HEADER HYDROLASE 23-FEB-15 4YDS
TITLE FLAH FROM SULFOLOBUS ACIDOCALDARIUS WITH ATP AND MG-ION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLA-RELATED PROTEIN H;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_TAXID: 330779;
SOURCE 4 STRAIN: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
SOURCE 5 GENE: SACI_1174;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS RECA SUPERFAMILY ATPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.REINDL,A.S.ARVAI,J.A.TAINER
REVDAT 5 27-SEP-23 4YDS 1 REMARK
REVDAT 4 04-DEC-19 4YDS 1 REMARK
REVDAT 3 20-SEP-17 4YDS 1 JRNL REMARK
REVDAT 2 24-FEB-16 4YDS 1 JRNL
REVDAT 1 11-NOV-15 4YDS 0
JRNL AUTH P.CHAUDHURY,T.NEINER,E.D'IMPRIMA,A.BANERJEE,S.REINDL,
JRNL AUTH 2 A.GHOSH,A.S.ARVAI,D.J.MILLS,C.VAN DER DOES,J.A.TAINER,
JRNL AUTH 3 J.VONCK,S.V.ALBERS
JRNL TITL THE NUCLEOTIDE-DEPENDENT INTERACTION OF FLAH AND FLAI IS
JRNL TITL 2 ESSENTIAL FOR ASSEMBLY AND FUNCTION OF THE ARCHAELLUM MOTOR.
JRNL REF MOL.MICROBIOL. V. 99 674 2016
JRNL REFN ESSN 1365-2958
JRNL PMID 26508112
JRNL DOI 10.1111/MMI.13260
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.5
REMARK 3 NUMBER OF REFLECTIONS : 11154
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 559
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 42.9408 - 3.6510 0.99 3232 171 0.1884 0.2302
REMARK 3 2 3.6510 - 2.8981 0.98 3174 166 0.1734 0.2408
REMARK 3 3 2.8981 - 2.5318 0.86 2714 142 0.2198 0.2989
REMARK 3 4 2.5318 - 2.3000 0.47 1475 80 0.2736 0.3302
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 : 0.37
REMARK 3 B_SOL : 80.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.580
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) : -7.73340
REMARK 3 B22 (A**2) : 6.94930
REMARK 3 B33 (A**2) : 0.78410
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.61550
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 1824
REMARK 3 ANGLE : 0.976 2465
REMARK 3 CHIRALITY : 0.058 297
REMARK 3 PLANARITY : 0.003 297
REMARK 3 DIHEDRAL : 15.933 691
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:79)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5338 21.1052 12.5316
REMARK 3 T TENSOR
REMARK 3 T11: 0.1993 T22: 0.2791
REMARK 3 T33: 0.2006 T12: 0.0172
REMARK 3 T13: -0.0212 T23: -0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 2.7561 L22: 2.3358
REMARK 3 L33: 2.6660 L12: -0.0405
REMARK 3 L13: 0.3314 L23: -0.8226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0742 S12: -0.5768 S13: 0.2457
REMARK 3 S21: 0.0825 S22: 0.0153 S23: -0.0416
REMARK 3 S31: -0.0775 S32: -0.2936 S33: 0.0331
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 80:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0792 5.9509 19.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.3640 T22: 0.8242
REMARK 3 T33: 0.6201 T12: 0.0735
REMARK 3 T13: 0.0369 T23: 0.4324
REMARK 3 L TENSOR
REMARK 3 L11: 1.8886 L22: 1.0971
REMARK 3 L33: 0.4987 L12: 0.3487
REMARK 3 L13: 0.4458 L23: 0.2385
REMARK 3 S TENSOR
REMARK 3 S11: 0.2335 S12: -1.3850 S13: -0.5435
REMARK 3 S21: -0.3989 S22: -0.3498 S23: -0.4403
REMARK 3 S31: 0.0832 S32: 0.1527 S33: 0.3030
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 97:184)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6618 6.9842 3.5113
REMARK 3 T TENSOR
REMARK 3 T11: 0.3969 T22: 0.2443
REMARK 3 T33: 0.3409 T12: -0.0387
REMARK 3 T13: 0.0534 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 2.4994 L22: 1.5074
REMARK 3 L33: 0.7212 L12: 0.6806
REMARK 3 L13: -0.1169 L23: -0.7205
REMARK 3 S TENSOR
REMARK 3 S11: -0.2713 S12: 0.1563 S13: -0.4276
REMARK 3 S21: -0.5022 S22: 0.0531 S23: -0.3069
REMARK 3 S31: 0.2407 S32: -0.0478 S33: 0.1589
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 185:226)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2390 29.6933 3.6190
REMARK 3 T TENSOR
REMARK 3 T11: 0.3205 T22: 0.2912
REMARK 3 T33: 0.4966 T12: -0.0005
REMARK 3 T13: 0.0045 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 1.7218 L22: 1.3063
REMARK 3 L33: 1.7136 L12: 0.6478
REMARK 3 L13: -0.7550 L23: -0.3154
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: 0.1447 S13: 0.9921
REMARK 3 S21: -0.3215 S22: -0.1892 S23: 0.2575
REMARK 3 S31: -0.5899 S32: -0.4181 S33: 0.0681
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 4YDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000207285.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11612
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.5
REMARK 200 DATA REDUNDANCY : 2.440
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 2DR3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.0, 32.5% PEG 3350,
REMARK 280 150MM NASCN, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.67550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.47250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.67550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.47250
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 103.35100
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1001 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1015 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1025 LIES ON A SPECIAL POSITION.
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 ARG A 227
REMARK 465 ALA A 228
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 SER A 226 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 48 42.75 -79.44
REMARK 500 PHE A 93 140.29 83.22
REMARK 500 SER A 123 79.77 83.88
REMARK 500 ILE A 185 -73.86 -107.08
REMARK 500 SER A 205 -90.42 -131.10
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 A1054 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1055 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1056 DISTANCE = 6.91 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 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 34 OG
REMARK 620 2 GLU A 57 OE1 69.3
REMARK 620 3 GLU A 57 OE2 113.9 49.2
REMARK 620 4 ATP A 901 O2B 80.0 136.6 163.2
REMARK 620 5 ATP A 901 O3B 105.5 104.4 110.3 54.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DR3 RELATED DB: PDB
DBREF 4YDS A 1 228 UNP Q4J9K9 Q4J9K9_SULAC 1 228
SEQRES 1 A 228 MET ILE ILE SER THR GLY ASN ASP ASP LEU ASP ARG ARG
SEQRES 2 A 228 LEU GLY GLY ILE PRO TYR PRO ALA SER ILE MET ILE GLU
SEQRES 3 A 228 GLY ASP HIS GLY THR GLY LYS SER VAL LEU SER ALA GLN
SEQRES 4 A 228 PHE VAL LEU GLY PHE LEU LEU SER ASP LYS LYS GLY TYR
SEQRES 5 A 228 VAL ILE THR THR GLU GLN THR THR LYS ASP TYR LEU ILE
SEQRES 6 A 228 LYS MET LYS GLU ILE LYS ILE ASP LEU ILE PRO TYR PHE
SEQRES 7 A 228 ILE ARG GLY LYS LEU ARG ILE ALA PRO LEU ASN THR LYS
SEQRES 8 A 228 LYS PHE ASN TRP ASN SER SER LEU ALA GLU LYS ILE LEU
SEQRES 9 A 228 ASP VAL ILE VAL ASN PHE ILE ARG SER LYS ASN ILE ASP
SEQRES 10 A 228 PHE ILE VAL ILE ASP SER LEU SER ILE LEU ALA ALA PHE
SEQRES 11 A 228 SER LYS GLU LYS GLN LEU LEU GLN PHE MET LYS ASP ILE
SEQRES 12 A 228 ARG VAL LEU VAL ASN THR GLY LYS MET ILE LEU PHE THR
SEQRES 13 A 228 ILE HIS PRO ASP THR PHE ASP GLU GLU MET LYS SER LYS
SEQRES 14 A 228 ILE THR SER ILE VAL ASP VAL TYR LEU LYS LEU SER ALA
SEQRES 15 A 228 ALA THR ILE GLY GLY ARG ARG VAL LYS ILE LEU GLU ARG
SEQRES 16 A 228 VAL LYS THR THR GLY GLY ILE SER GLY SER ASP THR ILE
SEQRES 17 A 228 SER PHE ASP VAL ASP PRO ALA LEU GLY ILE LYS VAL VAL
SEQRES 18 A 228 PRO LEU SER LEU SER ARG ALA
HET ATP A 901 31
HET MG A 902 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 ATP C10 H16 N5 O13 P3
FORMUL 3 MG MG 2+
FORMUL 4 HOH *81(H2 O)
HELIX 1 AA1 ASN A 7 GLY A 15 1 9
HELIX 2 AA2 GLY A 32 SER A 47 1 16
HELIX 3 AA3 THR A 59 ILE A 70 1 12
HELIX 4 AA4 LEU A 74 ARG A 80 1 7
HELIX 5 AA5 ASN A 96 SER A 113 1 18
HELIX 6 AA6 LEU A 124 SER A 131 1 8
HELIX 7 AA7 LYS A 132 THR A 149 1 18
HELIX 8 AA8 ASP A 163 VAL A 174 1 12
SHEET 1 AA1 2 ILE A 2 ILE A 3 0
SHEET 2 AA1 2 ILE A 17 PRO A 18 -1 O ILE A 17 N ILE A 3
SHEET 1 AA2 9 LEU A 83 PRO A 87 0
SHEET 2 AA2 9 GLY A 51 THR A 55 1 N VAL A 53 O ALA A 86
SHEET 3 AA2 9 PHE A 118 ASP A 122 1 O VAL A 120 N ILE A 54
SHEET 4 AA2 9 MET A 152 ILE A 157 1 O MET A 152 N ILE A 119
SHEET 5 AA2 9 SER A 22 GLY A 27 1 N ILE A 23 O ILE A 153
SHEET 6 AA2 9 VAL A 176 THR A 184 1 O LEU A 180 N GLU A 26
SHEET 7 AA2 9 ARG A 189 LYS A 197 -1 O VAL A 190 N ALA A 183
SHEET 8 AA2 9 ILE A 208 ASP A 213 -1 O ILE A 208 N LEU A 193
SHEET 9 AA2 9 GLY A 217 VAL A 220 -1 O GLY A 217 N ASP A 213
LINK OG SER A 34 MG MG A 902 1555 1555 2.57
LINK OE1 GLU A 57 MG MG A 902 1555 1555 2.50
LINK OE2 GLU A 57 MG MG A 902 1555 1555 2.76
LINK O2B ATP A 901 MG MG A 902 1555 1555 2.53
LINK O3B ATP A 901 MG MG A 902 1555 1555 2.88
CISPEP 1 TYR A 19 PRO A 20 0 -0.67
CISPEP 2 GLY A 201 ILE A 202 0 0.74
SITE 1 AC1 17 ASP A 28 HIS A 29 GLY A 30 THR A 31
SITE 2 AC1 17 GLY A 32 LYS A 33 SER A 34 VAL A 35
SITE 3 AC1 17 GLU A 57 ILE A 70 LYS A 191 VAL A 212
SITE 4 AC1 17 PRO A 214 MG A 902 HOH A1038 HOH A1043
SITE 5 AC1 17 HOH A1058
SITE 1 AC2 4 SER A 34 GLU A 57 ASP A 122 ATP A 901
CRYST1 103.351 52.945 73.590 90.00 130.78 90.00 C 1 2 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 0.009676 0.000000 0.008345 0.00000
SCALE2 0.000000 0.018888 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
