HEADER CELL CYCLE,HYDROLASE/CELL CYCLE 25-MAR-11 3R9I
TITLE 2.6A RESOLUTION STRUCTURE OF MIND COMPLEXED WITH MINE (12-31) PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEPTUM SITE-DETERMINING PROTEIN MIND;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CELL DIVISION INHIBITOR MIND;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CELL DIVISION TOPOLOGICAL SPECIFICITY FACTOR;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 FRAGMENT: UNP RESIDUES 12-31;
COMPND 11 SYNONYM: MINE;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B1175, JW1164, MIND;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 83333
KEYWDS ATPASE, BACTERIAL CELL DIVISION INHIBITOR, MINE, CELL CYCLE,
KEYWDS 2 HYDROLASE-CELL CYCLE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LOVELL,K.P.BATTAILE,K.-T.PARK,W.WU,T.HOLYOAK,J.LUTKENHAUS
REVDAT 2 13-SEP-23 3R9I 1 REMARK SEQADV
REVDAT 1 17-AUG-11 3R9I 0
JRNL AUTH K.T.PARK,W.WU,K.P.BATTAILE,S.LOVELL,T.HOLYOAK,J.LUTKENHAUS
JRNL TITL THE MIN OSCILLATOR USES MIND-DEPENDENT CONFORMATIONAL
JRNL TITL 2 CHANGES IN MINE TO SPATIALLY REGULATE CYTOKINESIS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 146 396 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 21816275
JRNL DOI 10.1016/J.CELL.2011.06.042
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_661
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 36875
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1852
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 43.4230 - 6.1084 0.98 2653 174 0.1848 0.2127
REMARK 3 2 6.1084 - 4.8505 0.99 2708 148 0.1913 0.2327
REMARK 3 3 4.8505 - 4.2379 0.99 2693 138 0.1492 0.1607
REMARK 3 4 4.2379 - 3.8507 0.99 2731 121 0.1640 0.2014
REMARK 3 5 3.8507 - 3.5749 0.99 2666 171 0.1938 0.2280
REMARK 3 6 3.5749 - 3.3642 0.99 2730 127 0.2178 0.2818
REMARK 3 7 3.3642 - 3.1957 0.99 2653 142 0.2253 0.2820
REMARK 3 8 3.1957 - 3.0567 0.98 2688 138 0.2168 0.2988
REMARK 3 9 3.0567 - 2.9390 0.98 2713 136 0.2222 0.2691
REMARK 3 10 2.9390 - 2.8376 0.98 2690 139 0.2196 0.3073
REMARK 3 11 2.8376 - 2.7489 0.98 2676 148 0.2424 0.2569
REMARK 3 12 2.7489 - 2.6703 0.98 2691 139 0.2607 0.3044
REMARK 3 13 2.6703 - 2.6001 0.98 2731 131 0.2677 0.3011
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.77
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 20.39
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.35290
REMARK 3 B22 (A**2) : 2.26760
REMARK 3 B33 (A**2) : -7.62060
REMARK 3 B12 (A**2) : -6.56110
REMARK 3 B13 (A**2) : -0.82530
REMARK 3 B23 (A**2) : -0.83670
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 : 0.011 8372
REMARK 3 ANGLE : 1.356 11333
REMARK 3 CHIRALITY : 0.067 1368
REMARK 3 PLANARITY : 0.004 1455
REMARK 3 DIHEDRAL : 16.959 3161
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 : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1913
REMARK 3 RMSD : 0.072
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1914
REMARK 3 RMSD : 0.068
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 2:258 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 1948
REMARK 3 RMSD : 0.049
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN E AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 110
REMARK 3 RMSD : 0.073
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN E AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 103
REMARK 3 RMSD : 0.071
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN E AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 13:26 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 110
REMARK 3 RMSD : 0.049
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : SCALA CCP4_3.3.16, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36883
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 73.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1490
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.47
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3Q9L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3350, 100 MM CITRATE, 200
REMARK 280 MM SODIUM CITRATE, PH 4.0, VAPOR DIFFUSION, TEMPERATURE 293K
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H
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 GLU A 259
REMARK 465 LYS A 260
REMARK 465 MET B 1
REMARK 465 ASP B 93
REMARK 465 LYS B 94
REMARK 465 ASP B 95
REMARK 465 GLU B 259
REMARK 465 LYS B 260
REMARK 465 MET C 1
REMARK 465 ASP C 93
REMARK 465 LYS C 94
REMARK 465 ASP C 95
REMARK 465 GLU C 259
REMARK 465 LYS C 260
REMARK 465 MET D 1
REMARK 465 GLU D 259
REMARK 465 LYS D 260
REMARK 465 LYS E 12
REMARK 465 ALA E 27
REMARK 465 GLU E 28
REMARK 465 ARG E 29
REMARK 465 ARG E 30
REMARK 465 ARG E 31
REMARK 465 LYS F 12
REMARK 465 ALA F 27
REMARK 465 GLU F 28
REMARK 465 ARG F 29
REMARK 465 ARG F 30
REMARK 465 ARG F 31
REMARK 465 LYS G 12
REMARK 465 VAL G 26
REMARK 465 ALA G 27
REMARK 465 GLU G 28
REMARK 465 ARG G 29
REMARK 465 ARG G 30
REMARK 465 ARG G 31
REMARK 465 LYS H 12
REMARK 465 ALA H 27
REMARK 465 GLU H 28
REMARK 465 ARG H 29
REMARK 465 ARG H 30
REMARK 465 ARG H 31
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 79 CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 ARG B 92 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 175 CG CD CE NZ
REMARK 470 GLU B 201 CG CD OE1 OE2
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 LYS C 78 CD CE NZ
REMARK 470 ARG C 79 CD NE CZ NH1 NH2
REMARK 470 ARG C 92 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 126 CG CD OE1 OE2
REMARK 470 GLU C 201 CG CD OE1 OE2
REMARK 470 GLU C 250 CG CD OE1 OE2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 GLU D 126 CG CD OE1 OE2
REMARK 470 GLU D 201 CG CD OE1 OE2
REMARK 470 LYS D 206 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND2 ASN B 232 O GLN C 29 1655 2.06
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 SER A 9 -35.07 -177.42
REMARK 500 ASN A 82 7.50 82.00
REMARK 500 ALA A 96 -52.65 -25.48
REMARK 500 GLU A 126 -117.57 -76.34
REMARK 500 SER B 9 -31.32 -173.42
REMARK 500 ASN B 82 3.31 83.34
REMARK 500 GLU B 126 -121.06 -81.25
REMARK 500 SER C 9 -32.74 -176.23
REMARK 500 ASN C 82 3.17 80.46
REMARK 500 ASP C 113 30.04 73.08
REMARK 500 GLU C 126 -121.30 -82.47
REMARK 500 SER D 9 -34.21 -176.01
REMARK 500 ALA D 96 -54.51 -23.84
REMARK 500 GLU D 126 -117.42 -77.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 261
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q9L RELATED DB: PDB
REMARK 900 MIND-ATP COMPLEX
REMARK 900 RELATED ID: 3R9J RELATED DB: PDB
DBREF 3R9I A 1 260 UNP P0AEZ3 MIND_ECOLI 1 260
DBREF 3R9I B 1 260 UNP P0AEZ3 MIND_ECOLI 1 260
DBREF 3R9I C 1 260 UNP P0AEZ3 MIND_ECOLI 1 260
DBREF 3R9I D 1 260 UNP P0AEZ3 MIND_ECOLI 1 260
DBREF 3R9I E 12 31 UNP P0A734 MINE_ECOLI 12 31
DBREF 3R9I F 12 31 UNP P0A734 MINE_ECOLI 12 31
DBREF 3R9I G 12 31 UNP P0A734 MINE_ECOLI 12 31
DBREF 3R9I H 12 31 UNP P0A734 MINE_ECOLI 12 31
SEQADV 3R9I ALA A 40 UNP P0AEZ3 ASP 40 ENGINEERED MUTATION
SEQADV 3R9I ALA B 40 UNP P0AEZ3 ASP 40 ENGINEERED MUTATION
SEQADV 3R9I ALA C 40 UNP P0AEZ3 ASP 40 ENGINEERED MUTATION
SEQADV 3R9I ALA D 40 UNP P0AEZ3 ASP 40 ENGINEERED MUTATION
SEQRES 1 A 260 MET ALA ARG ILE ILE VAL VAL THR SER GLY LYS GLY GLY
SEQRES 2 A 260 VAL GLY LYS THR THR SER SER ALA ALA ILE ALA THR GLY
SEQRES 3 A 260 LEU ALA GLN LYS GLY LYS LYS THR VAL VAL ILE ASP PHE
SEQRES 4 A 260 ALA ILE GLY LEU ARG ASN LEU ASP LEU ILE MET GLY CYS
SEQRES 5 A 260 GLU ARG ARG VAL VAL TYR ASP PHE VAL ASN VAL ILE GLN
SEQRES 6 A 260 GLY ASP ALA THR LEU ASN GLN ALA LEU ILE LYS ASP LYS
SEQRES 7 A 260 ARG THR GLU ASN LEU TYR ILE LEU PRO ALA SER GLN THR
SEQRES 8 A 260 ARG ASP LYS ASP ALA LEU THR ARG GLU GLY VAL ALA LYS
SEQRES 9 A 260 VAL LEU ASP ASP LEU LYS ALA MET ASP PHE GLU PHE ILE
SEQRES 10 A 260 VAL CYS ASP SER PRO ALA GLY ILE GLU THR GLY ALA LEU
SEQRES 11 A 260 MET ALA LEU TYR PHE ALA ASP GLU ALA ILE ILE THR THR
SEQRES 12 A 260 ASN PRO GLU VAL SER SER VAL ARG ASP SER ASP ARG ILE
SEQRES 13 A 260 LEU GLY ILE LEU ALA SER LYS SER ARG ARG ALA GLU ASN
SEQRES 14 A 260 GLY GLU GLU PRO ILE LYS GLU HIS LEU LEU LEU THR ARG
SEQRES 15 A 260 TYR ASN PRO GLY ARG VAL SER ARG GLY ASP MET LEU SER
SEQRES 16 A 260 MET GLU ASP VAL LEU GLU ILE LEU ARG ILE LYS LEU VAL
SEQRES 17 A 260 GLY VAL ILE PRO GLU ASP GLN SER VAL LEU ARG ALA SER
SEQRES 18 A 260 ASN GLN GLY GLU PRO VAL ILE LEU ASP ILE ASN ALA ASP
SEQRES 19 A 260 ALA GLY LYS ALA TYR ALA ASP THR VAL GLU ARG LEU LEU
SEQRES 20 A 260 GLY GLU GLU ARG PRO PHE ARG PHE ILE GLU GLU GLU LYS
SEQRES 1 B 260 MET ALA ARG ILE ILE VAL VAL THR SER GLY LYS GLY GLY
SEQRES 2 B 260 VAL GLY LYS THR THR SER SER ALA ALA ILE ALA THR GLY
SEQRES 3 B 260 LEU ALA GLN LYS GLY LYS LYS THR VAL VAL ILE ASP PHE
SEQRES 4 B 260 ALA ILE GLY LEU ARG ASN LEU ASP LEU ILE MET GLY CYS
SEQRES 5 B 260 GLU ARG ARG VAL VAL TYR ASP PHE VAL ASN VAL ILE GLN
SEQRES 6 B 260 GLY ASP ALA THR LEU ASN GLN ALA LEU ILE LYS ASP LYS
SEQRES 7 B 260 ARG THR GLU ASN LEU TYR ILE LEU PRO ALA SER GLN THR
SEQRES 8 B 260 ARG ASP LYS ASP ALA LEU THR ARG GLU GLY VAL ALA LYS
SEQRES 9 B 260 VAL LEU ASP ASP LEU LYS ALA MET ASP PHE GLU PHE ILE
SEQRES 10 B 260 VAL CYS ASP SER PRO ALA GLY ILE GLU THR GLY ALA LEU
SEQRES 11 B 260 MET ALA LEU TYR PHE ALA ASP GLU ALA ILE ILE THR THR
SEQRES 12 B 260 ASN PRO GLU VAL SER SER VAL ARG ASP SER ASP ARG ILE
SEQRES 13 B 260 LEU GLY ILE LEU ALA SER LYS SER ARG ARG ALA GLU ASN
SEQRES 14 B 260 GLY GLU GLU PRO ILE LYS GLU HIS LEU LEU LEU THR ARG
SEQRES 15 B 260 TYR ASN PRO GLY ARG VAL SER ARG GLY ASP MET LEU SER
SEQRES 16 B 260 MET GLU ASP VAL LEU GLU ILE LEU ARG ILE LYS LEU VAL
SEQRES 17 B 260 GLY VAL ILE PRO GLU ASP GLN SER VAL LEU ARG ALA SER
SEQRES 18 B 260 ASN GLN GLY GLU PRO VAL ILE LEU ASP ILE ASN ALA ASP
SEQRES 19 B 260 ALA GLY LYS ALA TYR ALA ASP THR VAL GLU ARG LEU LEU
SEQRES 20 B 260 GLY GLU GLU ARG PRO PHE ARG PHE ILE GLU GLU GLU LYS
SEQRES 1 C 260 MET ALA ARG ILE ILE VAL VAL THR SER GLY LYS GLY GLY
SEQRES 2 C 260 VAL GLY LYS THR THR SER SER ALA ALA ILE ALA THR GLY
SEQRES 3 C 260 LEU ALA GLN LYS GLY LYS LYS THR VAL VAL ILE ASP PHE
SEQRES 4 C 260 ALA ILE GLY LEU ARG ASN LEU ASP LEU ILE MET GLY CYS
SEQRES 5 C 260 GLU ARG ARG VAL VAL TYR ASP PHE VAL ASN VAL ILE GLN
SEQRES 6 C 260 GLY ASP ALA THR LEU ASN GLN ALA LEU ILE LYS ASP LYS
SEQRES 7 C 260 ARG THR GLU ASN LEU TYR ILE LEU PRO ALA SER GLN THR
SEQRES 8 C 260 ARG ASP LYS ASP ALA LEU THR ARG GLU GLY VAL ALA LYS
SEQRES 9 C 260 VAL LEU ASP ASP LEU LYS ALA MET ASP PHE GLU PHE ILE
SEQRES 10 C 260 VAL CYS ASP SER PRO ALA GLY ILE GLU THR GLY ALA LEU
SEQRES 11 C 260 MET ALA LEU TYR PHE ALA ASP GLU ALA ILE ILE THR THR
SEQRES 12 C 260 ASN PRO GLU VAL SER SER VAL ARG ASP SER ASP ARG ILE
SEQRES 13 C 260 LEU GLY ILE LEU ALA SER LYS SER ARG ARG ALA GLU ASN
SEQRES 14 C 260 GLY GLU GLU PRO ILE LYS GLU HIS LEU LEU LEU THR ARG
SEQRES 15 C 260 TYR ASN PRO GLY ARG VAL SER ARG GLY ASP MET LEU SER
SEQRES 16 C 260 MET GLU ASP VAL LEU GLU ILE LEU ARG ILE LYS LEU VAL
SEQRES 17 C 260 GLY VAL ILE PRO GLU ASP GLN SER VAL LEU ARG ALA SER
SEQRES 18 C 260 ASN GLN GLY GLU PRO VAL ILE LEU ASP ILE ASN ALA ASP
SEQRES 19 C 260 ALA GLY LYS ALA TYR ALA ASP THR VAL GLU ARG LEU LEU
SEQRES 20 C 260 GLY GLU GLU ARG PRO PHE ARG PHE ILE GLU GLU GLU LYS
SEQRES 1 D 260 MET ALA ARG ILE ILE VAL VAL THR SER GLY LYS GLY GLY
SEQRES 2 D 260 VAL GLY LYS THR THR SER SER ALA ALA ILE ALA THR GLY
SEQRES 3 D 260 LEU ALA GLN LYS GLY LYS LYS THR VAL VAL ILE ASP PHE
SEQRES 4 D 260 ALA ILE GLY LEU ARG ASN LEU ASP LEU ILE MET GLY CYS
SEQRES 5 D 260 GLU ARG ARG VAL VAL TYR ASP PHE VAL ASN VAL ILE GLN
SEQRES 6 D 260 GLY ASP ALA THR LEU ASN GLN ALA LEU ILE LYS ASP LYS
SEQRES 7 D 260 ARG THR GLU ASN LEU TYR ILE LEU PRO ALA SER GLN THR
SEQRES 8 D 260 ARG ASP LYS ASP ALA LEU THR ARG GLU GLY VAL ALA LYS
SEQRES 9 D 260 VAL LEU ASP ASP LEU LYS ALA MET ASP PHE GLU PHE ILE
SEQRES 10 D 260 VAL CYS ASP SER PRO ALA GLY ILE GLU THR GLY ALA LEU
SEQRES 11 D 260 MET ALA LEU TYR PHE ALA ASP GLU ALA ILE ILE THR THR
SEQRES 12 D 260 ASN PRO GLU VAL SER SER VAL ARG ASP SER ASP ARG ILE
SEQRES 13 D 260 LEU GLY ILE LEU ALA SER LYS SER ARG ARG ALA GLU ASN
SEQRES 14 D 260 GLY GLU GLU PRO ILE LYS GLU HIS LEU LEU LEU THR ARG
SEQRES 15 D 260 TYR ASN PRO GLY ARG VAL SER ARG GLY ASP MET LEU SER
SEQRES 16 D 260 MET GLU ASP VAL LEU GLU ILE LEU ARG ILE LYS LEU VAL
SEQRES 17 D 260 GLY VAL ILE PRO GLU ASP GLN SER VAL LEU ARG ALA SER
SEQRES 18 D 260 ASN GLN GLY GLU PRO VAL ILE LEU ASP ILE ASN ALA ASP
SEQRES 19 D 260 ALA GLY LYS ALA TYR ALA ASP THR VAL GLU ARG LEU LEU
SEQRES 20 D 260 GLY GLU GLU ARG PRO PHE ARG PHE ILE GLU GLU GLU LYS
SEQRES 1 E 20 LYS ASN THR ALA ASN ILE ALA LYS GLU ARG LEU GLN ILE
SEQRES 2 E 20 ILE VAL ALA GLU ARG ARG ARG
SEQRES 1 F 20 LYS ASN THR ALA ASN ILE ALA LYS GLU ARG LEU GLN ILE
SEQRES 2 F 20 ILE VAL ALA GLU ARG ARG ARG
SEQRES 1 G 20 LYS ASN THR ALA ASN ILE ALA LYS GLU ARG LEU GLN ILE
SEQRES 2 G 20 ILE VAL ALA GLU ARG ARG ARG
SEQRES 1 H 20 LYS ASN THR ALA ASN ILE ALA LYS GLU ARG LEU GLN ILE
SEQRES 2 H 20 ILE VAL ALA GLU ARG ARG ARG
HET ADP A 261 27
HET ADP B 261 27
HET ADP C 261 27
HET ADP D 261 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 9 ADP 4(C10 H15 N5 O10 P2)
FORMUL 13 HOH *177(H2 O)
HELIX 1 1 GLY A 15 LYS A 30 1 16
HELIX 2 2 ASN A 45 MET A 50 1 6
HELIX 3 3 ASP A 59 GLN A 65 1 7
HELIX 4 4 THR A 69 LEU A 74 1 6
HELIX 5 5 THR A 98 MET A 112 1 15
HELIX 6 6 GLU A 126 TYR A 134 1 9
HELIX 7 7 GLU A 146 ALA A 161 1 16
HELIX 8 8 ARG A 166 GLY A 170 5 5
HELIX 9 9 ASN A 184 ARG A 190 1 7
HELIX 10 10 SER A 195 LEU A 203 1 9
HELIX 11 11 GLN A 215 GLY A 224 1 10
HELIX 12 12 PRO A 226 ASP A 230 5 5
HELIX 13 13 ALA A 233 LEU A 247 1 15
HELIX 14 14 GLY B 15 LYS B 30 1 16
HELIX 15 15 ASN B 45 MET B 50 1 6
HELIX 16 16 ASP B 59 GLN B 65 1 7
HELIX 17 17 THR B 69 LEU B 74 1 6
HELIX 18 18 THR B 98 MET B 112 1 15
HELIX 19 19 GLU B 126 PHE B 135 1 10
HELIX 20 20 GLU B 146 LYS B 163 1 18
HELIX 21 21 ARG B 166 GLY B 170 5 5
HELIX 22 22 ASN B 184 ARG B 190 1 7
HELIX 23 23 SER B 195 LEU B 203 1 9
HELIX 24 24 GLN B 215 GLY B 224 1 10
HELIX 25 25 PRO B 226 ASP B 230 5 5
HELIX 26 26 ALA B 233 LEU B 247 1 15
HELIX 27 27 GLY C 15 LYS C 30 1 16
HELIX 28 28 ASN C 45 MET C 50 1 6
HELIX 29 29 ASP C 59 GLN C 65 1 7
HELIX 30 30 THR C 69 LEU C 74 1 6
HELIX 31 31 THR C 98 MET C 112 1 15
HELIX 32 32 GLU C 126 PHE C 135 1 10
HELIX 33 33 GLU C 146 LYS C 163 1 18
HELIX 34 34 ARG C 166 GLY C 170 5 5
HELIX 35 35 ASN C 184 ARG C 190 1 7
HELIX 36 36 SER C 195 LEU C 203 1 9
HELIX 37 37 GLN C 215 GLY C 224 1 10
HELIX 38 38 PRO C 226 ASP C 230 5 5
HELIX 39 39 ALA C 233 LEU C 247 1 15
HELIX 40 40 GLY D 15 LYS D 30 1 16
HELIX 41 41 ASN D 45 GLY D 51 1 7
HELIX 42 42 ASP D 59 GLN D 65 1 7
HELIX 43 43 THR D 69 LEU D 74 1 6
HELIX 44 44 THR D 98 MET D 112 1 15
HELIX 45 45 GLU D 126 TYR D 134 1 9
HELIX 46 46 GLU D 146 ALA D 161 1 16
HELIX 47 47 ARG D 166 GLY D 170 5 5
HELIX 48 48 ASN D 184 ARG D 190 1 7
HELIX 49 49 SER D 195 LEU D 203 1 9
HELIX 50 50 GLN D 215 GLY D 224 1 10
HELIX 51 51 PRO D 226 ASP D 230 5 5
HELIX 52 52 ALA D 233 LEU D 247 1 15
HELIX 53 53 ASN E 13 VAL E 26 1 14
HELIX 54 54 ASN F 13 VAL F 26 1 14
HELIX 55 55 ASN G 13 ILE G 25 1 13
HELIX 56 56 ASN H 13 VAL H 26 1 14
SHEET 1 A 8 ILE A 75 LYS A 76 0
SHEET 2 A 8 LEU A 83 LEU A 86 -1 O ILE A 85 N ILE A 75
SHEET 3 A 8 THR A 34 ASP A 38 1 N ASP A 38 O LEU A 86
SHEET 4 A 8 PHE A 116 ASP A 120 1 O VAL A 118 N VAL A 35
SHEET 5 A 8 ARG A 3 THR A 8 1 N VAL A 7 O CYS A 119
SHEET 6 A 8 GLU A 138 THR A 143 1 O ILE A 140 N VAL A 6
SHEET 7 A 8 LYS A 175 TYR A 183 1 O THR A 181 N THR A 143
SHEET 8 A 8 LYS A 206 PRO A 212 1 O LYS A 206 N LEU A 178
SHEET 1 B 8 ILE B 75 LYS B 76 0
SHEET 2 B 8 LEU B 83 LEU B 86 -1 O ILE B 85 N ILE B 75
SHEET 3 B 8 THR B 34 ASP B 38 1 N ASP B 38 O LEU B 86
SHEET 4 B 8 PHE B 116 ASP B 120 1 O VAL B 118 N ILE B 37
SHEET 5 B 8 ARG B 3 THR B 8 1 N VAL B 7 O CYS B 119
SHEET 6 B 8 GLU B 138 THR B 143 1 O ILE B 140 N VAL B 6
SHEET 7 B 8 LYS B 175 TYR B 183 1 O THR B 181 N THR B 143
SHEET 8 B 8 LYS B 206 PRO B 212 1 O LYS B 206 N LEU B 178
SHEET 1 C 8 ILE C 75 LYS C 76 0
SHEET 2 C 8 LEU C 83 LEU C 86 -1 O ILE C 85 N ILE C 75
SHEET 3 C 8 THR C 34 ASP C 38 1 N ASP C 38 O LEU C 86
SHEET 4 C 8 PHE C 116 ASP C 120 1 O VAL C 118 N VAL C 35
SHEET 5 C 8 ARG C 3 THR C 8 1 N VAL C 7 O CYS C 119
SHEET 6 C 8 GLU C 138 THR C 143 1 O ILE C 140 N VAL C 6
SHEET 7 C 8 LYS C 175 TYR C 183 1 O THR C 181 N THR C 143
SHEET 8 C 8 LYS C 206 PRO C 212 1 O LYS C 206 N LEU C 178
SHEET 1 D 8 ILE D 75 LYS D 76 0
SHEET 2 D 8 LEU D 83 LEU D 86 -1 O ILE D 85 N ILE D 75
SHEET 3 D 8 THR D 34 ASP D 38 1 N ASP D 38 O LEU D 86
SHEET 4 D 8 PHE D 116 ASP D 120 1 O VAL D 118 N VAL D 35
SHEET 5 D 8 ARG D 3 THR D 8 1 N VAL D 7 O CYS D 119
SHEET 6 D 8 GLU D 138 THR D 143 1 O ILE D 140 N VAL D 6
SHEET 7 D 8 LYS D 175 TYR D 183 1 O THR D 181 N THR D 143
SHEET 8 D 8 LYS D 206 PRO D 212 1 O LYS D 206 N LEU D 178
SITE 1 AC1 17 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 17 THR A 17 THR A 18 ARG A 182 ILE A 211
SITE 3 AC1 17 PRO A 212 GLU A 213 ASP A 214 VAL A 217
SITE 4 AC1 17 HOH A 276 HOH A 301 HOH A 309 HOH A 311
SITE 5 AC1 17 LYS B 11
SITE 1 AC2 16 LYS A 11 GLU A 146 GLY B 13 VAL B 14
SITE 2 AC2 16 GLY B 15 LYS B 16 THR B 17 THR B 18
SITE 3 AC2 16 ARG B 182 PRO B 212 GLU B 213 ASP B 214
SITE 4 AC2 16 VAL B 217 HOH B 283 HOH B 305 HOH B 306
SITE 1 AC3 17 GLY C 13 VAL C 14 GLY C 15 LYS C 16
SITE 2 AC3 17 THR C 17 THR C 18 ARG C 182 ILE C 211
SITE 3 AC3 17 PRO C 212 GLU C 213 ASP C 214 VAL C 217
SITE 4 AC3 17 HOH C 268 HOH C 280 LYS D 11 GLU D 146
SITE 5 AC3 17 HOH D 272
SITE 1 AC4 17 LYS C 11 GLU C 146 GLY D 13 VAL D 14
SITE 2 AC4 17 GLY D 15 LYS D 16 THR D 17 THR D 18
SITE 3 AC4 17 ARG D 182 ILE D 211 PRO D 212 GLU D 213
SITE 4 AC4 17 ASP D 214 VAL D 217 HOH D 264 HOH D 273
SITE 5 AC4 17 HOH D 284
CRYST1 64.293 71.796 76.644 102.64 95.87 111.72 P 1 4
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 0.015554 0.006197 0.003458 0.00000
SCALE2 0.000000 0.014993 0.004336 0.00000
SCALE3 0.000000 0.000000 0.013654 0.00000
MTRIX1 1 -0.816296 -0.576484 0.036422 -0.05569 1
MTRIX2 1 -0.577459 0.812876 -0.075984 0.10324 1
MTRIX3 1 0.014197 -0.083057 -0.996444 0.02754 1
MTRIX1 2 0.457269 0.060284 -0.887283 -16.22100 1
MTRIX2 2 0.697792 -0.642862 0.315935 63.75620 1
MTRIX3 2 -0.551354 -0.763606 -0.336026 -2.59737 1
MTRIX1 3 -0.783577 0.318854 0.533234 -23.93960 1
MTRIX2 3 0.339721 -0.498707 0.797422 61.16190 1
MTRIX3 3 0.520189 0.805992 0.282454 -2.25755 1
MTRIX1 4 -0.829505 -0.558349 0.012932 -0.43301 1
MTRIX2 4 -0.557704 0.826868 -0.072486 -0.15049 1
MTRIX3 4 0.029779 -0.067340 -0.997286 -0.13080 1
MTRIX1 5 0.464161 0.029462 -0.885260 -15.04340 1
MTRIX2 5 0.684016 -0.646897 0.337115 63.79740 1
MTRIX3 5 -0.562740 -0.762008 -0.320417 -2.65225 1
MTRIX1 6 -0.789982 0.310548 0.528667 -23.97150 1
MTRIX2 6 0.334230 -0.504751 0.795937 61.36340 1
MTRIX3 6 0.514022 0.805473 0.294950 -2.08804 1
(ATOM LINES ARE NOT SHOWN.)
END
