98 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 SF4 A 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 55 SG
REMARK 620 2 SF4 A 301 S2 123.9
REMARK 620 3 SF4 A 301 S3 122.1 99.2
REMARK 620 4 SF4 A 301 S4 109.2 99.7 97.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 55 SG
REMARK 620 2 SF4 A 301 S1 124.1
REMARK 620 3 SF4 A 301 S3 123.7 99.7
REMARK 620 4 SF4 A 301 S4 106.9 99.1 97.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 301 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 381 O
REMARK 620 2 SF4 A 301 S1 115.3
REMARK 620 3 SF4 A 301 S2 127.2 98.0
REMARK 620 4 SF4 A 301 S3 116.3 97.9 96.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 301 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 55 SG
REMARK 620 2 SF4 A 301 S1 121.7
REMARK 620 3 SF4 A 301 S2 123.1 99.6
REMARK 620 4 SF4 A 301 S4 110.6 98.7 98.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 301 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 55 SG
REMARK 620 2 SF4 D 301 S1 122.4
REMARK 620 3 SF4 D 301 S2 122.8 101.5
REMARK 620 4 SF4 D 301 S4 108.3 99.9 96.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 55 SG
REMARK 620 2 SF4 D 301 S2 124.2
REMARK 620 3 SF4 D 301 S3 124.8 99.0
REMARK 620 4 SF4 D 301 S4 108.7 96.3 97.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 55 SG
REMARK 620 2 SF4 D 301 S1 121.9
REMARK 620 3 SF4 D 301 S3 122.9 99.5
REMARK 620 4 SF4 D 301 S4 111.2 98.3 98.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 301 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 368 O
REMARK 620 2 SF4 D 301 S1 109.9
REMARK 620 3 SF4 D 301 S2 140.0 98.2
REMARK 620 4 SF4 D 301 S3 107.1 96.4 97.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DIH RELATED DB: PDB
REMARK 900 RELATED ID: 5DJB RELATED DB: PDB
DBREF 5DII A 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
DBREF 5DII B 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
DBREF 5DII C 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
DBREF 5DII D 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
DBREF 5DII E 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
DBREF 5DII F 1 205 UNP D0LHE3 D0LHE3_HALO1 1 205
SEQADV 5DII CYS A 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQADV 5DII CYS B 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQADV 5DII CYS C 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQADV 5DII CYS D 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQADV 5DII CYS E 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQADV 5DII CYS F 55 UNP D0LHE3 SER 55 ENGINEERED MUTATION
SEQRES 1 A 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 A 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 A 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 A 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 A 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 A 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 A 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 A 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 A 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 A 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 A 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 A 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 A 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 A 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 A 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 A 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
SEQRES 1 B 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 B 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 B 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 B 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 B 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 B 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 B 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 B 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 B 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 B 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 B 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 B 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 B 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 B 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 B 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 B 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
SEQRES 1 C 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 C 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 C 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 C 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 C 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 C 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 C 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 C 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 C 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 C 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 C 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 C 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 C 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 C 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 C 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 C 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
SEQRES 1 D 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 D 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 D 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 D 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 D 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 D 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 D 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 D 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 D 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 D 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 D 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 D 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 D 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 D 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 D 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 D 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
SEQRES 1 E 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 E 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 E 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 E 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 E 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 E 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 E 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 E 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 E 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 E 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 E 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 E 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 E 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 E 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 E 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 E 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
SEQRES 1 F 205 MET ASP HIS ALA PRO GLU ARG PHE ASP ALA THR PRO PRO
SEQRES 2 F 205 ALA GLY GLU PRO ASP ARG PRO ALA LEU GLY VAL LEU GLU
SEQRES 3 F 205 LEU THR SER ILE ALA ARG GLY ILE THR VAL ALA ASP ALA
SEQRES 4 F 205 ALA LEU LYS ARG ALA PRO SER LEU LEU LEU MET SER ARG
SEQRES 5 F 205 PRO VAL CYS SER GLY LYS HIS LEU LEU MET MET ARG GLY
SEQRES 6 F 205 GLN VAL ALA GLU VAL GLU GLU SER MET ILE ALA ALA ARG
SEQRES 7 F 205 GLU ILE ALA GLY ALA GLY SER GLY ALA LEU LEU ASP GLU
SEQRES 8 F 205 LEU GLU LEU PRO TYR ALA HIS GLU GLN LEU TRP ARG PHE
SEQRES 9 F 205 LEU ASP ALA PRO VAL VAL ALA ASP ALA TRP GLU GLU ASP
SEQRES 10 F 205 THR GLU SER VAL ILE ILE VAL GLU THR ALA THR VAL CYS
SEQRES 11 F 205 ALA ALA ILE ASP SER ALA ASP ALA ALA LEU LYS THR ALA
SEQRES 12 F 205 PRO VAL VAL LEU ARG ASP MET ARG LEU ALA ILE GLY ILE
SEQRES 13 F 205 ALA GLY LYS ALA PHE PHE THR LEU THR GLY GLU LEU ALA
SEQRES 14 F 205 ASP VAL GLU ALA ALA ALA GLU VAL VAL ARG GLU ARG CYS
SEQRES 15 F 205 GLY ALA ARG LEU LEU GLU LEU ALA CYS ILE ALA ARG PRO
SEQRES 16 F 205 VAL ASP GLU LEU ARG GLY ARG LEU PHE PHE
HET SF4 A 301 8
HET SF4 D 301 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 7 SF4 2(FE4 S4)
FORMUL 9 HOH *407(H2 O)
HELIX 1 AA1 PRO A 5 ASP A 9 5 5
HELIX 2 AA2 SER A 29 ALA A 44 1 16
HELIX 3 AA3 GLN A 66 GLY A 82 1 17
HELIX 4 AA4 LEU A 101 LEU A 105 5 5
HELIX 5 AA5 THR A 128 ALA A 143 1 16
HELIX 6 AA6 GLU A 167 GLY A 183 1 17
HELIX 7 AA7 SER B 29 ALA B 44 1 16
HELIX 8 AA8 GLN B 66 GLY B 82 1 17
HELIX 9 AA9 LEU B 101 LEU B 105 5 5
HELIX 10 AB1 THR B 128 ALA B 143 1 16
HELIX 11 AB2 GLU B 167 GLY B 183 1 17
HELIX 12 AB3 ALA C 4 ASP C 9 5 6
HELIX 13 AB4 SER C 29 ALA C 44 1 16
HELIX 14 AB5 GLN C 66 GLY C 82 1 17
HELIX 15 AB6 HIS C 98 LEU C 105 5 8
HELIX 16 AB7 THR C 128 ALA C 143 1 16
HELIX 17 AB8 GLU C 167 GLY C 183 1 17
HELIX 18 AB9 ALA D 4 ASP D 9 5 6
HELIX 19 AC1 SER D 29 ALA D 44 1 16
HELIX 20 AC2 GLN D 66 GLY D 82 1 17
HELIX 21 AC3 LEU D 101 LEU D 105 5 5
HELIX 22 AC4 THR D 128 ALA D 143 1 16
HELIX 23 AC5 GLU D 167 GLY D 183 1 17
HELIX 24 AC6 SER E 29 ALA E 44 1 16
HELIX 25 AC7 GLN E 66 GLY E 82 1 17
HELIX 26 AC8 LEU E 101 LEU E 105 5 5
HELIX 27 AC9 THR E 128 ALA E 143 1 16
HELIX 28 AD1 GLU E 167 GLY E 183 1 17
HELIX 29 AD2 PRO F 5 ASP F 9 5 5
HELIX 30 AD3 SER F 29 ALA F 44 1 16
HELIX 31 AD4 GLN F 66 GLY F 82 1 17
HELIX 32 AD5 HIS F 98 LEU F 105 5 8
HELIX 33 AD6 THR F 128 ALA F 143 1 16
HELIX 34 AD7 GLU F 167 GLY F 183 1 17
SHEET 1 AA1 4 LEU A 47 VAL A 54 0
SHEET 2 AA1 4 LYS A 58 GLY A 65 -1 O ARG A 64 N LEU A 47
SHEET 3 AA1 4 ALA A 21 LEU A 27 -1 N LEU A 27 O HIS A 59
SHEET 4 AA1 4 LEU A 88 LEU A 94 -1 O LEU A 89 N GLU A 26
SHEET 1 AA2 4 VAL A 146 LEU A 152 0
SHEET 2 AA2 4 ALA A 160 GLY A 166 -1 O THR A 163 N ARG A 148
SHEET 3 AA2 4 SER A 120 THR A 126 -1 N SER A 120 O GLY A 166
SHEET 4 AA2 4 LEU A 186 ILE A 192 -1 O LEU A 187 N GLU A 125
SHEET 1 AA3 4 LEU B 47 VAL B 54 0
SHEET 2 AA3 4 LYS B 58 GLY B 65 -1 O ARG B 64 N LEU B 47
SHEET 3 AA3 4 ALA B 21 LEU B 27 -1 N LEU B 25 O LEU B 61
SHEET 4 AA3 4 LEU B 88 LEU B 94 -1 O LEU B 89 N GLU B 26
SHEET 1 AA4 4 VAL B 146 LEU B 152 0
SHEET 2 AA4 4 ALA B 160 GLY B 166 -1 O THR B 165 N VAL B 146
SHEET 3 AA4 4 SER B 120 THR B 126 -1 N VAL B 124 O PHE B 162
SHEET 4 AA4 4 LEU B 186 ILE B 192 -1 O LEU B 187 N GLU B 125
SHEET 1 AA5 4 LEU C 47 VAL C 54 0
SHEET 2 AA5 4 LYS C 58 GLY C 65 -1 O ARG C 64 N LEU C 47
SHEET 3 AA5 4 ALA C 21 LEU C 27 -1 N LEU C 27 O HIS C 59
SHEET 4 AA5 4 LEU C 88 LEU C 94 -1 O LEU C 89 N GLU C 26
SHEET 1 AA6 4 VAL C 146 LEU C 152 0
SHEET 2 AA6 4 ALA C 160 GLY C 166 -1 O THR C 165 N VAL C 146
SHEET 3 AA6 4 SER C 120 THR C 126 -1 N VAL C 124 O PHE C 162
SHEET 4 AA6 4 LEU C 186 ILE C 192 -1 O LEU C 187 N GLU C 125
SHEET 1 AA7 4 LEU D 47 VAL D 54 0
SHEET 2 AA7 4 LYS D 58 GLY D 65 -1 O ARG D 64 N LEU D 47
SHEET 3 AA7 4 ALA D 21 LEU D 27 -1 N LEU D 27 O HIS D 59
SHEET 4 AA7 4 LEU D 88 LEU D 94 -1 O LEU D 89 N GLU D 26
SHEET 1 AA8 4 VAL D 146 LEU D 152 0
SHEET 2 AA8 4 ALA D 160 GLY D 166 -1 O PHE D 161 N ARG D 151
SHEET 3 AA8 4 SER D 120 THR D 126 -1 N SER D 120 O GLY D 166
SHEET 4 AA8 4 LEU D 186 ILE D 192 -1 O LEU D 187 N GLU D 125
SHEET 1 AA9 4 LEU E 47 VAL E 54 0
SHEET 2 AA9 4 LYS E 58 GLY E 65 -1 O ARG E 64 N LEU E 47
SHEET 3 AA9 4 ALA E 21 LEU E 27 -1 N LEU E 25 O LEU E 61
SHEET 4 AA9 4 LEU E 88 LEU E 94 -1 O LEU E 89 N GLU E 26
SHEET 1 AB1 4 VAL E 146 LEU E 152 0
SHEET 2 AB1 4 ALA E 160 GLY E 166 -1 O THR E 165 N VAL E 146
SHEET 3 AB1 4 SER E 120 THR E 126 -1 N VAL E 124 O PHE E 162
SHEET 4 AB1 4 LEU E 186 ILE E 192 -1 O LEU E 187 N GLU E 125
SHEET 1 AB2 4 LEU F 47 VAL F 54 0
SHEET 2 AB2 4 LYS F 58 GLY F 65 -1 O ARG F 64 N LEU F 47
SHEET 3 AB2 4 ALA F 21 LEU F 27 -1 N LEU F 27 O HIS F 59
SHEET 4 AB2 4 LEU F 88 LEU F 94 -1 O LEU F 89 N GLU F 26
SHEET 1 AB3 4 VAL F 146 LEU F 152 0
SHEET 2 AB3 4 ALA F 160 GLY F 166 -1 O THR F 165 N VAL F 146
SHEET 3 AB3 4 SER F 120 THR F 126 -1 N VAL F 124 O PHE F 162
SHEET 4 AB3 4 LEU F 186 ILE F 192 -1 O ILE F 192 N VAL F 121
LINK SG CYS A 55 FE1 SF4 A 301 1555 1555 2.28
LINK FE2 SF4 A 301 SG CYS B 55 1555 1555 2.28
LINK FE4 SF4 A 301 O HOH B 381 1555 1555 2.08
LINK FE3 SF4 A 301 SG CYS C 55 1555 1555 2.29
LINK SG CYS D 55 FE3 SF4 D 301 1555 1555 2.27
LINK FE1 SF4 D 301 SG CYS E 55 1555 1555 2.27
LINK FE2 SF4 D 301 SG CYS F 55 1555 1555 2.28
LINK FE4 SF4 D 301 O HOH F 368 1555 1555 2.08
SITE 1 AC1 7 CYS A 55 ALA A 157 CYS B 55 ALA B 157
SITE 2 AC1 7 HOH B 381 CYS C 55 ALA C 157
SITE 1 AC2 7 CYS D 55 ALA D 157 CYS E 55 ALA E 157
SITE 2 AC2 7 CYS F 55 ALA F 157 HOH F 368
CRYST1 42.897 55.558 117.930 83.45 81.22 86.95 P 1 6
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 0.023312 -0.001242 -0.003487 0.00000
SCALE2 0.000000 0.018025 -0.001947 0.00000
SCALE3 0.000000 0.000000 0.008630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
