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HEADER HYDROLASE 26-MAY-24 9C0L
TITLE FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES H, APO CRYSTAL FORM 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 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;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS FPHH, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 08-JAN-25 9C0L 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. 1.79 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) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 29956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1491
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 41.6600 - 3.9800 1.00 2823 156 0.1673 0.1941
REMARK 3 2 3.9800 - 3.1600 1.00 2657 144 0.1821 0.2030
REMARK 3 3 3.1600 - 2.7600 1.00 2639 122 0.1909 0.2197
REMARK 3 4 2.7600 - 2.5100 1.00 2592 140 0.1824 0.2391
REMARK 3 5 2.5100 - 2.3300 1.00 2583 127 0.1790 0.2090
REMARK 3 6 2.3300 - 2.1900 1.00 2558 138 0.1631 0.1935
REMARK 3 7 2.1900 - 2.0800 1.00 2570 138 0.1909 0.2341
REMARK 3 8 2.0800 - 1.9900 1.00 2544 142 0.2003 0.2480
REMARK 3 9 1.9900 - 1.9100 1.00 2542 121 0.2145 0.2540
REMARK 3 10 1.9100 - 1.8500 1.00 2529 142 0.2538 0.3035
REMARK 3 11 1.8500 - 1.7900 0.96 2428 121 0.3329 0.3436
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.270
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 : 0.007 2014
REMARK 3 ANGLE : 0.888 2725
REMARK 3 CHIRALITY : 0.059 285
REMARK 3 PLANARITY : 0.006 360
REMARK 3 DIHEDRAL : 5.437 263
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2626 -8.4004 19.2869
REMARK 3 T TENSOR
REMARK 3 T11: 0.2501 T22: 0.2434
REMARK 3 T33: 0.2215 T12: -0.0260
REMARK 3 T13: 0.0120 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 3.2233 L22: 1.7468
REMARK 3 L33: 2.6253 L12: -0.5638
REMARK 3 L13: -0.1242 L23: 0.1066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: 0.2809 S13: 0.1837
REMARK 3 S21: -0.2002 S22: -0.0072 S23: -0.0251
REMARK 3 S31: -0.2330 S32: 0.0124 S33: -0.0540
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8449 10.4303 14.1654
REMARK 3 T TENSOR
REMARK 3 T11: 0.6460 T22: 0.3664
REMARK 3 T33: 0.5860 T12: 0.0147
REMARK 3 T13: 0.0604 T23: 0.1047
REMARK 3 L TENSOR
REMARK 3 L11: 2.8899 L22: 2.4477
REMARK 3 L33: 2.4698 L12: 0.8296
REMARK 3 L13: -0.9983 L23: -0.7638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0665 S12: 0.3512 S13: 0.8349
REMARK 3 S21: -0.3800 S22: 0.0858 S23: -0.1720
REMARK 3 S31: -0.6591 S32: 0.0156 S33: -0.1328
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2412 -5.5352 34.5591
REMARK 3 T TENSOR
REMARK 3 T11: 0.2851 T22: 0.2911
REMARK 3 T33: 0.2231 T12: -0.0744
REMARK 3 T13: 0.0075 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 3.4138 L22: 1.7475
REMARK 3 L33: 2.7832 L12: -1.4192
REMARK 3 L13: -0.6997 L23: -0.4930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: -0.2845 S13: 0.2359
REMARK 3 S21: 0.0286 S22: 0.0395 S23: -0.1209
REMARK 3 S31: -0.3277 S32: 0.2222 S33: -0.0876
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 9C0L 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_1000284405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
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 : 30069
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 48.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 19.20
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 18.60
REMARK 200 R MERGE FOR SHELL (I) : 2.56500
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 (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 UL 9.1 MG/ML FPHH (10MM HEPES PH
REMARK 280 7.6, 100MM NACL) WERE MIXED WITH 0.15 UL OF RESERVOIR SOLUTION.
REMARK 280 SITTING DROP RESERVOIR CONTAINED 200MM CALCIUM ACETATE HYDRATE,
REMARK 280 100MM TRIS PH 8.5, 25 % W/V PEG 2000 MME. CRYSTAL WAS FROZEN IN
REMARK 280 A SOLUTION OF ~25% ETHYLENGLYCOL, 75% RESERVOIR., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 82.25650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.44900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.44900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 123.38475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.44900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.44900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.12825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.44900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.44900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 123.38475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.44900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.44900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.12825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.25650
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 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 A 466 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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 ILE A 3
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 402 O HOH A 529 2.17
REMARK 500 O HOH A 401 O HOH A 436 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 GLU A 13 -107.49 -128.66
REMARK 500 SER A 63 -155.60 -108.78
REMARK 500 SER A 93 -126.22 62.74
REMARK 500 ASN A 189 47.08 -103.27
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 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 82 OE1
REMARK 620 2 HOH A 405 O 96.2
REMARK 620 3 HOH A 440 O 84.9 79.2
REMARK 620 4 HOH A 514 O 81.9 60.9 136.0
REMARK 620 5 HOH A 516 O 84.5 152.3 73.2 145.7
REMARK 620 6 HOH A 523 O 96.8 135.1 144.6 78.8 71.8
REMARK 620 7 HOH A 533 O 171.0 82.9 86.2 105.2 92.2 90.0
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 GLU A 173 O
REMARK 620 2 ASP A 176 OD1 91.0
REMARK 620 3 ASP A 176 OD2 114.0 51.5
REMARK 620 4 HOH A 428 O 117.5 98.5 119.9
REMARK 620 5 HOH A 502 O 78.1 168.9 131.3 88.7
REMARK 620 N 1 2 3 4
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 ASP A 206 OD1
REMARK 620 2 HOH A 406 O 146.5
REMARK 620 3 HOH A 410 O 75.3 74.7
REMARK 620 4 HOH A 412 O 136.5 76.9 138.1
REMARK 620 5 HOH A 463 O 93.7 97.9 84.6 69.5
REMARK 620 6 HOH A 486 O 71.5 137.8 146.7 70.6 95.2
REMARK 620 7 HOH A 520 O 84.4 92.9 111.2 100.2 162.8 67.9
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 ASP A 209 OD1
REMARK 620 2 ASN A 211 OD1 131.0
REMARK 620 3 HOH A 418 O 87.2 58.4
REMARK 620 4 HOH A 420 O 137.7 58.4 116.8
REMARK 620 5 HOH A 420 O 80.4 123.4 163.3 67.7
REMARK 620 6 HOH A 421 O 80.1 136.5 102.3 122.9 86.6
REMARK 620 7 HOH A 466 O 70.6 77.2 93.2 73.5 72.2 146.1
REMARK 620 8 HOH A 466 O 70.7 77.2 93.4 73.4 72.0 146.0 0.2
REMARK 620 9 HOH A 511 O 151.1 71.7 93.9 66.3 102.4 71.5 137.9 137.8
REMARK 620 N 1 2 3 4 5 6 7 8
DBREF1 9C0L A 1 246 UNP A0A0D6HZA6_STAAU
DBREF2 9C0L A A0A0D6HZA6 1 246
SEQADV 9C0L GLY A -2 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 9C0L PRO A -1 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 9C0L GLY A 0 UNP A0A0D6HZA EXPRESSION TAG
SEQRES 1 A 249 GLY PRO GLY MET GLN ILE LYS LEU PRO LYS PRO PHE PHE
SEQRES 2 A 249 PHE GLU GLU GLY LYS ARG ALA VAL LEU LEU LEU HIS GLY
SEQRES 3 A 249 PHE THR GLY ASN SER SER ASP VAL ARG GLN LEU GLY ARG
SEQRES 4 A 249 PHE LEU GLN LYS LYS GLY TYR THR SER TYR ALA PRO GLN
SEQRES 5 A 249 TYR GLU GLY HIS ALA ALA PRO PRO ASP GLU ILE LEU LYS
SEQRES 6 A 249 SER SER PRO PHE VAL TRP PHE LYS ASP ALA LEU ASP GLY
SEQRES 7 A 249 TYR ASP TYR LEU VAL GLU GLN GLY TYR ASP GLU ILE VAL
SEQRES 8 A 249 VAL ALA GLY LEU SER LEU GLY GLY ASP PHE ALA LEU LYS
SEQRES 9 A 249 LEU SER LEU ASN ARG ASP VAL LYS GLY ILE VAL THR MET
SEQRES 10 A 249 CYS ALA PRO MET GLY GLY LYS THR GLU GLY ALA ILE TYR
SEQRES 11 A 249 GLU GLY PHE LEU GLU TYR ALA ARG ASN PHE LYS LYS TYR
SEQRES 12 A 249 GLU GLY LYS ASP GLN GLU THR ILE ASP ASN GLU MET ASP
SEQRES 13 A 249 HIS PHE LYS PRO THR GLU THR LEU LYS GLU LEU SER GLU
SEQRES 14 A 249 ALA LEU ASP THR ILE LYS GLU GLN VAL ASP GLU VAL LEU
SEQRES 15 A 249 ASP PRO ILE LEU VAL ILE GLN ALA GLU ASN ASP ASN MET
SEQRES 16 A 249 ILE ASP PRO GLN SER ALA ASN TYR ILE TYR ASP HIS VAL
SEQRES 17 A 249 ASP SER ASP ASP LYS ASN ILE LYS TRP TYR SER GLU SER
SEQRES 18 A 249 GLY HIS VAL ILE THR ILE ASP LYS GLU LYS GLU GLN VAL
SEQRES 19 A 249 PHE GLU ASP ILE TYR GLN PHE LEU GLU SER LEU ASP TRP
SEQRES 20 A 249 SER GLU
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 *145(H2 O)
HELIX 1 AA1 ASN A 27 ASP A 30 5 4
HELIX 2 AA2 VAL A 31 LYS A 41 1 11
HELIX 3 AA3 PRO A 57 LYS A 62 1 6
HELIX 4 AA4 SER A 64 GLN A 82 1 19
HELIX 5 AA5 SER A 93 LEU A 104 1 12
HELIX 6 AA6 GLY A 124 GLU A 141 1 18
HELIX 7 AA7 ASP A 144 HIS A 154 1 11
HELIX 8 AA8 PRO A 157 VAL A 175 1 19
HELIX 9 AA9 ASP A 176 VAL A 178 5 3
HELIX 10 AB1 GLN A 196 VAL A 205 1 10
HELIX 11 AB2 GLU A 227 SER A 241 1 15
SHEET 1 AA1 7 PHE A 9 PHE A 11 0
SHEET 2 AA1 7 THR A 44 ALA A 47 -1 O ALA A 47 N PHE A 9
SHEET 3 AA1 7 ALA A 17 LEU A 21 1 N LEU A 20 O TYR A 46
SHEET 4 AA1 7 ILE A 87 LEU A 92 1 O ALA A 90 N LEU A 19
SHEET 5 AA1 7 GLY A 110 MET A 114 1 O VAL A 112 N GLY A 91
SHEET 6 AA1 7 ILE A 182 ALA A 187 1 O ILE A 185 N THR A 113
SHEET 7 AA1 7 LYS A 210 TYR A 215 1 O ASN A 211 N VAL A 184
LINK OE1 GLN A 82 CA CA A 303 1555 1555 2.25
LINK O GLU A 173 CA CA A 304 1555 1555 2.41
LINK OD1 ASP A 176 CA CA A 304 1555 1555 2.42
LINK OD2 ASP A 176 CA CA A 304 1555 1555 2.58
LINK OD1 ASP A 206 CA CA A 302 1555 1555 2.56
LINK OD1 ASP A 209 CA CA A 301 1555 1555 2.41
LINK OD1BASN A 211 CA CA A 301 1555 1555 2.90
LINK CA CA A 301 O HOH A 418 1555 1555 2.31
LINK CA CA A 301 O HOH A 420 1555 1555 2.35
LINK CA CA A 301 O HOH A 420 1555 8555 2.42
LINK CA CA A 301 O HOH A 421 1555 1555 2.25
LINK CA CA A 301 O HOH A 466 1555 1555 2.43
LINK CA CA A 301 O HOH A 466 1555 8555 2.44
LINK CA CA A 301 O HOH A 511 1555 1555 2.28
LINK CA CA A 302 O HOH A 406 1555 8555 2.34
LINK CA CA A 302 O HOH A 410 1555 1555 2.30
LINK CA CA A 302 O HOH A 412 1555 8555 2.28
LINK CA CA A 302 O HOH A 463 1555 8555 2.36
LINK CA CA A 302 O HOH A 486 1555 1555 2.31
LINK CA CA A 302 O HOH A 520 1555 1555 2.26
LINK CA CA A 303 O HOH A 405 1555 1555 2.46
LINK CA CA A 303 O HOH A 440 1555 1555 2.38
LINK CA CA A 303 O HOH A 514 1555 1555 2.50
LINK CA CA A 303 O HOH A 516 1555 1555 2.43
LINK CA CA A 303 O HOH A 523 1555 1555 2.39
LINK CA CA A 303 O HOH A 533 1555 6545 2.35
LINK CA CA A 304 O HOH A 428 1555 1555 2.39
LINK CA CA A 304 O HOH A 502 1555 1555 2.27
CRYST1 60.898 60.898 164.513 90.00 90.00 90.00 P 43 21 2 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 0.016421 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016421 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006079 0.00000
TER 1968 GLU A 246
MASTER 367 0 4 11 7 0 0 6 2108 1 29 20
END |