HEADER LYASE 18-MAR-11 3R5G
TITLE CRYSTAL STRUCTURE OF THE ADENYLYL CYCLASE CYAB FROM P. AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYAB;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 220-416;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: CYAB, PA3217;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ADENYLYL CYCLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TOPAL,C.STEEGBORN
REVDAT 4 13-SEP-23 3R5G 1 REMARK SEQADV
REVDAT 3 15-FEB-12 3R5G 1 JRNL
REVDAT 2 25-JAN-12 3R5G 1 JRNL
REVDAT 1 11-JAN-12 3R5G 0
JRNL AUTH H.TOPAL,N.B.FULCHER,J.BITTERMAN,E.SALAZAR,J.BUCK,L.R.LEVIN,
JRNL AUTH 2 M.J.CANN,M.C.WOLFGANG,C.STEEGBORN
JRNL TITL CRYSTAL STRUCTURE AND REGULATION MECHANISMS OF THE CYAB
JRNL TITL 2 ADENYLYL CYCLASE FROM THE HUMAN PATHOGEN PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF J.MOL.BIOL. V. 416 271 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22226839
JRNL DOI 10.1016/J.JMB.2011.12.045
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48397
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2548
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2120
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.093
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.456
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3099 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4160 ; 2.367 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 389 ; 6.052 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;36.129 ;23.768
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 588 ;16.014 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;22.226 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 470 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2282 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1927 ; 1.647 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3096 ; 2.705 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1172 ; 4.064 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1064 ; 6.645 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3R5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : DOUBLE XTAL SI(111) FIXED-EXIT
REMARK 200 MONOCHROMATOR, FIRST XTAL LN2-
REMARK 200 COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50946
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1WC1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 10 % (V/V) 2
REMARK 280 -PROPANOL, 20 % (W/V) PEG 4000, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 51.36000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -14.43156
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 93.65462
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 219
REMARK 465 ARG A 220
REMARK 465 LEU A 221
REMARK 465 GLY B 219
REMARK 465 ARG B 220
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 150 O HOH A 470 1.95
REMARK 500 CG MET A 281 O HOH A 432 2.09
REMARK 500 O HOH B 467 O HOH B 468 2.10
REMARK 500 OE2 GLU B 222 O HOH B 461 2.13
REMARK 500 NE2 GLN B 290 O HOH B 463 2.16
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 B 162 O HOH B 418 1565 2.02
REMARK 500 OH TYR B 336 OH TYR B 336 2656 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 307 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 MET A 310 CG - SD - CE ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASP A 384 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 PRO A 402 C - N - CA ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG A 412 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 413 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 414 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP B 234 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 314 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 TYR B 336 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP B 390 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP B 390 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP B 414 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 414 CB - CG - OD2 ANGL. DEV. = -13.0 DEGREES
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 244 -14.00 -143.37
REMARK 500 ARG A 347 72.03 -156.80
REMARK 500 ARG B 347 71.00 -156.48
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 GOL B 1
DBREF 3R5G A 220 416 UNP Q9HZ23 Q9HZ23_PSEAE 220 416
DBREF 3R5G B 220 416 UNP Q9HZ23 Q9HZ23_PSEAE 220 416
SEQADV 3R5G GLY A 219 UNP Q9HZ23 EXPRESSION TAG
SEQADV 3R5G GLY B 219 UNP Q9HZ23 EXPRESSION TAG
SEQRES 1 A 198 GLY ARG LEU GLU THR GLN ARG LYS LYS LEU THR VAL PHE
SEQRES 2 A 198 PHE SER ASP ILE ARG GLY PHE THR GLU LEU SER GLU GLU
SEQRES 3 A 198 LEU GLU ALA GLU ALA LEU THR ASP LEU LEU ASN ASN TYR
SEQRES 4 A 198 LEU ASN GLU MET SER LYS ILE ALA LEU LYS TYR GLY GLY
SEQRES 5 A 198 THR ILE ASP LYS PHE VAL GLY ASP CYS VAL MET VAL PHE
SEQRES 6 A 198 PHE GLY ASP PRO SER THR GLN GLY ALA LYS LYS ASP ALA
SEQRES 7 A 198 VAL ALA ALA VAL SER MET GLY ILE ALA MET ARG LYS HIS
SEQRES 8 A 198 MET LYS VAL LEU ARG GLN GLN TRP ARG ALA GLN GLY ILE
SEQRES 9 A 198 THR LYS PRO LEU GLU ILE ARG MET GLY ILE ASN THR GLY
SEQRES 10 A 198 TYR CYS THR VAL GLY ASN PHE GLY ALA ASP THR ARG MET
SEQRES 11 A 198 ASP TYR THR ILE ILE GLY ARG GLU VAL ASN LEU ALA SER
SEQRES 12 A 198 ARG LEU GLU SER ALA SER GLU ALA GLY GLU ILE LEU ILE
SEQRES 13 A 198 SER HIS GLU THR TYR SER LEU ILE LYS ASP VAL ILE MET
SEQRES 14 A 198 CYS ARG ASP LYS GLY GLN ILE ALA VAL LYS GLY PHE SER
SEQRES 15 A 198 ARG PRO VAL GLN ILE TYR GLN VAL VAL ASP SER ARG ARG
SEQRES 16 A 198 ASP LEU GLY
SEQRES 1 B 198 GLY ARG LEU GLU THR GLN ARG LYS LYS LEU THR VAL PHE
SEQRES 2 B 198 PHE SER ASP ILE ARG GLY PHE THR GLU LEU SER GLU GLU
SEQRES 3 B 198 LEU GLU ALA GLU ALA LEU THR ASP LEU LEU ASN ASN TYR
SEQRES 4 B 198 LEU ASN GLU MET SER LYS ILE ALA LEU LYS TYR GLY GLY
SEQRES 5 B 198 THR ILE ASP LYS PHE VAL GLY ASP CYS VAL MET VAL PHE
SEQRES 6 B 198 PHE GLY ASP PRO SER THR GLN GLY ALA LYS LYS ASP ALA
SEQRES 7 B 198 VAL ALA ALA VAL SER MET GLY ILE ALA MET ARG LYS HIS
SEQRES 8 B 198 MET LYS VAL LEU ARG GLN GLN TRP ARG ALA GLN GLY ILE
SEQRES 9 B 198 THR LYS PRO LEU GLU ILE ARG MET GLY ILE ASN THR GLY
SEQRES 10 B 198 TYR CYS THR VAL GLY ASN PHE GLY ALA ASP THR ARG MET
SEQRES 11 B 198 ASP TYR THR ILE ILE GLY ARG GLU VAL ASN LEU ALA SER
SEQRES 12 B 198 ARG LEU GLU SER ALA SER GLU ALA GLY GLU ILE LEU ILE
SEQRES 13 B 198 SER HIS GLU THR TYR SER LEU ILE LYS ASP VAL ILE MET
SEQRES 14 B 198 CYS ARG ASP LYS GLY GLN ILE ALA VAL LYS GLY PHE SER
SEQRES 15 B 198 ARG PRO VAL GLN ILE TYR GLN VAL VAL ASP SER ARG ARG
SEQRES 16 B 198 ASP LEU GLY
HET GOL B 1 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *317(H2 O)
HELIX 1 1 GLY A 237 GLU A 243 1 7
HELIX 2 2 GLU A 246 GLY A 269 1 24
HELIX 3 3 GLY A 291 ALA A 319 1 29
HELIX 4 4 GLY A 354 SER A 367 1 14
HELIX 5 5 HIS A 376 LYS A 383 1 8
HELIX 6 6 GLY B 237 LEU B 245 1 9
HELIX 7 7 GLU B 246 GLY B 269 1 24
HELIX 8 8 GLY B 291 GLN B 320 1 30
HELIX 9 9 GLY B 354 SER B 367 1 14
HELIX 10 10 HIS B 376 LYS B 383 1 8
SHEET 1 A 5 THR A 271 VAL A 276 0
SHEET 2 A 5 CYS A 279 PHE A 284 -1 O PHE A 283 N THR A 271
SHEET 3 A 5 GLN A 224 ARG A 236 -1 N PHE A 231 O VAL A 282
SHEET 4 A 5 GLU A 327 ALA A 344 -1 O VAL A 339 N GLN A 224
SHEET 5 A 5 ARG A 347 ILE A 353 -1 O ASP A 349 N PHE A 342
SHEET 1 B 7 THR A 271 VAL A 276 0
SHEET 2 B 7 CYS A 279 PHE A 284 -1 O PHE A 283 N THR A 271
SHEET 3 B 7 GLN A 224 ARG A 236 -1 N PHE A 231 O VAL A 282
SHEET 4 B 7 GLU A 327 ALA A 344 -1 O VAL A 339 N GLN A 224
SHEET 5 B 7 ILE A 372 SER A 375 1 O LEU A 373 N MET A 330
SHEET 6 B 7 VAL A 403 VAL A 408 -1 O TYR A 406 N ILE A 374
SHEET 7 B 7 CYS A 388 ILE A 394 -1 N GLY A 392 O ILE A 405
SHEET 1 C 5 THR B 271 VAL B 276 0
SHEET 2 C 5 CYS B 279 PHE B 284 -1 O PHE B 283 N THR B 271
SHEET 3 C 5 GLN B 224 ARG B 236 -1 N PHE B 231 O VAL B 282
SHEET 4 C 5 GLU B 327 ALA B 344 -1 O VAL B 339 N GLN B 224
SHEET 5 C 5 ARG B 347 ILE B 353 -1 O THR B 351 N GLY B 340
SHEET 1 D 7 THR B 271 VAL B 276 0
SHEET 2 D 7 CYS B 279 PHE B 284 -1 O PHE B 283 N THR B 271
SHEET 3 D 7 GLN B 224 ARG B 236 -1 N PHE B 231 O VAL B 282
SHEET 4 D 7 GLU B 327 ALA B 344 -1 O VAL B 339 N GLN B 224
SHEET 5 D 7 ILE B 372 SER B 375 1 O LEU B 373 N MET B 330
SHEET 6 D 7 VAL B 403 VAL B 408 -1 O TYR B 406 N ILE B 374
SHEET 7 D 7 CYS B 388 ILE B 394 -1 N ARG B 389 O GLN B 407
CISPEP 1 ASP A 286 PRO A 287 0 -0.74
CISPEP 2 ASP B 286 PRO B 287 0 -2.90
SITE 1 AC1 4 HOH A 96 CYS A 388 LYS B 308 GLY B 416
CRYST1 51.360 36.310 94.760 90.00 98.76 90.00 P 1 2 1 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 0.019470 0.000000 0.003002 0.00000
SCALE2 0.000000 0.027541 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010678 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
