| content |
HEADER HYDROLASE 26-MAY-24 9C0N
TITLE FPHI, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES I, APO FORM AT ROOM TEMPERATURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBOXYLESTERASE,ESTERASE/LIPASE FAMILY PROTEIN;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-CA-263;
SOURCE 3 ORGANISM_TAXID: 1385529;
SOURCE 4 GENE: EST_2, EST_1, BN1321_100022, C7M54_03125, DD547_00417,
SOURCE 5 EP54_01625, EQ90_13375, FAF17_11905, GO814_02325, GO941_12735,
SOURCE 6 GO942_04080, GQX37_00145, HMPREF3211_01442, NCTC10702_00834,
SOURCE 7 NCTC13131_05910, SAMEA2078260_02464, SAMEA2078588_01365,
SOURCE 8 SAMEA2080344_01425, SAMEA2081063_02567, SAMEA4008575_01596,
SOURCE 9 SAMEA70146418_02725;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FPHI, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, ROOM TEMPERATURE, HUMIDITY, HUMIDIFIER,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,G.T.RANDALL
REVDAT 1 08-JAN-25 9C0N 0
JRNL AUTH M.FELLNER,G.RANDALL,I.R.C.G.BITAC,A.K.WARRENDER,A.SETHI,
JRNL AUTH 2 R.JELINEK,I.KASS
JRNL TITL SIMILAR BUT DISTINCT-BIOCHEMICAL CHARACTERIZATION OF THE
JRNL TITL 2 STAPHYLOCOCCUS AUREUS SERINE HYDROLASES FPHH AND FPHI.
JRNL REF PROTEINS 2024
JRNL REFN ESSN 1097-0134
JRNL PMID 39726198
JRNL DOI 10.1002/PROT.26785
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 28197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1395
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 40.0600 - 3.6600 0.99 2833 152 0.1317 0.1385
REMARK 3 2 3.6600 - 2.9100 0.99 2714 126 0.1396 0.1779
REMARK 3 3 2.9100 - 2.5400 1.00 2697 148 0.1498 0.1772
REMARK 3 4 2.5400 - 2.3100 1.00 2700 124 0.1446 0.1798
REMARK 3 5 2.3100 - 2.1400 1.00 2647 155 0.1554 0.1707
REMARK 3 6 2.1400 - 2.0200 0.99 2677 137 0.1523 0.1803
REMARK 3 7 2.0200 - 1.9100 1.00 2640 154 0.1655 0.1791
REMARK 3 8 1.9100 - 1.8300 1.00 2637 140 0.2228 0.2088
REMARK 3 9 1.8300 - 1.7600 1.00 2614 133 0.2340 0.2916
REMARK 3 10 1.7600 - 1.7000 0.99 2643 126 0.2607 0.3109
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.210
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) : 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 : 0.010 2092
REMARK 3 ANGLE : 1.044 2852
REMARK 3 CHIRALITY : 0.061 306
REMARK 3 PLANARITY : 0.009 380
REMARK 3 DIHEDRAL : 5.306 288
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9558 11.1057 21.1209
REMARK 3 T TENSOR
REMARK 3 T11: 0.2225 T22: 0.1839
REMARK 3 T33: 0.2375 T12: -0.0130
REMARK 3 T13: 0.0070 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 3.6286 L22: 2.5597
REMARK 3 L33: 2.2126 L12: -1.4810
REMARK 3 L13: -0.0104 L23: -0.0652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0645 S12: -0.1672 S13: 0.3202
REMARK 3 S21: 0.1201 S22: 0.0051 S23: -0.0468
REMARK 3 S31: -0.2301 S32: 0.0156 S33: 0.0482
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9491 0.6174 21.9708
REMARK 3 T TENSOR
REMARK 3 T11: 0.2252 T22: 0.1997
REMARK 3 T33: 0.2297 T12: -0.0194
REMARK 3 T13: 0.0248 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 1.2333 L22: 1.6162
REMARK 3 L33: 2.3992 L12: -0.1694
REMARK 3 L13: 0.6666 L23: 0.3442
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: -0.0255 S13: -0.1461
REMARK 3 S21: 0.1731 S22: 0.0202 S23: 0.0803
REMARK 3 S31: 0.0856 S32: 0.1031 S33: -0.0030
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9415 12.1226 22.1709
REMARK 3 T TENSOR
REMARK 3 T11: 0.4902 T22: 0.9389
REMARK 3 T33: 0.5109 T12: -0.2313
REMARK 3 T13: 0.0286 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 5.3966 L22: 2.8095
REMARK 3 L33: 5.3617 L12: 0.0803
REMARK 3 L13: 0.6714 L23: 1.5657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0720 S12: 0.0551 S13: 0.8532
REMARK 3 S21: -0.5167 S22: -0.0420 S23: -0.1740
REMARK 3 S31: -0.8273 S32: 1.2090 S33: 0.0981
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9638 -2.2400 22.0545
REMARK 3 T TENSOR
REMARK 3 T11: 0.2720 T22: 0.5464
REMARK 3 T33: 0.3563 T12: 0.0188
REMARK 3 T13: -0.0533 T23: -0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 3.0372 L22: 4.5795
REMARK 3 L33: 3.2555 L12: 1.8817
REMARK 3 L13: 0.6153 L23: 0.7303
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.2260 S13: -0.0940
REMARK 3 S21: 0.5432 S22: 0.1014 S23: -0.6044
REMARK 3 S31: 0.0692 S32: 1.0777 S33: -0.1446
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6856 2.2366 4.4710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3141 T22: 0.2848
REMARK 3 T33: 0.2055 T12: -0.0091
REMARK 3 T13: 0.0302 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.8181 L22: 3.5388
REMARK 3 L33: 2.7688 L12: -0.2871
REMARK 3 L13: -0.7960 L23: 0.0832
REMARK 3 S TENSOR
REMARK 3 S11: 0.1655 S12: 0.1453 S13: 0.2049
REMARK 3 S21: -0.4065 S22: -0.1079 S23: -0.2219
REMARK 3 S31: -0.3553 S32: 0.2988 S33: -0.0508
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 244 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5266 9.8506 6.9641
REMARK 3 T TENSOR
REMARK 3 T11: 0.3433 T22: 0.2639
REMARK 3 T33: 0.3418 T12: 0.0415
REMARK 3 T13: -0.0219 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 3.7250 L22: 3.8234
REMARK 3 L33: 6.6252 L12: 3.6932
REMARK 3 L13: -0.6549 L23: -0.2864
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: 0.3177 S13: 0.6118
REMARK 3 S21: -0.6641 S22: 0.0752 S23: 0.6886
REMARK 3 S31: -0.6401 S32: -0.3677 S33: -0.0606
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 9C0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1000284492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28252
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 48.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 1.12700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL 10 MG/ML FPHI (10 MM HEPES PH
REMARK 280 7.5, 100 MM NACL) WERE MIXED WITH 0.2 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 200MM CALCIUM CHLORIDE
REMARK 280 HEXAHYDRATE, 100MM HEPES PH 7.0, 20 % W/V PEG 6000., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.32800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.58850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.86800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.58850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.32800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.86800
REMARK 290 SMTRY3 4 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: 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 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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
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 A 405 O HOH A 496 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 SER A 94 -120.09 61.36
REMARK 500 SER A 94 -120.09 56.35
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 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 38 OE1
REMARK 620 2 GLU A 38 OE2 51.2
REMARK 620 3 GLU A 74 OE2 24.3 31.0
REMARK 620 4 HOH A 409 O 142.8 162.1 155.2
REMARK 620 5 HOH A 416 O 64.0 113.0 88.1 84.4
REMARK 620 6 HOH A 477 O 90.5 85.3 77.3 83.8 112.3
REMARK 620 7 HOH A 512 O 85.7 93.7 99.7 98.2 64.4 175.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 40 OD1
REMARK 620 2 ASP A 41 OD1 113.8
REMARK 620 3 ASP A 171 OD1 31.7 100.4
REMARK 620 4 ASP A 171 OD2 32.3 100.8 1.1
REMARK 620 5 HOH A 449 O 85.1 161.0 96.7 96.0
REMARK 620 6 HOH A 464 O 140.1 89.0 115.7 114.8 76.0
REMARK 620 7 HOH A 479 O 80.2 82.4 48.8 48.1 103.0 70.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 68 OD1
REMARK 620 2 GLU A 196 OE1 41.4
REMARK 620 3 GLU A 196 OE2 44.6 3.3
REMARK 620 4 HOH A 402 O 42.2 3.1 4.2
REMARK 620 5 HOH A 405 O 44.5 4.5 3.0 6.8
REMARK 620 6 HOH A 447 O 39.1 2.3 5.6 4.4 6.2
REMARK 620 7 HOH A 496 O 42.5 2.9 3.3 5.8 2.1 4.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 O
REMARK 620 2 GLU A 161 OE1 88.1
REMARK 620 3 GLU A 161 OE2 124.1 53.1
REMARK 620 4 HOH A 501 O 132.4 127.3 74.6
REMARK 620 5 HOH A 506 O 70.8 80.4 126.9 137.3
REMARK 620 N 1 2 3 4
DBREF 9C0N A 1 244 UNP X5DUZ9 X5DUZ9_STAAU 1 244
SEQADV 9C0N GLY A -2 UNP X5DUZ9 EXPRESSION TAG
SEQADV 9C0N PRO A -1 UNP X5DUZ9 EXPRESSION TAG
SEQADV 9C0N GLY A 0 UNP X5DUZ9 EXPRESSION TAG
SEQRES 1 A 247 GLY PRO GLY MET ARG ILE LYS THR PRO SER PRO SER TYR
SEQRES 2 A 247 LEU LYS GLY THR ASN GLY HIS ALA ILE LEU LEU LEU HIS
SEQRES 3 A 247 SER PHE THR GLY THR ASN ARG ASP VAL LYS HIS LEU ALA
SEQRES 4 A 247 ALA GLU LEU ASN ASP GLN GLY PHE SER CYS TYR ALA PRO
SEQRES 5 A 247 ASN TYR PRO GLY HIS GLY LEU LEU LEU LYS ASP PHE MET
SEQRES 6 A 247 THR TYR ASN VAL ASP ASP TRP TRP GLU GLU VAL GLU LYS
SEQRES 7 A 247 ALA TYR GLN PHE LEU VAL ASN GLU GLY TYR GLU SER ILE
SEQRES 8 A 247 SER ALA THR GLY VAL SER LEU GLY GLY LEU MET THR LEU
SEQRES 9 A 247 LYS LEU ALA GLN HIS TYR PRO LEU LYS ARG ILE ALA VAL
SEQRES 10 A 247 MET SER ALA PRO LYS GLU LYS SER ASP ASP GLY LEU ILE
SEQRES 11 A 247 GLU HIS LEU VAL TYR TYR SER GLN ARG MET SER ASN ILE
SEQRES 12 A 247 LEU ASN LEU ASP GLN GLN ALA SER SER ALA GLN LEU ALA
SEQRES 13 A 247 ALA ILE ASP ASP TYR GLU GLY GLU ILE THR LYS PHE GLN
SEQRES 14 A 247 HIS PHE ILE ASP ASP ILE MET THR ASN LEU ASN VAL ILE
SEQRES 15 A 247 LYS MET PRO ALA ASN ILE LEU PHE GLY GLY LYS ASP ALA
SEQRES 16 A 247 PRO SER TYR GLU THR SER ALA HIS PHE ILE TYR GLU HIS
SEQRES 17 A 247 LEU GLY SER VAL ASP LYS GLU LEU ASN GLY LEU LYS ASP
SEQRES 18 A 247 SER HIS HIS LEU MET THR HIS GLY GLU GLY ARG ASP ILE
SEQRES 19 A 247 LEU GLU GLU ASN VAL ILE ARG PHE PHE ASN ALA LEU THR
HET CA A 301 1
HET CA A 302 1
HET CA A 303 1
HET CA A 304 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 4(CA 2+)
FORMUL 6 HOH *119(H2 O)
HELIX 1 AA1 THR A 28 ASP A 31 5 4
HELIX 2 AA2 VAL A 32 GLN A 42 1 11
HELIX 3 AA3 LEU A 57 MET A 62 1 6
HELIX 4 AA4 ASN A 65 GLY A 84 1 20
HELIX 5 AA5 SER A 94 TYR A 107 1 14
HELIX 6 AA6 SER A 122 LEU A 141 1 20
HELIX 7 AA7 ASP A 144 ALA A 154 1 11
HELIX 8 AA8 ILE A 155 ASP A 157 5 3
HELIX 9 AA9 TYR A 158 ASN A 175 1 18
HELIX 10 AB1 LEU A 176 ILE A 179 5 4
HELIX 11 AB2 ALA A 192 LEU A 206 1 15
HELIX 12 AB3 GLY A 228 ASN A 241 1 14
HELIX 13 AB4 ALA A 242 THR A 244 5 3
SHEET 1 AA1 7 SER A 9 LEU A 11 0
SHEET 2 AA1 7 SER A 45 ALA A 48 -1 O CYS A 46 N LEU A 11
SHEET 3 AA1 7 HIS A 17 LEU A 22 1 N ILE A 19 O SER A 45
SHEET 4 AA1 7 SER A 87 VAL A 93 1 O THR A 91 N LEU A 20
SHEET 5 AA1 7 ILE A 112 MET A 115 1 O MET A 115 N GLY A 92
SHEET 6 AA1 7 ALA A 183 GLY A 188 1 O LEU A 186 N VAL A 114
SHEET 7 AA1 7 LYS A 211 LEU A 216 1 O ASN A 214 N ILE A 185
LINK OE1 GLU A 38 CA CA A 302 1555 1555 2.56
LINK OE2 GLU A 38 CA CA A 302 1555 1555 2.47
LINK OD1 ASN A 40 CA CA A 301 1555 1555 2.38
LINK OD1 ASP A 41 CA CA A 301 1555 1555 2.50
LINK OD1 ASP A 68 CA CA A 303 1555 2555 2.44
LINK OE2 GLU A 74 CA CA A 302 1555 3545 2.64
LINK O ASP A 157 CA CA A 304 1555 1555 2.62
LINK OE1AGLU A 161 CA CA A 304 1555 1555 2.33
LINK OE2AGLU A 161 CA CA A 304 1555 1555 2.53
LINK OD1BASP A 171 CA CA A 301 1555 3545 2.73
LINK OD2BASP A 171 CA CA A 301 1555 3545 2.50
LINK OE1 GLU A 196 CA CA A 303 1555 1555 2.61
LINK OE2 GLU A 196 CA CA A 303 1555 1555 2.48
LINK CA CA A 301 O HOH A 449 1555 3555 2.40
LINK CA CA A 301 O HOH A 464 1555 3555 2.51
LINK CA CA A 301 O HOH A 479 1555 1555 2.22
LINK CA CA A 302 O HOH A 409 1555 3555 2.42
LINK CA CA A 302 O HOH A 416 1555 1555 2.40
LINK CA CA A 302 O HOH A 477 1555 1555 2.47
LINK CA CA A 302 O HOH A 512 1555 1555 2.22
LINK CA CA A 303 O HOH A 402 1555 2554 2.45
LINK CA CA A 303 O HOH A 405 1555 2554 2.42
LINK CA CA A 303 O HOH A 447 1555 1555 2.33
LINK CA CA A 303 O HOH A 496 1555 2554 2.47
LINK CA CA A 304 O HOH A 501 1555 1555 2.57
LINK CA CA A 304 O HOH A 506 1555 1555 2.76
CRYST1 52.656 61.736 77.177 90.00 90.00 90.00 P 21 21 21 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 0.018991 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016198 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012957 0.00000
TER 4021 THR A 244
MASTER 380 0 4 13 7 0 0 6 2038 1 22 19
END |