HEADER TRANSFERASE 12-DEC-10 3PY9
TITLE X-RAY STRUCTURAL STUDIES OF THE ENTIRE EXTRA-CELLULAR REGION OF THE
TITLE 2 SER/THR KINASE PRKC FROM STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRA-CELLULAR DOMAIN (UNP RESIDUES 378-664);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MU50;
SOURCE 3 ORGANISM_TAXID: 158878;
SOURCE 4 STRAIN: MU50 / ATCC 700699;
SOURCE 5 GENE: SAV1220;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD24
KEYWDS PASTA, KINASE, MUROPEPTIDE BINDING, PHOSPHORYLATION, MEMBRANE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.RUGGIERO,F.SQUEGLIA,D.MARASCO,R.MARCHETTI,A.MOLINARO,R.BERISIO
REVDAT 3 21-FEB-24 3PY9 1 REMARK LINK
REVDAT 2 30-MAR-11 3PY9 1 JRNL
REVDAT 1 19-JAN-11 3PY9 0
JRNL AUTH A.RUGGIERO,F.SQUEGLIA,D.MARASCO,R.MARCHETTI,A.MOLINARO,
JRNL AUTH 2 R.BERISIO
JRNL TITL X-RAY STRUCTURAL STUDIES OF THE ENTIRE EXTRACELLULAR REGION
JRNL TITL 2 OF THE SERINE/THREONINE KINASE PRKC FROM STAPHYLOCOCCUS
JRNL TITL 3 AUREUS.
JRNL REF BIOCHEM.J. V. 435 33 2011
JRNL REFN ISSN 0264-6021
JRNL PMID 21208192
JRNL DOI 10.1042/BJ20101643
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 15327
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 829
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1031
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2180
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.347
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.263
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.385
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2206 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2960 ; 1.286 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 277 ; 6.427 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;40.673 ;26.882
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 446 ;17.809 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;15.275 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1591 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1001 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1491 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.200 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 42 ; 0.234 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.175 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1421 ; 0.762 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2258 ; 1.327 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 872 ; 1.702 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 702 ; 2.771 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3PY9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC BLUE CONFOCAL (RIGAKU)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18045
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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: SAD
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML PROTEIN SOLUTION, 21% (W/V)
REMARK 280 MPEG2000, 3% W/V D-(+)-GALACTOSE, 160 MM AMMONIUM SULFATE AND 60
REMARK 280 MM SODIUM ACETATE TRIHYDRATE BUFFER, PH 4.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 27.84050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.55150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.84050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.55150
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 300 REMARK: MONOMER
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 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 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 EU EU A 301 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 MET A 1
REMARK 465 PHE A 2
REMARK 465 GLY A 3
REMARK 465 ASN A 4
REMARK 465 LYS A 5
REMARK 465 TYR A 6
REMARK 465 GLU A 7
REMARK 465 ASN A 123
REMARK 465 ASP A 210
REMARK 465 SER A 211
REMARK 465 SER A 212
REMARK 465 ASP A 213
REMARK 465 ASP A 293
REMARK 465 ILE A 294
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 LYS A 215 CG CD CE NZ
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 NZ LYS A 205 O HOH A 385 2.17
REMARK 500 N GLU A 8 O HOH A 416 2.18
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 45 43.46 75.21
REMARK 500 LYS A 208 0.68 -53.46
REMARK 500 ASP A 241 -154.15 -149.81
REMARK 500 TYR A 291 5.09 -42.22
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 EU A 301 EU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 8 OE1
REMARK 620 2 GLU A 8 OE2 45.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 EU A 302 EU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 44 OE1
REMARK 620 2 GLU A 44 OE2 51.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 EU A 305 EU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 99 OD2
REMARK 620 2 ASP A 99 OD1 40.5
REMARK 620 3 ASP A 130 OD1 104.8 144.2
REMARK 620 4 ASN A 132 OD1 82.4 100.7 76.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 EU A 303 EU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 230 OD1
REMARK 620 2 ASP A 230 OD2 50.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EU A 305
DBREF 3PY9 A 1 294 UNP Q99UP8 Q99UP8_STAAM 371 664
SEQRES 1 A 294 MET PHE GLY ASN LYS TYR GLU GLU THR PRO ASP VAL ILE
SEQRES 2 A 294 GLY LYS SER VAL LYS GLU ALA GLU GLN ILE PHE ASN LYS
SEQRES 3 A 294 ASN ASN LEU LYS LEU GLY LYS ILE SER ARG SER TYR SER
SEQRES 4 A 294 ASP LYS TYR PRO GLU ASN GLU ILE ILE LYS THR THR PRO
SEQRES 5 A 294 ASN THR GLY GLU ARG VAL GLU ARG GLY ASP SER VAL ASP
SEQRES 6 A 294 VAL VAL ILE SER LYS GLY PRO GLU LYS VAL LYS MET PRO
SEQRES 7 A 294 ASN VAL ILE GLY LEU PRO LYS GLU GLU ALA LEU GLN LYS
SEQRES 8 A 294 LEU LYS SER LEU GLY LEU LYS ASP VAL THR ILE GLU LYS
SEQRES 9 A 294 VAL TYR ASN ASN GLN ALA PRO LYS GLY TYR ILE ALA ASN
SEQRES 10 A 294 GLN SER VAL THR ALA ASN THR GLU ILE ALA ILE HIS ASP
SEQRES 11 A 294 SER ASN ILE LYS LEU TYR GLU SER LEU GLY ILE LYS GLN
SEQRES 12 A 294 VAL TYR VAL GLU ASP PHE GLU HIS LYS SER PHE SER LYS
SEQRES 13 A 294 ALA LYS LYS ALA LEU GLU GLU LYS GLY PHE LYS VAL GLU
SEQRES 14 A 294 SER LYS GLU GLU TYR SER ASP ASP ILE ASP GLU GLY ASP
SEQRES 15 A 294 VAL ILE SER GLN SER PRO LYS GLY LYS SER VAL ASP GLU
SEQRES 16 A 294 GLY SER THR ILE SER PHE VAL VAL SER LYS GLY LYS LYS
SEQRES 17 A 294 SER ASP SER SER ASP VAL LYS THR THR THR GLU SER VAL
SEQRES 18 A 294 ASP VAL PRO TYR THR GLY LYS ASN ASP LYS SER GLN LYS
SEQRES 19 A 294 VAL LYS VAL TYR ILE LYS ASP LYS ASP ASN ASP GLY SER
SEQRES 20 A 294 THR GLU LYS GLY SER PHE ASP ILE THR SER ASP GLN ARG
SEQRES 21 A 294 ILE ASP ILE PRO LEU ARG ILE GLU LYS GLY LYS THR ALA
SEQRES 22 A 294 SER TYR ILE VAL LYS VAL ASP GLY LYS THR VAL ALA GLU
SEQRES 23 A 294 LYS GLU VAL SER TYR ASP ASP ILE
HET EU A 301 1
HET EU A 302 1
HET EU A 303 1
HET EU A 305 1
HETNAM EU EUROPIUM ION
FORMUL 2 EU 4(EU 2+)
FORMUL 6 HOH *124(H2 O)
HELIX 1 1 SER A 16 ASN A 27 1 12
HELIX 2 2 PRO A 84 SER A 94 1 11
HELIX 3 3 SER A 153 GLU A 163 1 11
SHEET 1 A 3 LYS A 30 SER A 37 0
SHEET 2 A 3 SER A 63 SER A 69 1 O ILE A 68 N SER A 35
SHEET 3 A 3 ILE A 47 THR A 51 -1 N ILE A 48 O VAL A 67
SHEET 1 B 2 LYS A 74 LYS A 76 0
SHEET 2 B 2 GLU A 125 ALA A 127 -1 O ILE A 126 N VAL A 75
SHEET 1 C 3 VAL A 100 VAL A 105 0
SHEET 2 C 3 ILE A 133 SER A 138 1 O LEU A 135 N THR A 101
SHEET 3 C 3 ILE A 115 GLN A 118 -1 N ALA A 116 O TYR A 136
SHEET 1 D 2 GLN A 143 VAL A 146 0
SHEET 2 D 2 LYS A 191 ASP A 194 -1 O LYS A 191 N VAL A 146
SHEET 1 E 3 LYS A 167 GLU A 173 0
SHEET 2 E 3 THR A 198 SER A 204 1 O ILE A 199 N LYS A 167
SHEET 3 E 3 VAL A 183 SER A 187 -1 N SER A 187 O SER A 200
SHEET 1 F 2 THR A 217 VAL A 223 0
SHEET 2 F 2 GLN A 259 LEU A 265 -1 O ILE A 263 N GLU A 219
SHEET 1 G 3 ASN A 244 ASP A 245 0
SHEET 2 G 3 GLN A 233 ASP A 241 -1 N ASP A 241 O ASN A 244
SHEET 3 G 3 GLY A 251 ILE A 255 -1 O PHE A 253 N VAL A 235
SHEET 1 H 4 ASN A 244 ASP A 245 0
SHEET 2 H 4 GLN A 233 ASP A 241 -1 N ASP A 241 O ASN A 244
SHEET 3 H 4 THR A 272 VAL A 279 -1 O ILE A 276 N TYR A 238
SHEET 4 H 4 LYS A 282 SER A 290 -1 O VAL A 289 N ALA A 273
LINK OE1 GLU A 8 EU EU A 301 1555 1555 2.84
LINK OE2 GLU A 8 EU EU A 301 1555 1555 2.89
LINK OE1 GLU A 44 EU EU A 302 1555 1555 2.51
LINK OE2 GLU A 44 EU EU A 302 1555 1555 2.58
LINK OD2 ASP A 99 EU EU A 305 1555 1555 2.42
LINK OD1 ASP A 99 EU EU A 305 1555 1555 3.37
LINK OD1 ASP A 130 EU EU A 305 1555 1555 2.43
LINK OD1 ASN A 132 EU EU A 305 1555 1555 2.63
LINK OD1 ASP A 230 EU EU A 303 1555 1555 2.54
LINK OD2 ASP A 230 EU EU A 303 1555 1555 2.60
CISPEP 1 THR A 51 PRO A 52 0 -3.71
CISPEP 2 SER A 187 PRO A 188 0 -9.74
SITE 1 AC1 1 GLU A 8
SITE 1 AC2 1 GLU A 44
SITE 1 AC3 1 ASP A 230
SITE 1 AC4 3 ASP A 99 ASP A 130 ASN A 132
CRYST1 55.681 69.103 88.430 90.00 90.00 90.00 P 21 21 2 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 0.017959 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011308 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
