HEADER BIOSYNTHETIC PROTEIN 16-DEC-09 2X0Q
TITLE CO-COMPLEX STRUCTURE OF ALCALIGIN BIOSYNTHESIS PROTEIN C (ALCC) WITH
TITLE 2 ATP FROM BORDETELLA BRONCHISEPTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALCALIGIN BIOSYNTHESIS PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALCC;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA BRONCHISEPTICA;
SOURCE 3 ORGANISM_TAXID: 518;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-151/TOPO
KEYWDS ALCALIGIN BIOSYNTHESIS, ADENYLATION, SIDEROPHORES, IRON ACQUISITION,
KEYWDS 2 BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SCHMELZ,G.L.CHALLIS,J.H.NAISMITH
REVDAT 2 20-DEC-23 2X0Q 1 REMARK LINK
REVDAT 1 27-OCT-10 2X0Q 0
JRNL AUTH S.SCHMELZ,G.L.CHALLIS,J.H.NAISMITH
JRNL TITL CO-COMPLEX STRUCTURE OF ALCALIGIN BIOSYNTHESIS PROTEIN C
JRNL TITL 2 (ALCC) WITH ATP FROM BORDETELLA BRONCHISEPTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39703
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2123
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2916
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4679
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 257
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : 0.09000
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): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.713
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4903 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6695 ; 1.173 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 596 ; 5.626 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 239 ;35.095 ;23.180
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 776 ;13.197 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;16.890 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 714 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3823 ; 0.005 ; 0.021
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): 2947 ; 0.554 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4757 ; 1.070 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1956 ; 1.665 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1932 ; 2.795 ; 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 : 1.40
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 2X0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1290042128.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41914
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 2X0O
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.7 M MGSO4, 0.18 M
REMARK 280 LI2S04 AND PROTEIN SOLUTION (2.5 MG/ML ALCC, 45 MM MES PH 6.5
REMARK 280 AND 5 MM ADENOSINE, 5 MM N-HYDROXY-N-SUCCINYLPUTRESCINE, PRE
REMARK 280 INCUBATED FOR 30 MIN ON ICE), CRYSTALS SOAKED IN 25 MM ATP, 25
REMARK 280 MM N-HYDROXY-N-SUCCINYLPUTRESCINE
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 47.29050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.29050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.72000
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 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: 6650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.4 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 94.58100
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 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 SER A 2
REMARK 465 ARG A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 ASN A 575
REMARK 465 LEU A 576
REMARK 465 GLN A 577
REMARK 465 MET A 578
REMARK 465 VAL A 579
REMARK 465 ASN A 580
REMARK 465 LEU A 581
REMARK 465 ALA A 582
REMARK 465 ASP A 583
REMARK 465 PRO A 584
REMARK 465 ILE A 585
REMARK 465 GLY A 586
REMARK 465 SER A 587
REMARK 465 PHE A 588
REMARK 465 GLN A 589
REMARK 465 MET A 590
REMARK 465 ALA A 591
REMARK 465 GLY A 607
REMARK 465 SER A 608
REMARK 465 GLY A 609
REMARK 465 GLU A 610
REMARK 465 ALA A 611
REMARK 465 LEU A 612
REMARK 465 GLN A 613
REMARK 465 THR A 614
REMARK 465 LEU A 615
REMARK 465 THR A 616
REMARK 465 ALA A 617
REMARK 465 ALA A 618
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 OD1 ASP A 175 O HOH A 2081 1.11
REMARK 500 CG ASP A 175 O HOH A 2081 1.80
REMARK 500 OH TYR A 360 O HOH A 2163 2.02
REMARK 500 NE2 GLN A 266 O HOH A 2119 2.14
REMARK 500 O ALA A 92 O HOH A 2034 2.15
REMARK 500 N GLY A 309 O HOH A 2137 2.18
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 NE ARG A 464 O HOH A 2109 4456 2.05
REMARK 500 OD2 ASP A 123 O HOH A 2163 2655 2.06
REMARK 500 O HOH A 2020 O HOH A 2151 3545 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 LYS A 255 -57.34 -123.32
REMARK 500 LEU A 258 -63.18 -102.29
REMARK 500 ILE A 285 -47.67 77.96
REMARK 500 ARG A 312 37.70 -99.61
REMARK 500 TYR A 431 -61.08 -105.70
REMARK 500 PHE A 446 -160.74 -124.60
REMARK 500 PRO A 448 49.85 -87.59
REMARK 500 ASP A 469 66.85 69.48
REMARK 500 ASN A 478 97.93 -165.79
REMARK 500 TYR A 511 -58.64 -124.22
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 MG A1609 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 451 OE1
REMARK 620 2 ASN A 452 OD1 83.1
REMARK 620 3 ASP A 469 OD2 169.6 98.6
REMARK 620 4 ATP A1607 O1G 85.8 107.9 103.3
REMARK 620 5 ATP A1607 O1A 89.0 109.0 80.7 141.8
REMARK 620 6 ATP A1607 O3A 94.2 170.8 82.5 80.6 62.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1608 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 469 OD2
REMARK 620 2 ASP A 469 OD1 48.2
REMARK 620 3 GLU A 472 OE1 136.7 88.5
REMARK 620 4 GLU A 473 OE2 91.9 96.4 94.6
REMARK 620 5 ATP A1607 O2B 88.2 90.2 91.3 171.3
REMARK 620 6 ATP A1607 O2A 93.2 140.6 129.1 92.1 79.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1609
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X0P RELATED DB: PDB
REMARK 900 CO-COMPLEX STRUCTURE OF ALCALIGIN BIOSYNTHETASE PROTEIN C (ALCC)
REMARK 900 WITH ADENOSINE FROM BORDETELLA BRONCHISEPTICA
REMARK 900 RELATED ID: 2X0O RELATED DB: PDB
REMARK 900 APO STRUCTURE OF THE ALCALIGIN BIOSYNTHESIS PROTEIN C (ALCC) FROM
REMARK 900 BORDETELLA BRONCHISEPTICA
DBREF 2X0Q A 1 618 UNP P94255 P94255_BORBR 1 618
SEQRES 1 A 618 MET SER ARG THR THR PRO PRO HIS PRO ALA GLU ILE VAL
SEQRES 2 A 618 ALA HIS LEU GLN PRO GLU ILE TRP ASN LYS VAL ASN ARG
SEQRES 3 A 618 LEU LEU VAL ARG LYS ALA ILE SER GLU TYR ALA HIS GLU
SEQRES 4 A 618 TRP LEU LEU GLU PRO GLN ARG LEU GLY PRO GLY GLU THR
SEQRES 5 A 618 PRO GLY PHE GLU ARG PHE ARG LEU THR LEU ALA ASP GLY
SEQRES 6 A 618 ALA GLN TYR ASP PHE ASP ALA GLN VAL MET ALA MET ARG
SEQRES 7 A 618 HIS TRP ARG ILE PRO PRO GLU SER ILE VAL LYS THR VAL
SEQRES 8 A 618 ALA GLY VAL PRO ALA PRO LEU ASP ALA LEU GLN PHE VAL
SEQRES 9 A 618 ILE GLU ILE ARG ASP LYS LEU GLY LEU PRO VAL ASP ARG
SEQRES 10 A 618 LEU PRO ILE TYR MET ASP GLU ILE THR SER THR LEU HIS
SEQRES 11 A 618 GLY SER ALA TYR LYS HIS GLY ARG THR THR LEU GLY ALA
SEQRES 12 A 618 ALA ALA LEU ALA ARG ALA ASP TYR GLN THR ILE GLU THR
SEQRES 13 A 618 SER MET ILE GLU GLY HIS PRO SER PHE VAL ALA ASN ASN
SEQRES 14 A 618 GLY ARG LEU GLY PHE ASP ALA GLU ASP TYR HIS GLY TYR
SEQRES 15 A 618 ALA PRO GLU ALA ALA THR PRO VAL ARG LEU MET TRP LEU
SEQRES 16 A 618 ALA VAL HIS LYS ASP ASN ALA HIS PHE SER CYS LEU SER
SEQRES 17 A 618 ASP MET ASP TYR ASP SER LEU MET SER GLU GLU LEU GLY
SEQRES 18 A 618 GLU SER ALA VAL THR ASP PHE ALA ALA ARG LEU ARG GLU
SEQRES 19 A 618 GLN GLY LEU HIS PRO ALA ASP TYR TYR PHE MET PRO ALA
SEQRES 20 A 618 HIS PRO TRP GLN TRP PHE ASN LYS LEU SER LEU ALA PHE
SEQRES 21 A 618 ALA PRO TYR VAL ALA GLN ARG LYS ILE VAL CYS LEU GLY
SEQRES 22 A 618 TYR GLY GLU GLU GLN TYR LEU ALA GLN GLN SER ILE ARG
SEQRES 23 A 618 THR PHE PHE ASN ILE SER ARG PRO GLY LYS ARG TYR VAL
SEQRES 24 A 618 LYS THR SER LEU SER ILE LEU ASN MET GLY PHE MET ARG
SEQRES 25 A 618 GLY LEU SER PRO TYR TYR MET ALA GLY THR PRO ALA ILE
SEQRES 26 A 618 ASN GLU TYR ILE HIS ASP LEU ILE SER ALA ASP PRO TRP
SEQRES 27 A 618 LEU ARG ALA ASN GLY PHE ARG ILE LEU ARG GLU VAL ALA
SEQRES 28 A 618 SER MET GLY PHE ARG ASN TYR TYR TYR GLU ALA ALA ILE
SEQRES 29 A 618 ASP THR ASP THR PRO TYR LYS LYS MET PHE SER ALA LEU
SEQRES 30 A 618 TRP ARG GLU ASN PRO LEU THR LEU ILE ALA PRO GLY GLN
SEQRES 31 A 618 ASN LEU MET THR MET ALA ALA LEU LEU HIS VAL ASP PRO
SEQRES 32 A 618 GLN GLY ARG ALA LEU LEU PRO GLU LEU ILE GLN ALA SER
SEQRES 33 A 618 GLY LEU ASP ALA GLY THR TRP LEU GLU ARG TYR VAL ASP
SEQRES 34 A 618 ALA TYR LEU THR PRO LEU ILE HIS CYS PHE TYR ALA HIS
SEQRES 35 A 618 ASP LEU VAL PHE MET PRO HIS GLY GLU ASN VAL ILE LEU
SEQRES 36 A 618 VAL ILE GLN ASP GLY VAL PRO VAL ARG ALA PHE MET LYS
SEQRES 37 A 618 ASP ILE ALA GLU GLU SER SER ILE LEU ASN PRO GLN VAL
SEQRES 38 A 618 ARG LEU PRO GLN ALA ALA GLN ARG LEU ALA ALA ASP VAL
SEQRES 39 A 618 PRO GLU ALA TYR LYS LEU LEU THR ILE PHE VAL ASP VAL
SEQRES 40 A 618 PHE GLU GLY TYR PHE ARG HIS LEU THR GLN ILE LEU VAL
SEQRES 41 A 618 GLU THR GLU LEU MET PRO GLU HIS ASP PHE TRP ARG LEU
SEQRES 42 A 618 VAL ALA GLY ARG ILE ALA ALA TYR GLN GLN ALA HIS PRO
SEQRES 43 A 618 GLN ARG LEU ASP LYS TYR ARG ARG TYR ASP LEU PHE ALA
SEQRES 44 A 618 PRO ASP MET ILE HIS SER CYS LEU ASN ARG LEU GLN LEU
SEQRES 45 A 618 ALA ASN ASN LEU GLN MET VAL ASN LEU ALA ASP PRO ILE
SEQRES 46 A 618 GLY SER PHE GLN MET ALA PRO ASN LEU PRO ASN PRO ILE
SEQRES 47 A 618 ALA CYS PHE ARG PRO SER TRP LEU GLY SER GLY GLU ALA
SEQRES 48 A 618 LEU GLN THR LEU THR ALA ALA
HET ATP A1607 31
HET MG A1608 1
HET MG A1609 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 ATP C10 H16 N5 O13 P3
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *257(H2 O)
HELIX 1 1 ALA A 10 ALA A 14 5 5
HELIX 2 2 GLN A 17 GLU A 39 1 23
HELIX 3 3 PRO A 83 ILE A 87 5 5
HELIX 4 4 ASP A 99 ILE A 107 1 9
HELIX 5 5 ILE A 107 GLY A 112 1 6
HELIX 6 6 ARG A 117 ARG A 138 1 22
HELIX 7 7 GLY A 142 ALA A 147 1 6
HELIX 8 8 ASP A 150 MET A 158 1 9
HELIX 9 9 ASP A 175 ALA A 183 1 9
HELIX 10 10 PRO A 184 ALA A 187 5 4
HELIX 11 11 ASP A 211 LEU A 220 1 10
HELIX 12 12 GLY A 221 GLN A 235 1 15
HELIX 13 13 HIS A 238 ALA A 240 5 3
HELIX 14 14 HIS A 248 LYS A 255 1 8
HELIX 15 15 LYS A 255 PHE A 260 1 6
HELIX 16 16 PHE A 260 GLN A 266 1 7
HELIX 17 17 SER A 315 GLY A 343 1 29
HELIX 18 18 ASN A 357 ILE A 364 1 8
HELIX 19 19 THR A 368 MET A 373 5 6
HELIX 20 20 ASN A 381 ILE A 386 5 6
HELIX 21 21 ALA A 396 HIS A 400 5 5
HELIX 22 22 ALA A 407 GLY A 417 1 11
HELIX 23 23 ASP A 419 ASP A 443 1 25
HELIX 24 24 PRO A 484 LEU A 490 5 7
HELIX 25 25 PRO A 495 LYS A 499 5 5
HELIX 26 26 LEU A 500 VAL A 505 1 6
HELIX 27 27 ASP A 506 GLY A 510 1 5
HELIX 28 28 TYR A 511 THR A 522 1 12
HELIX 29 29 PRO A 526 HIS A 545 1 20
HELIX 30 30 ARG A 548 TYR A 555 1 8
HELIX 31 31 CYS A 566 ASN A 574 1 9
HELIX 32 32 ILE A 598 ARG A 602 5 5
SHEET 1 AA 4 GLN A 45 PRO A 49 0
SHEET 2 AA 4 GLU A 56 THR A 61 -1 O ARG A 57 N LEU A 47
SHEET 3 AA 4 ALA A 66 MET A 75 -1 O TYR A 68 N LEU A 60
SHEET 4 AA 4 HIS A 79 ARG A 81 1 O HIS A 79 N MET A 75
SHEET 1 AB 5 GLN A 45 PRO A 49 0
SHEET 2 AB 5 GLU A 56 THR A 61 -1 O ARG A 57 N LEU A 47
SHEET 3 AB 5 ALA A 66 MET A 75 -1 O TYR A 68 N LEU A 60
SHEET 4 AB 5 VAL A 88 VAL A 91 -1 O VAL A 88 N ASP A 69
SHEET 5 AB 5 VAL A 94 ALA A 96 -1 O VAL A 94 N VAL A 91
SHEET 1 AC 2 HIS A 79 ARG A 81 0
SHEET 2 AC 2 ALA A 66 MET A 75 1 O GLN A 73 N ARG A 81
SHEET 1 AD 8 ALA A 202 CYS A 206 0
SHEET 2 AD 8 GLU A 349 PHE A 355 -1 O SER A 352 N SER A 205
SHEET 3 AD 8 SER A 375 ARG A 379 -1 O ALA A 376 N MET A 353
SHEET 4 AD 8 TYR A 298 THR A 301 -1 O TYR A 298 N ARG A 379
SHEET 5 AD 8 THR A 287 ASN A 290 -1 O PHE A 288 N VAL A 299
SHEET 6 AD 8 ILE A 269 ALA A 281 -1 O LEU A 280 N PHE A 289
SHEET 7 AD 8 VAL A 190 HIS A 198 -1 O VAL A 190 N TYR A 279
SHEET 8 AD 8 TYR A 242 ALA A 247 -1 O TYR A 243 N VAL A 197
SHEET 1 AE 2 LEU A 303 ASN A 307 0
SHEET 2 AE 2 PHE A 310 ARG A 312 -1 O PHE A 310 N ASN A 307
SHEET 1 AF 4 ARG A 345 ILE A 346 0
SHEET 2 AF 4 VAL A 461 MET A 467 1 O ALA A 465 N ARG A 345
SHEET 3 AF 4 VAL A 453 GLN A 458 -1 O ILE A 454 N PHE A 466
SHEET 4 AF 4 ASN A 391 THR A 394 -1 O ASN A 391 N ILE A 457
SHEET 1 AG 2 LEU A 444 VAL A 445 0
SHEET 2 AG 2 SER A 475 ILE A 476 -1 O SER A 475 N VAL A 445
SHEET 1 AH 2 ASP A 561 MET A 562 0
SHEET 2 AH 2 LEU A 594 PRO A 595 -1 O LEU A 594 N MET A 562
LINK OE1 GLU A 451 MG MG A1609 1555 1555 2.37
LINK OD1 ASN A 452 MG MG A1609 1555 1555 2.19
LINK OD2 ASP A 469 MG MG A1608 1555 1555 2.39
LINK OD1 ASP A 469 MG MG A1608 1555 1555 2.85
LINK OD2 ASP A 469 MG MG A1609 1555 1555 2.46
LINK OE1 GLU A 472 MG MG A1608 1555 1555 2.60
LINK OE2 GLU A 473 MG MG A1608 1555 1555 2.41
LINK O2B ATP A1607 MG MG A1608 1555 1555 2.29
LINK O2A ATP A1607 MG MG A1608 1555 1555 2.58
LINK O1G ATP A1607 MG MG A1609 1555 1555 2.13
LINK O1A ATP A1607 MG MG A1609 1555 1555 2.36
LINK O3A ATP A1607 MG MG A1609 1555 1555 2.49
SITE 1 AC1 28 GLY A 161 HIS A 162 ASN A 168 GLN A 283
SITE 2 AC1 28 SER A 284 ARG A 286 THR A 287 LYS A 300
SITE 3 AC1 28 ASN A 307 MET A 308 ARG A 312 ARG A 379
SITE 4 AC1 28 ALA A 396 HIS A 449 GLU A 451 ASN A 452
SITE 5 AC1 28 ASP A 469 GLU A 472 GLU A 473 MG A1608
SITE 6 AC1 28 MG A1609 HOH A2077 HOH A2194 HOH A2200
SITE 7 AC1 28 HOH A2254 HOH A2255 HOH A2256 HOH A2257
SITE 1 AC2 4 ASP A 469 GLU A 472 GLU A 473 ATP A1607
SITE 1 AC3 4 GLU A 451 ASN A 452 ASP A 469 ATP A1607
CRYST1 94.581 129.440 46.484 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 0.010573 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007726 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021513 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
