HEADER TRANSPORT PROTEIN 10-APR-13 4K3F
TITLE CRYSTAL STRUCTURE OF A PUTATIVE TONB-DEPENDENT RECEPTOR (PA5505) FROM
TITLE 2 PSEUDOMONAS AERUGINOSA PAO1 AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE TONB-DEPENDENT RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: PA5505;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PERIPLASMIC METHIONINE BINDING PROTEIN, NLPA LIPOPROTEIN, PF03180
KEYWDS 2 FAMILY, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 01-FEB-23 4K3F 1 REMARK SEQADV LINK
REVDAT 3 24-JAN-18 4K3F 1 JRNL
REVDAT 2 15-NOV-17 4K3F 1 REMARK
REVDAT 1 24-APR-13 4K3F 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE TONB-DEPENDENT RECEPTOR
JRNL TITL 2 (PA5505) FROM PSEUDOMONAS AERUGINOSA PAO1 AT 1.60 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 32319
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1641
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2242
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1832
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 257
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.95000
REMARK 3 B22 (A**2) : -0.68000
REMARK 3 B33 (A**2) : -0.28000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.945
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2004 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2013 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2729 ; 1.536 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4669 ; 0.812 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 261 ; 5.903 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;42.163 ;26.329
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;13.063 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;15.994 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 326 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2248 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 386 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1007 ; 1.826 ; 3.077
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1006 ; 1.827 ; 3.078
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1269 ; 2.415 ; 5.766
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3590 8.7600 12.8430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0138 T22: 0.0096
REMARK 3 T33: 0.0107 T12: 0.0084
REMARK 3 T13: 0.0088 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.1378 L22: 0.4739
REMARK 3 L33: 0.7150 L12: 0.0644
REMARK 3 L13: 0.0397 L23: 0.2792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: -0.0080 S13: -0.0068
REMARK 3 S21: 0.0321 S22: -0.0199 S23: 0.0453
REMARK 3 S31: -0.0216 S32: -0.0580 S33: 0.0200
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS
REMARK 3 ASSIGNMENT. 5. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 6. SULFATE ION (SO4) AND GLYCEROL (GOL) MOLECULES
REMARK 3 FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTION ARE MODELED. 7.
REMARK 3 A SELENOMETHIONINE AMINO ACID IS BOUND TO THE PROTEIN. ANOMALOUS
REMARK 3 DIFFERENCE FOURIER MAP CONFIRMS THIS METHIONINE TO BE
REMARK 3 SELENOMETHIONINE.
REMARK 4
REMARK 4 4K3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078841.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-13
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 : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8265,0.9794,0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : RHODIUM-COATED VERTICAL AND
REMARK 200 HORIZONTAL FOCUSING MIRRORS;
REMARK 200 LIQUID-NITROGEN COOLED DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32359
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.135
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.20M AMMONIUM SULFATE, 0.7% N
REMARK 280 -BUTANOL, 0.1M HEPES PH 7.0, NANODROP, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 49.78850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.25450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.78850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.25450
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: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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 HOH A 499 LIES ON A SPECIAL POSITION.
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 113 CG CD CE NZ
REMARK 470 LYS A 159 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 O HOH A 568 O HOH A 636 2.17
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 PHE A 77 -16.68 -167.34
REMARK 500 VAL A 100 -55.15 -120.74
REMARK 500 ALA A 222 -151.19 -147.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-417287 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 22-260 OF THE TARGET
REMARK 999 SEQUENCE.
DBREF 4K3F A 22 260 UNP Q9HT68 Q9HT68_PSEAE 22 260
SEQADV 4K3F GLY A 0 UNP Q9HT68 EXPRESSION TAG
SEQRES 1 A 240 GLY ALA GLU SER LEU THR VAL ALA ALA THR PRO VAL PRO
SEQRES 2 A 240 HIS ALA GLU ILE LEU ASN VAL VAL LYS PRO LEU LEU ALA
SEQRES 3 A 240 LYS GLU GLY VAL ASP LEU LYS ILE LYS GLU PHE THR ASP
SEQRES 4 A 240 TYR VAL GLN PRO ASN VAL GLN VAL SER GLU LYS ARG LEU
SEQRES 5 A 240 ASP ALA ASN PHE PHE GLN HIS GLN PRO TYR LEU ASP GLU
SEQRES 6 A 240 PHE ASN LYS ALA LYS GLY THR ASP LEU VAL ALA VAL THR
SEQRES 7 A 240 GLY VAL HIS ILE GLU PRO LEU GLY ALA TYR SER SER LYS
SEQRES 8 A 240 TYR LYS LYS LEU ASP GLU LEU PRO SER GLY ALA THR VAL
SEQRES 9 A 240 VAL ILE PRO ASN ASP ALA THR ASN GLY GLY ARG ALA LEU
SEQRES 10 A 240 LEU LEU LEU ASP LYS ALA GLY VAL ILE LYS LEU LYS ASP
SEQRES 11 A 240 ASN LYS SER ILE THR ALA THR PRO LYS ASP ILE VAL ASP
SEQRES 12 A 240 ASN PRO LYS ASN ILE LYS ILE ARG GLU LEU GLU ALA ALA
SEQRES 13 A 240 THR LEU PRO ARG VAL LEU THR GLN VAL ASP MSE ALA LEU
SEQRES 14 A 240 ILE ASN THR ASN TYR ALA LEU GLU ALA LYS LEU ASN PRO
SEQRES 15 A 240 THR LYS ASP ALA LEU ALA ILE GLU GLY SER ASP SER PRO
SEQRES 16 A 240 TYR VAL ASN ILE LEU VAL ALA ARG PRO ASP ASN LYS ASP
SEQRES 17 A 240 SER ASP ALA MSE GLN LYS LEU ALA LYS ALA LEU HIS SER
SEQRES 18 A 240 ALA GLU ILE LYS GLN PHE ILE GLN GLU LYS TYR LYS GLY
SEQRES 19 A 240 ALA VAL VAL PRO ALA PHE
MODRES 4K3F MSE A 187 MET SELENOMETHIONINE
MODRES 4K3F MSE A 232 MET SELENOMETHIONINE
HET MSE A 187 8
HET MSE A 232 8
HET MSE A 300 9
HET CL A 301 1
HET SO4 A 302 5
HET SO4 A 303 5
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET GOL A 308 6
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 3 CL CL 1-
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 GOL 5(C3 H8 O3)
FORMUL 11 HOH *257(H2 O)
HELIX 1 1 PRO A 33 LYS A 47 1 15
HELIX 2 2 VAL A 61 GLU A 69 1 9
HELIX 3 3 GLN A 80 GLY A 91 1 12
HELIX 4 4 LYS A 114 LEU A 118 5 5
HELIX 5 5 ASP A 129 ALA A 143 1 15
HELIX 6 6 THR A 157 LYS A 159 5 3
HELIX 7 7 GLU A 174 ALA A 176 5 3
HELIX 8 8 THR A 177 LEU A 182 1 6
HELIX 9 9 THR A 183 VAL A 185 5 3
HELIX 10 10 ASN A 191 ALA A 198 1 8
HELIX 11 11 ASN A 201 ALA A 206 1 6
HELIX 12 12 SER A 229 LEU A 239 1 11
HELIX 13 13 SER A 241 LYS A 253 1 13
SHEET 1 A 6 VAL A 50 GLU A 56 0
SHEET 2 A 6 GLU A 23 ALA A 29 1 N GLU A 23 O ASP A 51
SHEET 3 A 6 ALA A 74 HIS A 79 1 O PHE A 76 N ALA A 28
SHEET 4 A 6 ASN A 218 ALA A 222 -1 O VAL A 221 N ASN A 75
SHEET 5 A 6 VAL A 95 ILE A 102 -1 N HIS A 101 O ASN A 218
SHEET 6 A 6 VAL A 257 PRO A 258 -1 O VAL A 257 N ILE A 102
SHEET 1 B 5 LYS A 169 LEU A 173 0
SHEET 2 B 5 THR A 123 PRO A 127 1 N VAL A 124 O ARG A 171
SHEET 3 B 5 MSE A 187 ILE A 190 1 O MSE A 187 N VAL A 125
SHEET 4 B 5 GLY A 106 TYR A 108 -1 N TYR A 108 O ALA A 188
SHEET 5 B 5 ALA A 208 ILE A 209 -1 O ALA A 208 N ALA A 107
SHEET 1 C 2 LYS A 147 LEU A 148 0
SHEET 2 C 2 ILE A 161 ASP A 163 -1 O VAL A 162 N LYS A 147
LINK C ASP A 186 N MSE A 187 1555 1555 1.35
LINK C MSE A 187 N ALA A 188 1555 1555 1.33
LINK C ALA A 231 N MSE A 232 1555 1555 1.35
LINK C MSE A 232 N GLN A 233 1555 1555 1.33
CISPEP 1 VAL A 32 PRO A 33 0 1.24
SITE 1 AC1 5 SER A 68 THR A 92 ASP A 93 HOH A 524
SITE 2 AC1 5 HOH A 635
SITE 1 AC2 8 LYS A 149 ASP A 150 ARG A 171 HOH A 439
SITE 2 AC2 8 HOH A 479 HOH A 480 HOH A 498 HOH A 628
SITE 1 AC3 3 LYS A 147 LYS A 169 ARG A 171
SITE 1 AC4 9 LYS A 142 GLU A 210 GLY A 211 ASP A 213
SITE 2 AC4 9 SER A 214 PRO A 215 HOH A 434 HOH A 620
SITE 3 AC4 9 HOH A 621
SITE 1 AC5 9 SER A 24 LEU A 25 ASP A 84 SER A 229
SITE 2 AC5 9 MSE A 232 HOH A 435 HOH A 597 HOH A 614
SITE 3 AC5 9 HOH A 641
SITE 1 AC6 3 GLU A 36 ASN A 39 LYS A 251
SITE 1 AC7 5 ASN A 39 ILE A 54 GLU A 56 GLU A 250
SITE 2 AC7 5 HOH A 583
SITE 1 AC8 3 HIS A 240 HOH A 547 HOH A 595
CRYST1 99.577 40.509 60.813 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 0.010042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.024686 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016444 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
