HEADER DNA BINDING PROTEIN 20-MAR-02 1L8H
TITLE DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA PROTECTION DURING STARVATION PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DODECAMER, METAL BOUND COMPLEX, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUO,D.LIU,M.A.WHITE,R.O.FOX
REVDAT 4 16-AUG-23 1L8H 1 REMARK
REVDAT 3 27-OCT-21 1L8H 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1L8H 1 VERSN
REVDAT 1 24-JUN-03 1L8H 0
JRNL AUTH J.LUO,D.LIU,M.A.WHITE,R.O.FOX
JRNL TITL DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENG AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3697305.580
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 35985
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1834
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1636
REMARK 3 BIN R VALUE (WORKING SET) : 0.3420
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 99
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14727
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : 1.04000
REMARK 3 B12 (A**2) : 4.70000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.63
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.70
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 17.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.670
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.280 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.280 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.550 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.620 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 49.52
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: WEIGHTED R=18.5%
REMARK 4
REMARK 4 1L8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015737.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : 8.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36212
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: CNS 1.0
REMARK 200 STARTING MODEL: 1F33
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM MOPS, 100MM KCL, 10%GLYCEROL +
REMARK 280 100MM TRISHCL, 100MM KCL, 10% GLYCEROL, 11% PEG 8000, AND 5MM
REMARK 280 DTT, PH 8.10, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 159.80933
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 79.90467
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 300 REMARK: THE DODECAMER IS THE BIOLOGICAL ASSEMBLY
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 49380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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 SER A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 LYS A 5
REMARK 465 LEU A 6
REMARK 465 VAL A 7
REMARK 465 LYS A 8
REMARK 465 SER A 9
REMARK 465 LYS A 10
REMARK 465 ALA A 11
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 LYS B 5
REMARK 465 LEU B 6
REMARK 465 VAL B 7
REMARK 465 LYS B 8
REMARK 465 SER B 9
REMARK 465 LYS B 10
REMARK 465 ALA B 11
REMARK 465 THR B 12
REMARK 465 ASN B 13
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 ALA C 4
REMARK 465 LYS C 5
REMARK 465 LEU C 6
REMARK 465 VAL C 7
REMARK 465 LYS C 8
REMARK 465 SER C 9
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 THR D 3
REMARK 465 ALA D 4
REMARK 465 LYS D 5
REMARK 465 LEU D 6
REMARK 465 VAL D 7
REMARK 465 LYS D 8
REMARK 465 SER D 9
REMARK 465 LYS D 10
REMARK 465 ALA D 11
REMARK 465 THR D 12
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 THR E 3
REMARK 465 ALA E 4
REMARK 465 LYS E 5
REMARK 465 LEU E 6
REMARK 465 VAL E 7
REMARK 465 LYS E 8
REMARK 465 SER E 9
REMARK 465 LYS E 10
REMARK 465 ALA E 11
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 THR F 3
REMARK 465 ALA F 4
REMARK 465 LYS F 5
REMARK 465 LEU F 6
REMARK 465 VAL F 7
REMARK 465 LYS F 8
REMARK 465 SER F 9
REMARK 465 LYS F 10
REMARK 465 ALA F 11
REMARK 465 THR F 12
REMARK 465 ASN F 13
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 THR G 3
REMARK 465 ALA G 4
REMARK 465 LYS G 5
REMARK 465 LEU G 6
REMARK 465 VAL G 7
REMARK 465 LYS G 8
REMARK 465 SER G 9
REMARK 465 LYS G 10
REMARK 465 ALA G 11
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 THR H 3
REMARK 465 ALA H 4
REMARK 465 LYS H 5
REMARK 465 LEU H 6
REMARK 465 VAL H 7
REMARK 465 LYS H 8
REMARK 465 SER H 9
REMARK 465 LYS H 10
REMARK 465 ALA H 11
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 THR I 3
REMARK 465 ALA I 4
REMARK 465 LYS I 5
REMARK 465 LEU I 6
REMARK 465 VAL I 7
REMARK 465 LYS I 8
REMARK 465 SER I 9
REMARK 465 LYS I 10
REMARK 465 ALA I 11
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 THR J 3
REMARK 465 ALA J 4
REMARK 465 LYS J 5
REMARK 465 LEU J 6
REMARK 465 VAL J 7
REMARK 465 LYS J 8
REMARK 465 SER J 9
REMARK 465 LYS J 10
REMARK 465 ALA J 11
REMARK 465 MET K 1
REMARK 465 SER K 2
REMARK 465 THR K 3
REMARK 465 ALA K 4
REMARK 465 LYS K 5
REMARK 465 LEU K 6
REMARK 465 VAL K 7
REMARK 465 LYS K 8
REMARK 465 SER K 9
REMARK 465 LYS K 10
REMARK 465 ALA K 11
REMARK 465 THR K 12
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 THR L 3
REMARK 465 ALA L 4
REMARK 465 LYS L 5
REMARK 465 LEU L 6
REMARK 465 VAL L 7
REMARK 465 LYS L 8
REMARK 465 SER L 9
REMARK 465 LYS L 10
REMARK 465 ALA L 11
REMARK 465 THR L 12
REMARK 465 ASN L 13
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 ARG B 70 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG H 70 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG H 70 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG J 35 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG J 35 NE - CZ - NH2 ANGL. DEV. = 4.5 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 LEU A 14 154.09 -36.90
REMARK 500 ARG A 18 1.43 -64.29
REMARK 500 ASP A 20 41.50 -72.59
REMARK 500 ASN A 53 52.03 -96.48
REMARK 500 HIS A 112 -43.26 -144.71
REMARK 500 SER A 164 -18.79 -47.25
REMARK 500 ARG B 18 5.18 -63.74
REMARK 500 ASP B 20 41.01 -73.46
REMARK 500 ASN B 53 50.91 -97.73
REMARK 500 SER B 100 -70.50 -76.14
REMARK 500 HIS B 112 -44.98 -143.00
REMARK 500 SER B 164 -16.05 -49.39
REMARK 500 ALA C 11 -71.06 -125.90
REMARK 500 ARG C 18 2.35 -63.94
REMARK 500 ASP C 20 40.84 -72.01
REMARK 500 ASN C 53 51.77 -96.33
REMARK 500 SER C 100 -70.44 -74.35
REMARK 500 HIS C 112 -43.54 -141.68
REMARK 500 SER C 164 -18.38 -47.78
REMARK 500 ARG D 18 1.83 -65.20
REMARK 500 ASP D 20 40.20 -74.02
REMARK 500 ASN D 53 54.45 -96.04
REMARK 500 HIS D 112 -44.00 -143.82
REMARK 500 SER D 164 -13.67 -49.20
REMARK 500 ASN E 13 -160.36 -126.55
REMARK 500 ASP E 20 41.12 -74.30
REMARK 500 ASN E 53 54.04 -96.90
REMARK 500 SER E 100 -70.66 -76.63
REMARK 500 HIS E 112 -46.24 -141.29
REMARK 500 SER E 164 -18.57 -46.15
REMARK 500 ARG F 18 4.89 -66.42
REMARK 500 ASP F 20 41.67 -72.87
REMARK 500 ASN F 53 53.88 -95.55
REMARK 500 SER F 100 -71.52 -75.31
REMARK 500 HIS F 112 -47.73 -142.26
REMARK 500 SER F 164 -16.29 -49.11
REMARK 500 ASP G 20 39.09 -72.09
REMARK 500 ASN G 53 51.33 -98.10
REMARK 500 SER G 100 -70.01 -76.75
REMARK 500 HIS G 112 -44.89 -145.30
REMARK 500 SER G 164 -17.02 -49.29
REMARK 500 ARG H 18 1.27 -65.45
REMARK 500 ASP H 20 38.19 -70.62
REMARK 500 ASN H 53 51.92 -98.09
REMARK 500 HIS H 112 -44.13 -144.16
REMARK 500 SER H 164 -17.23 -48.57
REMARK 500 LEU I 14 -171.40 -58.86
REMARK 500 ARG I 18 4.27 -62.66
REMARK 500 ASP I 20 41.97 -71.57
REMARK 500 ASN I 53 51.31 -97.34
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
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 K B 256 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 82 OE1
REMARK 620 2 GLU B 82 OE2 34.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 262 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 146 OD2
REMARK 620 2 ASP F 146 OD2 75.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 251 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 82 OE1
REMARK 620 2 GLU E 82 OE2 35.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K K 257 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 82 OE1
REMARK 620 2 GLU K 82 OE2 34.5
REMARK 620 3 HOH L 603 O 116.6 82.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K L 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K K 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS G 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS J 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS D 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS E 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DPS RELATED DB: PDB
REMARK 900 1DPS CONTAINS THE STRUCTURE OF APO DPS IN A DIFFERENT SPACE GROUP
REMARK 900 RELATED ID: 1F33 RELATED DB: PDB
REMARK 900 1F33 CONTAINS THE APO WT PROTEIN IN SPACE GROUP C2221
REMARK 900 RELATED ID: 1F30 RELATED DB: PDB
REMARK 900 1F30 CONTAINS THE WT PROTEIN WITH ZINC IN SPACE GROUP C2221
REMARK 900 RELATED ID: 1JRE RELATED DB: PDB
REMARK 900 1JRE IS A DPS CD COMPLEX
REMARK 900 RELATED ID: 1L8I RELATED DB: PDB
REMARK 900 1L8I IS DNA PROTECTION AND BINDING BY E. COLI DPS PROTEIN
DBREF 1L8H A 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H B 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H C 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H D 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H E 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H F 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H G 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H H 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H I 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H J 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H K 1 167 UNP P0ABT2 DPS_ECOLI 0 166
DBREF 1L8H L 1 167 UNP P0ABT2 DPS_ECOLI 0 166
SEQADV 1L8H CYS A 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA A 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS B 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA B 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS C 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA C 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS D 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA D 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS E 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA E 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS F 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA F 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS G 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA G 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS H 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA H 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS I 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA I 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS J 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA J 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS K 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA K 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQADV 1L8H CYS L 75 UNP P0ABT2 ASP 74 ENGINEERED MUTATION
SEQADV 1L8H ALA L 78 UNP P0ABT2 ASP 77 ENGINEERED MUTATION
SEQRES 1 A 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 A 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 A 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 A 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 A 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 A 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 A 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 A 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 A 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 A 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 A 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 A 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 A 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 B 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 B 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 B 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 B 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 B 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 B 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 B 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 B 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 B 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 B 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 B 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 B 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 B 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 C 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 C 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 C 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 C 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 C 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 C 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 C 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 C 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 C 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 C 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 C 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 C 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 C 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 D 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 D 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 D 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 D 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 D 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 D 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 D 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 D 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 D 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 D 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 D 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 D 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 D 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 E 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 E 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 E 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 E 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 E 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 E 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 E 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 E 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 E 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 E 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 E 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 E 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 E 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 F 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 F 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 F 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 F 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 F 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 F 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 F 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 F 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 F 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 F 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 F 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 F 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 F 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 G 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 G 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 G 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 G 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 G 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 G 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 G 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 G 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 G 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 G 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 G 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 G 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 G 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 H 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 H 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 H 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 H 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 H 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 H 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 H 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 H 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 H 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 H 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 H 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 H 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 H 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 I 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 I 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 I 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 I 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 I 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 I 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 I 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 I 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 I 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 I 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 I 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 I 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 I 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 J 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 J 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 J 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 J 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 J 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 J 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 J 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 J 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 J 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 J 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 J 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 J 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 J 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 K 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 K 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 K 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 K 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 K 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 K 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 K 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 K 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 K 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 K 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 K 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 K 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 K 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
SEQRES 1 L 167 MET SER THR ALA LYS LEU VAL LYS SER LYS ALA THR ASN
SEQRES 2 L 167 LEU LEU TYR THR ARG ASN ASP VAL SER ASP SER GLU LYS
SEQRES 3 L 167 LYS ALA THR VAL GLU LEU LEU ASN ARG GLN VAL ILE GLN
SEQRES 4 L 167 PHE ILE ASP LEU SER LEU ILE THR LYS GLN ALA HIS TRP
SEQRES 5 L 167 ASN MET ARG GLY ALA ASN PHE ILE ALA VAL HIS GLU MET
SEQRES 6 L 167 LEU ASP GLY PHE ARG THR ALA LEU ILE CYS HIS LEU ALA
SEQRES 7 L 167 THR MET ALA GLU ARG ALA VAL GLN LEU GLY GLY VAL ALA
SEQRES 8 L 167 LEU GLY THR THR GLN VAL ILE ASN SER LYS THR PRO LEU
SEQRES 9 L 167 LYS SER TYR PRO LEU ASP ILE HIS ASN VAL GLN ASP HIS
SEQRES 10 L 167 LEU LYS GLU LEU ALA ASP ARG TYR ALA ILE VAL ALA ASN
SEQRES 11 L 167 ASP VAL ARG LYS ALA ILE GLY GLU ALA LYS ASP ASP ASP
SEQRES 12 L 167 THR ALA ASP ILE LEU THR ALA ALA SER ARG ASP LEU ASP
SEQRES 13 L 167 LYS PHE LEU TRP PHE ILE GLU SER ASN ILE GLU
HET K A 252 1
HET TRS A 301 8
HET TRS A 309 8
HET K B 256 1
HET TRS B 304 8
HET TRS B 312 8
HET K C 262 1
HET TRS C 307 8
HET K D 261 1
HET TRS D 305 8
HET TRS D 306 8
HET TRS D 310 8
HET K E 251 1
HET TRS E 311 8
HET K G 254 1
HET K G 259 1
HET K G 260 1
HET TRS G 303 8
HET K H 253 1
HET K J 258 1
HET TRS J 308 8
HET K K 257 1
HET TRS K 302 8
HET K L 255 1
HETNAM K POTASSIUM ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 13 K 12(K 1+)
FORMUL 14 TRS 12(C4 H12 N O3 1+)
FORMUL 37 HOH *114(H2 O)
HELIX 1 1 SER A 22 ASN A 53 1 32
HELIX 2 2 ASN A 58 LEU A 87 1 30
HELIX 3 3 THR A 94 THR A 102 1 9
HELIX 4 4 ASN A 113 ALA A 139 1 27
HELIX 5 5 ASP A 141 ASN A 165 1 25
HELIX 6 6 SER B 22 ASN B 53 1 32
HELIX 7 7 ASN B 58 LEU B 87 1 30
HELIX 8 8 THR B 94 THR B 102 1 9
HELIX 9 9 ASN B 113 ALA B 139 1 27
HELIX 10 10 ASP B 141 ASN B 165 1 25
HELIX 11 11 SER C 22 ASN C 53 1 32
HELIX 12 12 ASN C 58 LEU C 87 1 30
HELIX 13 13 THR C 94 THR C 102 1 9
HELIX 14 14 ASN C 113 ALA C 139 1 27
HELIX 15 15 ASP C 141 ASN C 165 1 25
HELIX 16 16 SER D 22 ASN D 53 1 32
HELIX 17 17 ASN D 58 LEU D 87 1 30
HELIX 18 18 THR D 94 THR D 102 1 9
HELIX 19 19 ASN D 113 ALA D 139 1 27
HELIX 20 20 ASP D 141 SER D 164 1 24
HELIX 21 21 SER E 22 ASN E 53 1 32
HELIX 22 22 ASN E 58 LEU E 87 1 30
HELIX 23 23 THR E 94 THR E 102 1 9
HELIX 24 24 ASN E 113 ALA E 139 1 27
HELIX 25 25 ASP E 141 ASN E 165 1 25
HELIX 26 26 SER F 22 ASN F 53 1 32
HELIX 27 27 ASN F 58 LEU F 87 1 30
HELIX 28 28 THR F 94 THR F 102 1 9
HELIX 29 29 ASN F 113 ALA F 139 1 27
HELIX 30 30 ASP F 141 ASN F 165 1 25
HELIX 31 31 SER G 22 ASN G 53 1 32
HELIX 32 32 ASN G 58 LEU G 87 1 30
HELIX 33 33 THR G 94 THR G 102 1 9
HELIX 34 34 ASN G 113 ALA G 139 1 27
HELIX 35 35 ASP G 141 ASN G 165 1 25
HELIX 36 36 SER H 22 ASN H 53 1 32
HELIX 37 37 ASN H 58 LEU H 87 1 30
HELIX 38 38 THR H 94 THR H 102 1 9
HELIX 39 39 ASN H 113 ALA H 139 1 27
HELIX 40 40 ASP H 141 ASN H 165 1 25
HELIX 41 41 SER I 22 ASN I 53 1 32
HELIX 42 42 ASN I 58 LEU I 87 1 30
HELIX 43 43 THR I 94 THR I 102 1 9
HELIX 44 44 ASN I 113 ALA I 139 1 27
HELIX 45 45 ASP I 141 SER I 164 1 24
HELIX 46 46 SER J 22 ASN J 53 1 32
HELIX 47 47 ASN J 58 LEU J 87 1 30
HELIX 48 48 THR J 94 THR J 102 1 9
HELIX 49 49 ASN J 113 ALA J 139 1 27
HELIX 50 50 ASP J 141 ASN J 165 1 25
HELIX 51 51 SER K 22 ASN K 53 1 32
HELIX 52 52 ASN K 58 LEU K 87 1 30
HELIX 53 53 THR K 94 THR K 102 1 9
HELIX 54 54 ASN K 113 ALA K 139 1 27
HELIX 55 55 ASP K 141 ASN K 165 1 25
HELIX 56 56 SER L 22 ASN L 53 1 32
HELIX 57 57 ASN L 58 LEU L 87 1 30
HELIX 58 58 THR L 94 THR L 102 1 9
HELIX 59 59 ASN L 113 ALA L 139 1 27
HELIX 60 60 ASP L 141 ASN L 165 1 25
LINK OE1 GLU B 82 K K B 256 1555 1555 3.71
LINK OE2 GLU B 82 K K B 256 1555 1555 3.72
LINK OD2 ASP C 146 K K C 262 1555 1555 3.24
LINK K K C 262 OD2 ASP F 146 1555 1555 3.68
LINK OE1 GLU E 82 K K E 251 1555 1555 3.71
LINK OE2 GLU E 82 K K E 251 1555 1555 3.59
LINK OD2 ASP G 146 K K G 260 1555 1555 3.33
LINK NH1 ARG G 153 K K G 259 1555 1555 2.93
LINK K K J 258 O HOH J 513 1555 1555 3.28
LINK OE1 GLU K 82 K K K 257 1555 1555 3.72
LINK OE2 GLU K 82 K K K 257 1555 1555 3.70
LINK K K K 257 O HOH L 603 1555 1555 3.05
LINK K K L 255 O HOH L 589 1555 1555 3.06
SITE 1 AC1 1 GLU E 82
SITE 1 AC2 1 HOH L 589
SITE 1 AC3 1 HOH L 603
SITE 1 AC4 1 ARG G 153
SITE 1 AC5 1 ASP G 146
SITE 1 AC6 2 ASP C 146 ASP F 146
SITE 1 AC7 3 ASP A 146 ASP E 146 ASP I 146
SITE 1 AC8 3 GLU C 64 GLU G 64 GLU K 64
SITE 1 AC9 3 GLU C 167 GLU G 167 GLU K 167
SITE 1 BC1 3 ASP B 146 ASP H 146 ASP K 146
SITE 1 BC2 3 GLU D 64 GLU F 64 GLU I 64
SITE 1 BC3 3 GLU D 167 GLU F 167 GLU I 167
SITE 1 BC4 3 ASP C 146 ASP F 146 ASP L 146
SITE 1 BC5 3 GLU A 64 GLU H 64 GLU J 64
SITE 1 BC6 3 GLU A 167 GLU H 167 GLU J 167
SITE 1 BC7 3 ASP D 146 ASP G 146 ASP J 146
SITE 1 BC8 3 GLU B 64 GLU E 64 GLU L 64
SITE 1 BC9 3 GLU B 167 GLU E 167 GLU L 167
CRYST1 91.265 91.265 239.714 90.00 90.00 120.00 P 32 36
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 0.010957 0.006326 0.000000 0.00000
SCALE2 0.000000 0.012652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004172 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
