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HEADER HYDROLASE 26-MAY-24 9C0M
TITLE FPHH, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES H, APO FORM 2 AT ROOM TEMPERATURE
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, ROOM TEMPERATURE, HUMIDITY, HUMIDIFIER,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 08-JAN-25 9C0M 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 11523
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 542
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 49.6100 - 3.9700 0.99 2968 140 0.1491 0.1767
REMARK 3 2 3.9700 - 3.1500 0.98 2768 127 0.1753 0.2097
REMARK 3 3 3.1500 - 2.7500 1.00 2738 146 0.2260 0.3205
REMARK 3 4 2.7500 - 2.5000 0.92 2507 129 0.2623 0.3270
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.140
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 : 0.008 1996
REMARK 3 ANGLE : 0.871 2700
REMARK 3 CHIRALITY : 0.050 283
REMARK 3 PLANARITY : 0.008 356
REMARK 3 DIHEDRAL : 5.748 260
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7443 -9.9794 16.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.3770 T22: 0.6720
REMARK 3 T33: 0.3360 T12: -0.0123
REMARK 3 T13: 0.0076 T23: 0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 5.1826 L22: 6.0604
REMARK 3 L33: 4.7395 L12: 0.1014
REMARK 3 L13: -0.7978 L23: -1.0296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 1.0851 S13: 0.3141
REMARK 3 S21: -0.6972 S22: -0.0529 S23: -0.1127
REMARK 3 S31: -0.3707 S32: 0.1684 S33: 0.0995
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 86 THROUGH 124 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5799 -5.4153 24.3888
REMARK 3 T TENSOR
REMARK 3 T11: 0.3255 T22: 0.4779
REMARK 3 T33: 0.4086 T12: 0.0508
REMARK 3 T13: -0.0056 T23: 0.1243
REMARK 3 L TENSOR
REMARK 3 L11: 6.9022 L22: 5.5621
REMARK 3 L33: 7.3526 L12: 1.6469
REMARK 3 L13: -0.0596 L23: 1.0798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0778 S12: 0.5187 S13: 0.9047
REMARK 3 S21: -0.1200 S22: 0.0455 S23: 0.6251
REMARK 3 S31: -0.9246 S32: -0.5393 S33: -0.0221
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 125 THROUGH 157 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3669 14.1811 9.7148
REMARK 3 T TENSOR
REMARK 3 T11: 1.4721 T22: 1.2310
REMARK 3 T33: 1.4544 T12: -0.1001
REMARK 3 T13: 0.1969 T23: 0.5464
REMARK 3 L TENSOR
REMARK 3 L11: 3.8503 L22: 6.4711
REMARK 3 L33: 8.6729 L12: 1.4254
REMARK 3 L13: -2.1428 L23: -2.1127
REMARK 3 S TENSOR
REMARK 3 S11: 0.2806 S12: 0.3963 S13: 1.1637
REMARK 3 S21: -0.1113 S22: -0.7180 S23: -0.6142
REMARK 3 S31: -2.0845 S32: 1.4401 S33: 0.2261
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 158 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4820 -3.1192 31.0451
REMARK 3 T TENSOR
REMARK 3 T11: 0.4156 T22: 0.3694
REMARK 3 T33: 0.3870 T12: -0.0367
REMARK 3 T13: 0.0276 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 6.4239 L22: 5.3467
REMARK 3 L33: 5.7624 L12: -0.2916
REMARK 3 L13: -1.4101 L23: -0.5497
REMARK 3 S TENSOR
REMARK 3 S11: 0.2422 S12: -0.0255 S13: 0.8112
REMARK 3 S21: 0.1906 S22: -0.0905 S23: 0.0447
REMARK 3 S31: -0.8891 S32: 0.1169 S33: -0.0814
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 9C0M 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_1000284406.
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 : 7.5
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 : 11665
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 49.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 1.19000
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 (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL 12 MG/ML FPHH (10MM HEPES PH 7.5,
REMARK 280 100MM NACL) WERE MIXED WITH 1.5 UL OF RESERVOIR SOLUTION AND 0.5
REMARK 280 UL CRYSTALS SEEDS IN RESERVOIR SOLUTION. SITTING DROP RESERVOIR
REMARK 280 CONTAINED 100MM CALCIUM ACETATE HYDRATE, 100MM TRIS PH 7.5 AND
REMARK 280 12.5 % W/V PEG 4000., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289.15K
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 82.04700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.14250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.14250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 123.07050
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.14250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.14250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.02350
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.14250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.14250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 123.07050
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.14250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.14250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.02350
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 82.04700
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 435 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 465 LYS A 4
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 403 O HOH A 458 1.87
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 A 448 O HOH A 452 6545 2.08
REMARK 500 O HOH A 423 O HOH A 474 6545 2.16
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 -106.46 -129.45
REMARK 500 THR A 25 15.60 58.15
REMARK 500 SER A 63 -165.81 -107.92
REMARK 500 SER A 93 -122.33 57.64
REMARK 500 LYS A 121 96.49 -66.85
REMARK 500 ASP A 243 68.36 -108.98
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 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 173 O
REMARK 620 2 ASP A 176 OD1 110.7
REMARK 620 3 ASP A 176 OD2 73.3 50.2
REMARK 620 4 HOH A 441 O 127.2 95.9 146.0
REMARK 620 5 HOH A 464 O 79.3 169.8 138.2 75.7
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 417 O 68.4
REMARK 620 3 HOH A 438 O 129.9 126.8
REMARK 620 4 HOH A 463 O 80.9 75.3 63.0
REMARK 620 5 HOH A 466 O 82.0 67.6 147.0 142.7
REMARK 620 6 HOH A 467 O 88.7 152.5 57.4 86.6 125.9
REMARK 620 7 HOH A 468 O 130.4 63.2 76.2 77.4 89.1 133.1
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 HOH A 421 O 72.5
REMARK 620 3 HOH A 435 O 75.4 144.9
REMARK 620 4 HOH A 435 O 75.9 144.6 2.0
REMARK 620 5 HOH A 436 O 77.8 79.4 80.5 78.7
REMARK 620 6 HOH A 436 O 148.8 124.7 79.3 78.2 80.4
REMARK 620 7 HOH A 449 O 76.8 94.1 91.8 93.8 154.5 122.2
REMARK 620 8 HOH A 453 O 133.6 62.6 151.0 150.5 103.8 73.4 94.7
REMARK 620 N 1 2 3 4 5 6 7
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 HOH A 403 O
REMARK 620 2 HOH A 423 O 107.6
REMARK 620 3 HOH A 458 O 43.1 126.8
REMARK 620 4 HOH A 462 O 67.7 57.2 69.6
REMARK 620 5 HOH A 469 O 119.6 104.5 76.6 90.3
REMARK 620 6 HOH A 474 O 133.7 45.2 115.5 66.0 59.6
REMARK 620 N 1 2 3 4 5
DBREF1 9C0M A 1 246 UNP A0A0D6HZA6_STAAU
DBREF2 9C0M A A0A0D6HZA6 1 246
SEQADV 9C0M GLY A -2 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 9C0M PRO A -1 UNP A0A0D6HZA EXPRESSION TAG
SEQADV 9C0M 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 *78(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 GLY A 83 1 20
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 ASP A 153 1 10
HELIX 8 AA8 PRO A 157 GLU A 173 1 17
HELIX 9 AA9 GLN A 174 VAL A 178 5 5
HELIX 10 AB1 GLN A 196 VAL A 205 1 10
HELIX 11 AB2 VAL A 221 ASP A 225 5 5
HELIX 12 AB3 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 SER A 45 N PHE A 11
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 O GLU A 173 CA CA A 304 1555 1555 2.49
LINK OD1 ASP A 176 CA CA A 304 1555 1555 2.66
LINK OD2 ASP A 176 CA CA A 304 1555 1555 2.51
LINK OD1 ASP A 206 CA CA A 302 1555 1555 2.40
LINK OD1 ASP A 209 CA CA A 301 1555 1555 2.44
LINK CA CA A 301 O HOH A 421 1555 1555 2.34
LINK CA CA A 301 O HOH A 435 1555 1555 2.17
LINK CA CA A 301 O HOH A 435 1555 8555 2.23
LINK CA CA A 301 O HOH A 436 1555 1555 2.05
LINK CA CA A 301 O HOH A 436 1555 8555 2.09
LINK CA CA A 301 O HOH A 449 1555 1555 2.41
LINK CA CA A 301 O HOH A 453 1555 1555 2.21
LINK CA CA A 302 O HOH A 417 1555 1555 2.38
LINK CA CA A 302 O HOH A 438 1555 8555 2.55
LINK CA CA A 302 O HOH A 463 1555 1555 2.52
LINK CA CA A 302 O HOH A 466 1555 1555 2.61
LINK CA CA A 302 O HOH A 467 1555 1555 2.40
LINK CA CA A 302 O HOH A 468 1555 8555 2.42
LINK CA CA A 303 O HOH A 403 1555 1555 2.48
LINK CA CA A 303 O HOH A 423 1555 1555 2.76
LINK CA CA A 303 O HOH A 458 1555 1555 2.60
LINK CA CA A 303 O HOH A 462 1555 6545 2.71
LINK CA CA A 303 O HOH A 469 1555 1555 2.42
LINK CA CA A 303 O HOH A 474 1555 6545 2.85
LINK CA CA A 304 O HOH A 441 1555 1555 2.66
LINK CA CA A 304 O HOH A 464 1555 1555 2.57
CRYST1 62.285 62.285 164.094 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 0.016055 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016055 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006094 0.00000
TER 1951 GLU A 246
MASTER 395 0 4 12 7 0 0 6 2032 1 27 20
END |