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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-DEC-08 3FLE
TITLE SE_1780 PROTEIN OF UNKNOWN FUNCTION FROM STAPHYLOCOCCUS
TITLE 2 EPIDERMIDIS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SE_1780 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS EPIDERMIDIS ATCC 12228;
SOURCE 3 ORGANISM_TAXID: 176280;
SOURCE 4 STRAIN: ATCC 12228;
SOURCE 5 GENE: SE_1780;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, APC61035.1, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,C.HATZOS,S.CLANCY,Y.KIM,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 13-JAN-09 3FLE 0
JRNL AUTH J.OSIPIUK,C.HATZOS,S.CLANCY,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF SE_1780 PROTEIN OF
JRNL TITL 2 UNKNOWN FUNCTION FROM STAPHYLOCOCCUS EPIDERMIDIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.01 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-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 71468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.330
REMARK 3 FREE R VALUE TEST SET COUNT : 3810
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 26.9980 - 5.4400 0.98 3526 199 0.1970 0.2530
REMARK 3 2 5.4400 - 4.3240 0.98 3415 145 0.1150 0.1480
REMARK 3 3 4.3240 - 3.7790 0.98 3469 155 0.1110 0.1440
REMARK 3 4 3.7790 - 3.4340 0.98 3488 171 0.1260 0.1610
REMARK 3 5 3.4340 - 3.1880 0.98 3420 187 0.1570 0.1740
REMARK 3 6 3.1880 - 3.0000 0.98 3559 186 0.1750 0.2140
REMARK 3 7 3.0000 - 2.8500 0.98 3543 228 0.1860 0.2420
REMARK 3 8 2.8500 - 2.7270 0.98 3532 230 0.2000 0.2430
REMARK 3 9 2.7270 - 2.6220 0.98 3525 195 0.2080 0.2430
REMARK 3 10 2.6220 - 2.5310 0.98 3465 174 0.2130 0.2410
REMARK 3 11 2.5310 - 2.4520 0.98 3547 180 0.2290 0.2700
REMARK 3 12 2.4520 - 2.3820 0.98 3553 180 0.2310 0.2780
REMARK 3 13 2.3820 - 2.3190 0.98 3408 229 0.2280 0.2590
REMARK 3 14 2.3190 - 2.2630 0.98 3523 191 0.2510 0.2800
REMARK 3 15 2.2630 - 2.2110 0.98 3428 160 0.2460 0.3140
REMARK 3 16 2.2110 - 2.1640 0.98 3474 174 0.2420 0.3080
REMARK 3 17 2.1640 - 2.1210 0.98 3303 173 0.2530 0.3180
REMARK 3 18 2.1210 - 2.0810 0.98 3144 177 0.2610 0.2580
REMARK 3 19 2.0810 - 2.0440 0.98 2977 160 0.2630 0.2800
REMARK 3 20 2.0440 - 2.0090 0.98 2556 119 0.2680 0.3140
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 : 0.36
REMARK 3 B_SOL : 52.20
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.34500
REMARK 3 B22 (A**2) : -7.95800
REMARK 3 B33 (A**2) : 0.42400
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00700
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.4880
REMARK 3 OPERATOR: -H,-K,L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 3966
REMARK 3 ANGLE : 1.112 5320
REMARK 3 CHIRALITY : 0.075 560
REMARK 3 PLANARITY : 0.004 692
REMARK 3 DIHEDRAL : 18.742 1462
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: REFINEMENT WAS PERFORMED USING TWIN
REMARK 3 LAW -H,-K,L AND TWIN FRACTION 0.49. UNKNOWN LIGANDS WERE
REMARK 3 MODELED AS WATERS IN CHAINS X AND Y. THE FRIEDEL PAIRS WERE
REMARK 3 USED FOR PHASING.
REMARK 4
REMARK 4 3FLE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB050733.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77366
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.009
REMARK 200 RESOLUTION RANGE LOW (A) : 27.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.6820
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 1000, 0.1 M TRIS BUFFER, PH
REMARK 280 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
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 46.36100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.72900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.36100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.72900
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 300 REMARK: A PUTATIVE BIOLOGICAL UNIT IS A MONOMER BASED ON PISA
REMARK 300 PROGRAM
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 40
REMARK 465 ASN A 41
REMARK 465 ALA A 42
REMARK 465 ILE A 43
REMARK 465 GLU A 96
REMARK 465 ASP A 97
REMARK 465 SER B 40
REMARK 465 ASN B 41
REMARK 465 ALA B 42
REMARK 465 ILE B 43
REMARK 465 GLU B 96
REMARK 465 ASP B 97
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 136 CG
REMARK 480 HIS A 162 CE1 NE2
REMARK 480 MSE A 260 SE
REMARK 480 SER B 131 CA
REMARK 480 GLN B 136 CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 935 O HOH B 937 1.91
REMARK 500 O HOH B 927 O HOH B 928 1.97
REMARK 500 O HOH A 943 O HOH A 944 2.00
REMARK 500 O HOH B 942 O HOH B 943 2.05
REMARK 500 O HOH B 909 O HOH B 912 2.05
REMARK 500 O HOH A 925 O HOH A 926 2.06
REMARK 500 O HOH A 935 O HOH A 936 2.07
REMARK 500 O HOH A 905 O HOH A 906 2.08
REMARK 500 O HOH B 913 O HOH B 917 2.08
REMARK 500 O HOH A 940 O HOH A 941 2.08
REMARK 500 O HOH A 941 O HOH A 942 2.11
REMARK 500 O HOH A 926 O HOH A 927 2.11
REMARK 500 O HOH A 938 O HOH A 940 2.11
REMARK 500 O HOH A 951 O HOH A 957 2.13
REMARK 500 O HOH B 914 O HOH B 915 2.13
REMARK 500 O HOH B 906 O HOH B 908 2.14
REMARK 500 O HOH A 914 O HOH A 915 2.14
REMARK 500 O HOH A 937 O HOH A 940 2.14
REMARK 500 O HOH A 942 O HOH A 943 2.15
REMARK 500 O HOH A 907 O HOH A 908 2.15
REMARK 500 O HOH B 913 O HOH B 914 2.15
REMARK 500 O HOH A 917 O HOH A 919 2.16
REMARK 500 O HOH A 945 O HOH A 949 2.16
REMARK 500 O HOH B 905 O HOH B 910 2.16
REMARK 500 O HOH A 919 O HOH A 920 2.17
REMARK 500 O HOH A 935 O HOH A 937 2.17
REMARK 500 O HOH A 911 O HOH A 912 2.18
REMARK 500 O HOH A 945 O HOH A 946 2.18
REMARK 500 O HOH B 940 O HOH B 941 2.18
REMARK 500 O HOH A 925 O HOH A 930 2.19
REMARK 500 O HOH B 930 O HOH B 931 2.19
REMARK 500 O HOH A 904 O HOH A 905 2.19
REMARK 500 O HOH B 903 O HOH B 904 2.19
REMARK 500 O HOH B 342 O HOH B 434 2.19
REMARK 500 O HOH B 325 O HOH B 327 2.19
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 O HOH B 907 O HOH B 908 4555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 72 -10.02 66.50
REMARK 500 VAL A 73 -53.42 -25.95
REMARK 500 SER A 83 -150.03 -59.62
REMARK 500 LYS A 167 -58.23 -123.07
REMARK 500 ASN A 177 42.80 -100.84
REMARK 500 ASN A 187 13.29 58.85
REMARK 500 ASP A 192 -150.62 -82.86
REMARK 500 ALA A 202 -71.53 -35.68
REMARK 500 SER A 209 36.60 -87.77
REMARK 500 GLU A 229 11.06 84.33
REMARK 500 SER B 84 -32.47 -38.87
REMARK 500 LYS B 111 65.69 -116.16
REMARK 500 VAL B 186 128.38 -35.53
REMARK 500 ASN B 187 17.81 52.15
REMARK 500 ARG B 237 -41.09 -139.06
REMARK 500 ARG B 251 87.11 42.36
REMARK 500 SER B 253 -5.28 -145.91
REMARK 500 HIS B 269 -55.66 -28.12
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 A 317 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 334 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B 441 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH B 442 DISTANCE = 6.33 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61035.1 RELATED DB: TARGETDB
DBREF 3FLE A 43 288 UNP Q8CRJ5 Q8CRJ5_STAES 43 288
DBREF 3FLE B 43 288 UNP Q8CRJ5 Q8CRJ5_STAES 43 288
SEQADV 3FLE SER A 40 UNP Q8CRJ5 EXPRESSION TAG
SEQADV 3FLE ASN A 41 UNP Q8CRJ5 EXPRESSION TAG
SEQADV 3FLE ALA A 42 UNP Q8CRJ5 EXPRESSION TAG
SEQADV 3FLE SER B 40 UNP Q8CRJ5 EXPRESSION TAG
SEQADV 3FLE ASN B 41 UNP Q8CRJ5 EXPRESSION TAG
SEQADV 3FLE ALA B 42 UNP Q8CRJ5 EXPRESSION TAG
SEQRES 1 A 249 SER ASN ALA ILE LYS THR THR ALA THR LEU PHE LEU HIS
SEQRES 2 A 249 GLY TYR GLY GLY SER GLU ARG SER GLU THR PHE MSE VAL
SEQRES 3 A 249 LYS GLN ALA LEU ASN LYS ASN VAL THR ASN GLU VAL ILE
SEQRES 4 A 249 THR ALA ARG VAL SER SER GLU GLY LYS VAL TYR PHE ASP
SEQRES 5 A 249 LYS LYS LEU SER GLU ASP ALA ALA ASN PRO ILE VAL LYS
SEQRES 6 A 249 VAL GLU PHE LYS ASP ASN LYS ASN GLY ASN PHE LYS GLU
SEQRES 7 A 249 ASN ALA TYR TRP ILE LYS GLU VAL LEU SER GLN LEU LYS
SEQRES 8 A 249 SER GLN PHE GLY ILE GLN GLN PHE ASN PHE VAL GLY HIS
SEQRES 9 A 249 SER MSE GLY ASN MSE SER PHE ALA PHE TYR MSE LYS ASN
SEQRES 10 A 249 TYR GLY ASP ASP ARG HIS LEU PRO GLN LEU LYS LYS GLU
SEQRES 11 A 249 VAL ASN ILE ALA GLY VAL TYR ASN GLY ILE LEU ASN MSE
SEQRES 12 A 249 ASN GLU ASN VAL ASN GLU ILE ILE VAL ASP LYS GLN GLY
SEQRES 13 A 249 LYS PRO SER ARG MSE ASN ALA ALA TYR ARG GLN LEU LEU
SEQRES 14 A 249 SER LEU TYR LYS ILE TYR CYS GLY LYS GLU ILE GLU VAL
SEQRES 15 A 249 LEU ASN ILE TYR GLY ASP LEU GLU ASP GLY SER HIS SER
SEQRES 16 A 249 ASP GLY ARG VAL SER ASN SER SER SER GLN SER LEU GLN
SEQRES 17 A 249 TYR LEU LEU ARG GLY SER THR LYS SER TYR GLN GLU MSE
SEQRES 18 A 249 LYS PHE LYS GLY ALA LYS ALA GLN HIS SER GLN LEU HIS
SEQRES 19 A 249 GLU ASN LYS ASP VAL ALA ASN GLU ILE ILE GLN PHE LEU
SEQRES 20 A 249 TRP GLU
SEQRES 1 B 249 SER ASN ALA ILE LYS THR THR ALA THR LEU PHE LEU HIS
SEQRES 2 B 249 GLY TYR GLY GLY SER GLU ARG SER GLU THR PHE MSE VAL
SEQRES 3 B 249 LYS GLN ALA LEU ASN LYS ASN VAL THR ASN GLU VAL ILE
SEQRES 4 B 249 THR ALA ARG VAL SER SER GLU GLY LYS VAL TYR PHE ASP
SEQRES 5 B 249 LYS LYS LEU SER GLU ASP ALA ALA ASN PRO ILE VAL LYS
SEQRES 6 B 249 VAL GLU PHE LYS ASP ASN LYS ASN GLY ASN PHE LYS GLU
SEQRES 7 B 249 ASN ALA TYR TRP ILE LYS GLU VAL LEU SER GLN LEU LYS
SEQRES 8 B 249 SER GLN PHE GLY ILE GLN GLN PHE ASN PHE VAL GLY HIS
SEQRES 9 B 249 SER MSE GLY ASN MSE SER PHE ALA PHE TYR MSE LYS ASN
SEQRES 10 B 249 TYR GLY ASP ASP ARG HIS LEU PRO GLN LEU LYS LYS GLU
SEQRES 11 B 249 VAL ASN ILE ALA GLY VAL TYR ASN GLY ILE LEU ASN MSE
SEQRES 12 B 249 ASN GLU ASN VAL ASN GLU ILE ILE VAL ASP LYS GLN GLY
SEQRES 13 B 249 LYS PRO SER ARG MSE ASN ALA ALA TYR ARG GLN LEU LEU
SEQRES 14 B 249 SER LEU TYR LYS ILE TYR CYS GLY LYS GLU ILE GLU VAL
SEQRES 15 B 249 LEU ASN ILE TYR GLY ASP LEU GLU ASP GLY SER HIS SER
SEQRES 16 B 249 ASP GLY ARG VAL SER ASN SER SER SER GLN SER LEU GLN
SEQRES 17 B 249 TYR LEU LEU ARG GLY SER THR LYS SER TYR GLN GLU MSE
SEQRES 18 B 249 LYS PHE LYS GLY ALA LYS ALA GLN HIS SER GLN LEU HIS
SEQRES 19 B 249 GLU ASN LYS ASP VAL ALA ASN GLU ILE ILE GLN PHE LEU
SEQRES 20 B 249 TRP GLU
MODRES 3FLE MSE A 64 MET SELENOMETHIONINE
MODRES 3FLE MSE A 145 MET SELENOMETHIONINE
MODRES 3FLE MSE A 148 MET SELENOMETHIONINE
MODRES 3FLE MSE A 154 MET SELENOMETHIONINE
MODRES 3FLE MSE A 182 MET SELENOMETHIONINE
MODRES 3FLE MSE A 200 MET SELENOMETHIONINE
MODRES 3FLE MSE A 260 MET SELENOMETHIONINE
MODRES 3FLE MSE B 64 MET SELENOMETHIONINE
MODRES 3FLE MSE B 145 MET SELENOMETHIONINE
MODRES 3FLE MSE B 148 MET SELENOMETHIONINE
MODRES 3FLE MSE B 154 MET SELENOMETHIONINE
MODRES 3FLE MSE B 182 MET SELENOMETHIONINE
MODRES 3FLE MSE B 200 MET SELENOMETHIONINE
MODRES 3FLE MSE B 260 MET SELENOMETHIONINE
HET MSE A 64 8
HET MSE A 145 8
HET MSE A 148 8
HET MSE A 154 8
HET MSE A 182 8
HET MSE A 200 8
HET MSE A 260 8
HET MSE B 64 8
HET MSE B 145 8
HET MSE B 148 8
HET MSE B 154 8
HET MSE B 182 8
HET MSE B 200 8
HET MSE B 260 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 HOH *448(H2 O)
HELIX 1 1 SER A 57 SER A 60 5 4
HELIX 2 2 GLU A 61 ASN A 70 1 10
HELIX 3 3 ASN A 114 GLN A 132 1 19
HELIX 4 4 ASN A 147 GLY A 158 1 12
HELIX 5 5 ASN A 201 LEU A 207 1 7
HELIX 6 6 LEU A 210 CYS A 215 1 6
HELIX 7 7 SER A 239 SER A 245 1 7
HELIX 8 8 SER A 245 LEU A 250 1 6
HELIX 9 9 ALA A 265 GLN A 268 5 4
HELIX 10 10 HIS A 269 GLU A 274 5 6
HELIX 11 11 ASN A 275 TRP A 287 1 13
HELIX 12 12 SER B 57 SER B 60 5 4
HELIX 13 13 GLU B 61 LYS B 71 1 11
HELIX 14 14 ASN B 114 GLY B 134 1 21
HELIX 15 15 MSE B 145 GLY B 158 1 14
HELIX 16 16 ASN B 201 GLN B 206 1 6
HELIX 17 17 LEU B 207 LEU B 208 5 2
HELIX 18 18 SER B 209 TYR B 214 5 6
HELIX 19 19 SER B 239 SER B 245 1 7
HELIX 20 20 SER B 245 ARG B 251 1 7
HELIX 21 21 ALA B 265 GLN B 268 5 4
HELIX 22 22 SER B 270 GLU B 274 5 5
HELIX 23 23 ASN B 275 GLU B 288 1 14
SHEET 1 A 8 VAL A 88 PHE A 90 0
SHEET 2 A 8 VAL A 77 VAL A 82 -1 N ARG A 81 O TYR A 89
SHEET 3 A 8 ILE A 102 PHE A 107 1 O LYS A 104 N ALA A 80
SHEET 4 A 8 THR A 46 LEU A 51 1 N PHE A 50 O VAL A 103
SHEET 5 A 8 GLN A 137 HIS A 143 1 O VAL A 141 N LEU A 51
SHEET 6 A 8 GLN A 165 ILE A 172 1 O VAL A 170 N PHE A 140
SHEET 7 A 8 GLU A 220 ASP A 227 1 O LEU A 222 N GLU A 169
SHEET 8 A 8 SER A 256 LYS A 263 1 O MSE A 260 N ASN A 223
SHEET 1 B 8 VAL B 88 PHE B 90 0
SHEET 2 B 8 VAL B 77 VAL B 82 -1 N ARG B 81 O TYR B 89
SHEET 3 B 8 ILE B 102 PHE B 107 1 O LYS B 104 N ILE B 78
SHEET 4 B 8 THR B 46 LEU B 51 1 N THR B 48 O VAL B 103
SHEET 5 B 8 GLN B 137 HIS B 143 1 O VAL B 141 N LEU B 49
SHEET 6 B 8 GLN B 165 ILE B 172 1 O VAL B 170 N PHE B 140
SHEET 7 B 8 GLU B 220 ASP B 227 1 O ILE B 224 N ASN B 171
SHEET 8 B 8 SER B 256 LYS B 263 1 O PHE B 262 N TYR B 225
LINK C PHE A 63 N MSE A 64 1555 1555 1.33
LINK C MSE A 64 N VAL A 65 1555 1555 1.33
LINK C SER A 144 N MSE A 145 1555 1555 1.33
LINK C MSE A 145 N GLY A 146 1555 1555 1.33
LINK C ASN A 147 N MSE A 148 1555 1555 1.33
LINK C MSE A 148 N SER A 149 1555 1555 1.33
LINK C TYR A 153 N MSE A 154 1555 1555 1.32
LINK C MSE A 154 N LYS A 155 1555 1555 1.33
LINK C ASN A 181 N MSE A 182 1555 1555 1.33
LINK C MSE A 182 N ASN A 183 1555 1555 1.34
LINK C ARG A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N ASN A 201 1555 1555 1.33
LINK C GLU A 259 N MSE A 260 1555 1555 1.33
LINK C MSE A 260 N LYS A 261 1555 1555 1.33
LINK C PHE B 63 N MSE B 64 1555 1555 1.33
LINK C MSE B 64 N VAL B 65 1555 1555 1.33
LINK C SER B 144 N MSE B 145 1555 1555 1.34
LINK C MSE B 145 N GLY B 146 1555 1555 1.33
LINK C ASN B 147 N MSE B 148 1555 1555 1.33
LINK C MSE B 148 N SER B 149 1555 1555 1.33
LINK C TYR B 153 N MSE B 154 1555 1555 1.32
LINK C MSE B 154 N LYS B 155 1555 1555 1.33
LINK C ASN B 181 N MSE B 182 1555 1555 1.34
LINK C MSE B 182 N ASN B 183 1555 1555 1.33
LINK C ARG B 199 N MSE B 200 1555 1555 1.33
LINK C MSE B 200 N ASN B 201 1555 1555 1.33
LINK C GLU B 259 N MSE B 260 1555 1555 1.33
LINK C MSE B 260 N LYS B 261 1555 1555 1.33
CRYST1 92.722 41.458 153.996 90.00 90.06 90.00 C 1 2 1 8
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 0.010785 0.000000 0.000012 0.00000
SCALE2 0.000000 0.024121 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006494 0.00000
TER 1949 GLU A 288
TER 3898 GLU B 288
MASTER 370 0 14 23 16 0 0 6 4344 2 140 40
END |