HEADER CELL CYCLE 10-SEP-14 4V03
TITLE MIND CELL DIVISION PROTEIN, AQUIFEX AEOLICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SITE-DETERMINING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL AMPHIPATHIC HELIX REMOVED, UNP RESDIUES 1-250;
COMPND 5 SYNONYM: MIND;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL CYCLE, BACTERIAL CELL DIVISION, FTSZ, MIN SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.TRAMBAIOLO,J.LOWE
REVDAT 1 14-JAN-15 4V03 0
JRNL AUTH D.GHOSAL,D.TRAMBAIOLO,L.A.AMOS,J.LOWE
JRNL TITL MINCD CELL DIVISION PROTEINS FORM ALTERNATING COPOLYMERIC
JRNL TITL 2 CYTOMOTIVE FILAMENTS.
JRNL REF NAT.COMMUN. V. 5 5341 2014
JRNL REFN ISSN 2041-1723
JRNL PMID 25500731
JRNL DOI 10.1038/NCOMMS6341
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.900
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.937
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.61
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.36
REMARK 3 NUMBER OF REFLECTIONS : 32486
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.2191
REMARK 3 R VALUE (WORKING SET) : 0.2157
REMARK 3 FREE R VALUE : 0.2793
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3214
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 23.9384 - 5.3838 0.90 2635 120 0.2319 0.2925
REMARK 3 2 5.3838 - 4.2812 0.93 2607 160 0.1898 0.2348
REMARK 3 3 4.2812 - 3.7424 0.93 2713 155 0.1967 0.2646
REMARK 3 4 3.7424 - 3.4013 0.93 2648 147 0.2003 0.2317
REMARK 3 5 3.4013 - 3.1581 0.92 2658 154 0.2120 0.2737
REMARK 3 6 3.1581 - 2.9722 0.92 2668 128 0.2159 0.3057
REMARK 3 7 2.9722 - 2.8236 0.93 2657 160 0.2034 0.3180
REMARK 3 8 2.8236 - 2.7009 0.92 2627 130 0.2123 0.2988
REMARK 3 9 2.7009 - 2.5970 0.92 2596 150 0.2095 0.2951
REMARK 3 10 2.5970 - 2.5075 0.92 2760 120 0.2075 0.2629
REMARK 3 11 2.5075 - 2.4292 0.91 2575 148 0.2089 0.3135
REMARK 3 12 2.4292 - 2.3598 0.92 2650 124 0.2008 0.2763
REMARK 3 13 2.3598 - 2.2977 0.92 2660 152 0.2035 0.2466
REMARK 3 14 2.2977 - 2.2417 0.91 2564 130 0.2263 0.3104
REMARK 3 15 2.2417 - 2.1908 0.91 2679 156 0.2293 0.2959
REMARK 3 16 2.1908 - 2.1442 0.91 2584 124 0.2219 0.2988
REMARK 3 17 2.1442 - 2.1013 0.91 2680 147 0.2262 0.2923
REMARK 3 18 2.1013 - 2.0617 0.91 2589 135 0.2373 0.2512
REMARK 3 19 2.0617 - 2.0249 0.91 2586 121 0.2389 0.3389
REMARK 3 20 2.0249 - 1.9906 0.90 2601 143 0.2439 0.3209
REMARK 3 21 1.9906 - 1.9585 0.90 2713 142 0.2650 0.3422
REMARK 3 22 1.9585 - 1.9284 0.90 2529 138 0.2811 0.3277
REMARK 3 23 1.9284 - 1.9000 0.90 2575 130 0.3167 0.3609
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) : 0.27
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.49
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 : 0.014 3752
REMARK 3 ANGLE : 1.591 5081
REMARK 3 CHIRALITY : 0.086 614
REMARK 3 PLANARITY : 0.007 629
REMARK 3 DIHEDRAL : 17.212 1441
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 4V03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31504
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 2.4
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.4
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.1 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 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 ILE A 41
REMARK 465 GLY A 42
REMARK 465 LEU A 43
REMARK 465 ALA A 88
REMARK 465 ASN A 89
REMARK 465 GLN A 90
REMARK 465 ARG A 91
REMARK 465 ALA A 92
REMARK 465 ASN A 93
REMARK 465 LYS A 94
REMARK 465 ASP A 95
REMARK 465 TYR A 249
REMARK 465 GLY A 250
REMARK 465 SER A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 HIS A 256
REMARK 465 HIS A 257
REMARK 465 MET B 1
REMARK 465 ILE B 41
REMARK 465 GLY B 42
REMARK 465 LEU B 43
REMARK 465 ASN B 89
REMARK 465 GLN B 90
REMARK 465 ARG B 91
REMARK 465 ALA B 92
REMARK 465 ASN B 93
REMARK 465 LYS B 94
REMARK 465 ASP B 95
REMARK 465 ARG B 248
REMARK 465 TYR B 249
REMARK 465 GLY B 250
REMARK 465 SER B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 HIS B 257
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 GLN B 131 CG CD OE1 NE2
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 ARG B 183 CG CD NE CZ NH1 NH2
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 NZ LYS A 11 O HOH A 2003 2.19
REMARK 500 NH1 ARG A 67 O HOH A 2023 2.15
REMARK 500 OE2 GLU A 207 O HOH A 2054 2.15
REMARK 500 NZ LYS B 72 O HOH B 2038 2.14
REMARK 500 O PRO B 87 O HOH B 2028 1.88
REMARK 500 OE1 GLU B 108 O HOH B 2046 2.06
REMARK 500 OE1 GLU B 190 O HOH B 2059 2.02
REMARK 500 OE2 GLU B 207 O HOH B 2063 2.00
REMARK 500 OE2 GLU B 218 O HOH B 2065 2.04
REMARK 500 O HOH A 2032 O HOH A 2055 2.17
REMARK 500 O HOH A 2043 O HOH A 2044 2.11
REMARK 500 O HOH A 2045 O HOH A 2046 2.19
REMARK 500 O HOH A 2051 O HOH A 2060 2.01
REMARK 500 O HOH A 2054 O HOH A 2055 1.95
REMARK 500 O HOH B 2001 O HOH B 2002 2.03
REMARK 500 O HOH B 2015 O HOH B 2042 1.93
REMARK 500
REMARK 500 REMARK: NULL
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 OE2 GLU A 190 O HOH A 2023 2565 2.01
REMARK 500 O HOH A 2023 O HOH A 2048 2545 2.15
REMARK 500 O HOH B 2032 O HOH B 2059 2565 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY B 66 N - CA - C ANGL. DEV. = 19.5 DEGREES
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 THR A 8 -169.70 -125.85
REMARK 500 SER A 9 -174.99 -174.83
REMARK 500 ARG A 175 39.24 76.09
REMARK 500 LEU A 246 90.89 -69.60
REMARK 500 SER B 9 -179.66 -172.24
REMARK 500 VAL B 57 -51.51 -126.02
REMARK 500 ARG B 175 34.84 72.37
REMARK 500 LEU B 246 97.14 -63.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 79 GLY A 80 -46.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 79 23.3 L L OUTSIDE RANGE
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 B2071 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH B2072 DISTANCE = 5.45 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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 HOH A2006 O 83.6
REMARK 620 3 HOH A2007 O 89.7 92.0
REMARK 620 4 HOH A2012 O 170.8 89.1 96.1
REMARK 620 5 ADP A 303 O1B 93.9 175.9 84.8 93.7
REMARK 620 6 HOH A2005 O 80.7 86.5 170.4 93.3 96.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2018 O
REMARK 620 2 THR B 17 OG1 174.1
REMARK 620 3 ADP B 303 O1B 89.8 95.7
REMARK 620 4 HOH B2005 O 95.0 82.5 93.2
REMARK 620 5 HOH B2006 O 88.9 85.7 178.2 88.2
REMARK 620 6 HOH B2008 O 90.3 91.9 91.1 173.2 87.6
REMARK 620 N 1 2 3 4 5
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 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4V02 RELATED DB: PDB
REMARK 900 MINC:MIND CELL DIVISION PROTEIN COMPLEX, AQUIFEX
REMARK 900 AEOLICUS
DBREF 4V03 A 1 250 UNP O67033 O67033_AQUAE 1 250
DBREF 4V03 B 1 250 UNP O67033 O67033_AQUAE 1 250
SEQADV 4V03 SER A 251 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 252 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 253 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 254 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 255 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 256 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS A 257 UNP O67033 EXPRESSION TAG
SEQADV 4V03 SER B 251 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 252 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 253 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 254 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 255 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 256 UNP O67033 EXPRESSION TAG
SEQADV 4V03 HIS B 257 UNP O67033 EXPRESSION TAG
SEQRES 1 A 257 MET ALA GLU VAL ILE VAL ILE THR SER GLY LYS GLY GLY
SEQRES 2 A 257 VAL GLY LYS THR THR LEU THR ALA ASN ILE GLY THR ALA
SEQRES 3 A 257 LEU ALA LYS LEU GLY LYS LYS VAL LEU LEU ILE ASP ALA
SEQRES 4 A 257 ASP ILE GLY LEU ARG ASN LEU ASP MET ILE LEU GLY LEU
SEQRES 5 A 257 GLU ASN ARG ILE VAL TYR ASP ILE LEU ASP VAL LEU GLU
SEQRES 6 A 257 GLY ARG VAL PRO TYR GLU LYS ALA LEU VAL LYS ASP LYS
SEQRES 7 A 257 ARG GLY LEU SER LEU TRP LEU LEU PRO ALA ASN GLN ARG
SEQRES 8 A 257 ALA ASN LYS ASP VAL ILE ASP ILE GLU LYS TRP ASN LYS
SEQRES 9 A 257 THR VAL GLU GLU ILE LYS ASN SER GLY ASN TYR ASP TYR
SEQRES 10 A 257 ILE LEU VAL ASP SER PRO ALA GLY ILE GLU LYS GLY PHE
SEQRES 11 A 257 GLN ILE ALA VAL SER PRO ALA ASP LYS ALA LEU ILE VAL
SEQRES 12 A 257 VAL ASN PRO GLU VAL SER SER ILE ARG ASP ALA ASP ARG
SEQRES 13 A 257 VAL ILE GLY LEU LEU GLU SER MET ASP LYS ARG ASN TYR
SEQRES 14 A 257 LYS VAL ILE VAL ASN ARG ILE LYS TRP GLU MET VAL LYS
SEQRES 15 A 257 ARG GLY ALA MET LEU SER VAL GLU ASP ILE VAL ASP ILE
SEQRES 16 A 257 LEU LYS ALA GLU ILE ILE GLY ILE ILE PRO GLU GLU PRO
SEQRES 17 A 257 LYS LEU VAL ASP PHE THR ASN ARG GLY GLU PRO ILE VAL
SEQRES 18 A 257 LEU ASP GLU LYS PHE PRO ALA SER GLN ALA ILE ILE ASP
SEQRES 19 A 257 THR ALA ARG ARG LEU MET GLY GLU SER ILE PRO LEU LYS
SEQRES 20 A 257 ARG TYR GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 257 MET ALA GLU VAL ILE VAL ILE THR SER GLY LYS GLY GLY
SEQRES 2 B 257 VAL GLY LYS THR THR LEU THR ALA ASN ILE GLY THR ALA
SEQRES 3 B 257 LEU ALA LYS LEU GLY LYS LYS VAL LEU LEU ILE ASP ALA
SEQRES 4 B 257 ASP ILE GLY LEU ARG ASN LEU ASP MET ILE LEU GLY LEU
SEQRES 5 B 257 GLU ASN ARG ILE VAL TYR ASP ILE LEU ASP VAL LEU GLU
SEQRES 6 B 257 GLY ARG VAL PRO TYR GLU LYS ALA LEU VAL LYS ASP LYS
SEQRES 7 B 257 ARG GLY LEU SER LEU TRP LEU LEU PRO ALA ASN GLN ARG
SEQRES 8 B 257 ALA ASN LYS ASP VAL ILE ASP ILE GLU LYS TRP ASN LYS
SEQRES 9 B 257 THR VAL GLU GLU ILE LYS ASN SER GLY ASN TYR ASP TYR
SEQRES 10 B 257 ILE LEU VAL ASP SER PRO ALA GLY ILE GLU LYS GLY PHE
SEQRES 11 B 257 GLN ILE ALA VAL SER PRO ALA ASP LYS ALA LEU ILE VAL
SEQRES 12 B 257 VAL ASN PRO GLU VAL SER SER ILE ARG ASP ALA ASP ARG
SEQRES 13 B 257 VAL ILE GLY LEU LEU GLU SER MET ASP LYS ARG ASN TYR
SEQRES 14 B 257 LYS VAL ILE VAL ASN ARG ILE LYS TRP GLU MET VAL LYS
SEQRES 15 B 257 ARG GLY ALA MET LEU SER VAL GLU ASP ILE VAL ASP ILE
SEQRES 16 B 257 LEU LYS ALA GLU ILE ILE GLY ILE ILE PRO GLU GLU PRO
SEQRES 17 B 257 LYS LEU VAL ASP PHE THR ASN ARG GLY GLU PRO ILE VAL
SEQRES 18 B 257 LEU ASP GLU LYS PHE PRO ALA SER GLN ALA ILE ILE ASP
SEQRES 19 B 257 THR ALA ARG ARG LEU MET GLY GLU SER ILE PRO LEU LYS
SEQRES 20 B 257 ARG TYR GLY SER HIS HIS HIS HIS HIS HIS
HET ADP A 303 27
HET MG A 401 1
HET ADP B 303 27
HET MG B 401 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 HOH *135(H2 O)
HELIX 1 1 GLY A 15 LEU A 30 1 16
HELIX 2 2 ASN A 45 LEU A 50 1 6
HELIX 3 3 LEU A 52 ILE A 56 5 5
HELIX 4 4 ASP A 59 GLY A 66 1 8
HELIX 5 5 PRO A 69 LEU A 74 1 6
HELIX 6 6 ASP A 98 SER A 112 1 15
HELIX 7 7 GLY A 129 SER A 135 1 7
HELIX 8 8 GLU A 147 SER A 163 1 17
HELIX 9 9 LYS A 177 ARG A 183 1 7
HELIX 10 10 SER A 188 LYS A 197 1 10
HELIX 11 11 LYS A 209 ARG A 216 1 8
HELIX 12 12 PRO A 219 ASP A 223 5 5
HELIX 13 13 PHE A 226 MET A 240 1 15
HELIX 14 14 GLY B 15 LEU B 30 1 16
HELIX 15 15 ASN B 45 LEU B 50 1 6
HELIX 16 16 LEU B 52 ILE B 56 5 5
HELIX 17 17 ASP B 59 GLY B 66 1 8
HELIX 18 18 PRO B 69 ALA B 73 5 5
HELIX 19 19 ASP B 98 GLY B 113 1 16
HELIX 20 20 GLY B 129 SER B 135 1 7
HELIX 21 21 GLU B 147 MET B 164 1 18
HELIX 22 22 LYS B 177 ARG B 183 1 7
HELIX 23 23 SER B 188 LYS B 197 1 10
HELIX 24 24 LYS B 209 ARG B 216 1 8
HELIX 25 25 PRO B 219 ASP B 223 5 5
HELIX 26 26 PHE B 226 MET B 240 1 15
SHEET 1 AA 8 VAL A 75 LYS A 76 0
SHEET 2 AA 8 LEU A 83 LEU A 86 -1 O LEU A 85 N VAL A 75
SHEET 3 AA 8 VAL A 34 ASP A 38 1 O VAL A 34 N TRP A 84
SHEET 4 AA 8 TYR A 117 ASP A 121 1 O TYR A 117 N LEU A 35
SHEET 5 AA 8 GLU A 3 SER A 9 1 O GLU A 3 N ILE A 118
SHEET 6 AA 8 LYS A 139 VAL A 144 1 O LYS A 139 N VAL A 6
SHEET 7 AA 8 TYR A 169 ILE A 176 1 O LYS A 170 N ILE A 142
SHEET 8 AA 8 ILE A 200 PRO A 205 1 N ILE A 201 O VAL A 171
SHEET 1 BA 8 VAL B 75 LYS B 76 0
SHEET 2 BA 8 LEU B 83 LEU B 86 -1 O LEU B 85 N VAL B 75
SHEET 3 BA 8 VAL B 34 ASP B 38 1 O VAL B 34 N TRP B 84
SHEET 4 BA 8 TYR B 117 ASP B 121 1 O TYR B 117 N LEU B 35
SHEET 5 BA 8 GLU B 3 SER B 9 1 O GLU B 3 N ILE B 118
SHEET 6 BA 8 LYS B 139 VAL B 144 1 O LYS B 139 N VAL B 6
SHEET 7 BA 8 TYR B 169 ILE B 176 1 O LYS B 170 N ILE B 142
SHEET 8 BA 8 ILE B 200 PRO B 205 1 N ILE B 201 O VAL B 171
LINK O1B ADP A 303 MG MG A 401 1555 1555 2.08
LINK MG MG A 401 OG1 THR A 17 1555 1555 2.03
LINK MG MG A 401 O HOH A2006 1555 1555 2.25
LINK MG MG A 401 O HOH A2007 1555 1555 2.04
LINK MG MG A 401 O HOH A2012 1555 1555 2.04
LINK MG MG A 401 O HOH A2005 1555 1555 2.09
LINK O1B ADP B 303 MG MG B 401 1555 1555 2.08
LINK MG MG B 401 OG1 THR B 17 1555 1555 2.10
LINK MG MG B 401 O HOH B2005 1555 1555 2.01
LINK MG MG B 401 O HOH B2006 1555 1555 2.18
LINK MG MG B 401 O HOH B2008 1555 1555 1.85
LINK MG MG B 401 O HOH B2018 1555 1555 2.12
CISPEP 1 GLY A 66 ARG A 67 0 -14.33
CISPEP 2 GLY B 66 ARG B 67 0 -19.22
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 44 ASN A 174
SITE 3 AC1 17 ARG A 175 PRO A 205 GLU A 206 GLU A 207
SITE 4 AC1 17 LEU A 210 THR A 214 MG A 401 HOH A2007
SITE 5 AC1 17 HOH A2012
SITE 1 AC2 6 THR A 17 ADP A 303 HOH A2005 HOH A2006
SITE 2 AC2 6 HOH A2007 HOH A2012
SITE 1 AC3 20 GLY B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC3 20 THR B 17 THR B 18 ARG B 44 ASN B 174
SITE 3 AC3 20 ARG B 175 PRO B 205 GLU B 206 GLU B 207
SITE 4 AC3 20 LEU B 210 VAL B 211 THR B 214 MG B 401
SITE 5 AC3 20 HOH B2005 HOH B2008 HOH B2018 HOH B2070
SITE 1 AC4 6 THR B 17 ADP B 303 HOH B2005 HOH B2006
SITE 2 AC4 6 HOH B2008 HOH B2018
CRYST1 36.234 51.671 69.085 71.30 89.21 69.93 P 1 2
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 0.027598 -0.010083 0.003197 0.00000
SCALE2 0.000000 0.020604 -0.007359 0.00000
SCALE3 0.000000 0.000000 0.015372 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
