HEADER LIGASE 30-AUG-08 2JKU
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL REGION OF THE BIOTIN ACCEPTOR
TITLE 2 DOMAIN OF HUMAN PROPIONYL-COA CARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPIONYL-COA CARBOXYLASE ALPHA CHAIN, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BIOTIN ACCEPTOR DOMAIN, RESIDUES 633-703;
COMPND 5 SYNONYM: PROPANOYL-COA\:CARBON DIOXIDE LIGASE SUBUNIT ALPHA;
COMPND 6 EC: 6.4.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGANELLE: MITOCHONDRIA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS LIGASE, BIOTIN, ATP-BINDING, DISEASE MUTATION, NUCLEOTIDE-BINDING,
KEYWDS 2 MITOCHONDRION, PHOSPHOPROTEIN, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HEALY,W.W.YUE,G.KOCHAN,E.S.PILKA,J.W.MURRAY,A.K.ROOS,
AUTHOR 2 P.FILIPPAKOPOULOS,F.VON DELFT,C.ARROWSMITH,M.WIKSTROM,A.EDWARDS,
AUTHOR 3 C.BOUNTRA,R.A.GRAVEL,U.OPPERMANN
REVDAT 8 13-DEC-23 2JKU 1 REMARK
REVDAT 7 04-MAR-20 2JKU 1 REMARK
REVDAT 6 28-FEB-18 2JKU 1 JRNL
REVDAT 5 04-DEC-13 2JKU 1 SOURCE REMARK VERSN
REVDAT 4 20-APR-11 2JKU 1 AUTHOR JRNL REMARK
REVDAT 3 19-MAY-10 2JKU 1 VERSN JRNL
REVDAT 2 24-FEB-09 2JKU 1 VERSN
REVDAT 1 09-SEP-08 2JKU 0
JRNL AUTH S.HEALY,M.K.MCDONALD,X.WU,W.W.YUE,G.KOCHAN,U.OPPERMANN,
JRNL AUTH 2 R.A.GRAVEL
JRNL TITL STRUCTURAL IMPACT OF HUMAN AND ESCHERICHIA COLI BIOTIN
JRNL TITL 2 CARBOXYL CARRIER PROTEINS ON BIOTIN ATTACHMENT.
JRNL REF BIOCHEMISTRY V. 49 4687 2010
JRNL REFN ISSN 1520-4995
JRNL PMID 20443544
JRNL DOI 10.1021/BI901612Y
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0036
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) : 28.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 8711
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) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 438
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) : 614
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 242
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.10000
REMARK 3 B12 (A**2) : -0.03000
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): 0.056
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.027
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 289 ; 0.011 ; 0.023
REMARK 3 BOND LENGTHS OTHERS (A): 202 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 389 ; 1.546 ; 2.120
REMARK 3 BOND ANGLES OTHERS (DEGREES): 469 ; 0.893 ; 3.018
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 41 ; 5.668 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 6 ;25.095 ;26.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 47 ;10.220 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ;10.952 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 50 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 294 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 39 ; 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): 188 ; 2.330 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 311 ; 3.823 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 101 ; 5.842 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 75 ; 7.248 ;11.000
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 : 1.20
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 2JKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1290037365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.97628
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.6000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.40
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2D5D, 3BG3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.20M NA FORMATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 19.36100
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.72200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.36100
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 38.72200
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 19.36100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 38.72200
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 19.36100
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 38.72200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 -56.10700
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 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 A2002 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2048 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 610
REMARK 465 HIS A 611
REMARK 465 HIS A 612
REMARK 465 HIS A 613
REMARK 465 HIS A 614
REMARK 465 HIS A 615
REMARK 465 HIS A 616
REMARK 465 SER A 617
REMARK 465 SER A 618
REMARK 465 GLY A 619
REMARK 465 VAL A 620
REMARK 465 ASP A 621
REMARK 465 LEU A 622
REMARK 465 GLY A 623
REMARK 465 THR A 624
REMARK 465 GLU A 625
REMARK 465 ASN A 626
REMARK 465 LEU A 627
REMARK 465 TYR A 628
REMARK 465 PHE A 629
REMARK 465 GLN A 630
REMARK 465 SER A 631
REMARK 465 MET A 632
REMARK 465 MET A 668
REMARK 465 LYS A 669
REMARK 465 MET A 670
REMARK 465 GLN A 671
REMARK 465 ASN A 672
REMARK 465 SER A 673
REMARK 465 MET A 674
REMARK 465 THR A 675
REMARK 465 ALA A 676
REMARK 465 GLY A 677
REMARK 465 LYS A 678
REMARK 465 THR A 679
REMARK 465 GLY A 680
REMARK 465 THR A 681
REMARK 465 VAL A 682
REMARK 465 LYS A 683
REMARK 465 SER A 684
REMARK 465 VAL A 685
REMARK 465 HIS A 686
REMARK 465 CYS A 687
REMARK 465 GLN A 688
REMARK 465 ALA A 689
REMARK 465 GLY A 690
REMARK 465 ASP A 691
REMARK 465 THR A 692
REMARK 465 VAL A 693
REMARK 465 GLY A 694
REMARK 465 GLU A 695
REMARK 465 GLY A 696
REMARK 465 ASP A 697
REMARK 465 LEU A 698
REMARK 465 LEU A 699
REMARK 465 VAL A 700
REMARK 465 GLU A 701
REMARK 465 LEU A 702
REMARK 465 GLU A 703
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 SER A 649 O HOH A 2036 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2008 DISTANCE = 6.18 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 1669
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1669
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CQY RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF B DOMAIN FROM HUMAN PROPIONYL-COACARBOXYLASE
REMARK 900 ALPHA SUBUNIT
DBREF 2JKU A 633 703 UNP P05165 PCCA_HUMAN 633 703
SEQADV 2JKU MET A 610 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 611 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 612 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 613 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 614 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 615 UNP P05165 EXPRESSION TAG
SEQADV 2JKU HIS A 616 UNP P05165 EXPRESSION TAG
SEQADV 2JKU SER A 617 UNP P05165 EXPRESSION TAG
SEQADV 2JKU SER A 618 UNP P05165 EXPRESSION TAG
SEQADV 2JKU GLY A 619 UNP P05165 EXPRESSION TAG
SEQADV 2JKU VAL A 620 UNP P05165 EXPRESSION TAG
SEQADV 2JKU ASP A 621 UNP P05165 EXPRESSION TAG
SEQADV 2JKU LEU A 622 UNP P05165 EXPRESSION TAG
SEQADV 2JKU GLY A 623 UNP P05165 EXPRESSION TAG
SEQADV 2JKU THR A 624 UNP P05165 EXPRESSION TAG
SEQADV 2JKU GLU A 625 UNP P05165 EXPRESSION TAG
SEQADV 2JKU ASN A 626 UNP P05165 EXPRESSION TAG
SEQADV 2JKU LEU A 627 UNP P05165 EXPRESSION TAG
SEQADV 2JKU TYR A 628 UNP P05165 EXPRESSION TAG
SEQADV 2JKU PHE A 629 UNP P05165 EXPRESSION TAG
SEQADV 2JKU GLN A 630 UNP P05165 EXPRESSION TAG
SEQADV 2JKU SER A 631 UNP P05165 EXPRESSION TAG
SEQADV 2JKU MET A 632 UNP P05165 EXPRESSION TAG
SEQRES 1 A 94 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 94 GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER SER
SEQRES 3 A 94 VAL LEU ARG SER PRO MET PRO GLY VAL VAL VAL ALA VAL
SEQRES 4 A 94 SER VAL LYS PRO GLY ASP ALA VAL ALA GLU GLY GLN GLU
SEQRES 5 A 94 ILE CYS VAL ILE GLU ALA MET LYS MET GLN ASN SER MET
SEQRES 6 A 94 THR ALA GLY LYS THR GLY THR VAL LYS SER VAL HIS CYS
SEQRES 7 A 94 GLN ALA GLY ASP THR VAL GLY GLU GLY ASP LEU LEU VAL
SEQRES 8 A 94 GLU LEU GLU
HET PG4 A1668 13
HET PG4 A1669 10
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 2 PG4 2(C8 H18 O5)
FORMUL 4 HOH *58(H2 O)
SHEET 1 AA 2 VAL A 644 VAL A 648 0
SHEET 2 AA 2 CYS A 663 GLU A 666 -1 O VAL A 664 N VAL A 646
SITE 1 AC1 5 SER A 634 VAL A 636 ALA A 647 GLU A 661
SITE 2 AC1 5 VAL A 664
SITE 1 AC2 4 ARG A 638 GLU A 658 GLY A 659 HOH A2058
CRYST1 56.107 56.107 58.083 90.00 90.00 120.00 P 64 2 2 12
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 0.017823 0.010290 0.000000 0.00000
SCALE2 0.000000 0.020580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017217 0.00000
(ATOM LINES ARE NOT SHOWN.)
END