HEADER LIGASE 03-MAR-08 2VPQ
TITLE CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM S. AUREUS COMPLEXED WITH
TITLE 2 AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA CARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BIOTIN CARBOXYLASE;
COMPND 5 EC: 6.3.4.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACTERIA, ATP-GRASP DOMAIN, BIOTIN CARBOXYLASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOCHALKIN
REVDAT 4 13-DEC-23 2VPQ 1 LINK
REVDAT 3 24-FEB-09 2VPQ 1 VERSN
REVDAT 2 30-SEP-08 2VPQ 1 JRNL
REVDAT 1 09-SEP-08 2VPQ 0
JRNL AUTH I.MOCHALKIN,J.R.MILLER,A.EVDOKIMOV,S.LIGHTLE,C.YAN,
JRNL AUTH 2 C.K.STOVER,G.L.WALDROP
JRNL TITL STRUCTURAL EVIDENCE FOR SUBSTRATE-INDUCED SYNERGISM AND
JRNL TITL 2 HALF-SITES REACTIVITY IN BIOTIN CARBOXYLASE.
JRNL REF PROTEIN SCI. V. 17 1706 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18725455
JRNL DOI 10.1110/PS.035584.108
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 52269
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2810
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2822
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 817
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35000
REMARK 3 B22 (A**2) : -1.68000
REMARK 3 B33 (A**2) : 1.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.289
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.240
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.212
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7184 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4887 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9719 ; 1.231 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11957 ; 0.885 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 899 ; 6.009 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;36.811 ;24.788
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1274 ;16.201 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.623 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1075 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7997 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1395 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1561 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5333 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3508 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3825 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 617 ; 0.182 ; 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): 21 ; 0.204 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 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): 5823 ; 0.608 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7179 ; 0.707 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3137 ; 1.181 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2538 ; 1.790 ; 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 : 1.20
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 2VPQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1290035534.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-07
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 : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
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 : 55214
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1DV2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL; 20% PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.65900
REMARK 290 SMTRY3 2 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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASP A 449
REMARK 465 GLU A 450
REMARK 465 GLY A 451
REMARK 465 MET B 1
REMARK 465 GLU B 450
REMARK 465 GLY B 451
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 ILE A 245 CG1 CG2 CD1
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 2332 O HOH B 2306 2.14
REMARK 500 O HOH A 2179 O HOH A 2201 2.15
REMARK 500 OE1 GLN A 26 O HOH A 2027 2.17
REMARK 500 O HOH A 2135 O HOH A 2298 2.19
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 2027 O HOH B 2172 2545 2.16
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 SER A 58 -84.27 -119.56
REMARK 500 PHE A 83 -100.43 55.60
REMARK 500 ASN A 193 107.07 -160.09
REMARK 500 MET A 234 -36.30 78.60
REMARK 500 ASN A 269 -158.40 72.60
REMARK 500 ASN A 375 2.99 80.50
REMARK 500 TYR A 382 -51.18 -131.74
REMARK 500 SER B 58 -80.66 -124.95
REMARK 500 PHE B 83 -104.36 55.01
REMARK 500 ARG B 233 68.74 22.02
REMARK 500 MET B 234 -22.54 80.62
REMARK 500 ASN B 266 58.70 39.80
REMARK 500 ASN B 269 -157.68 74.99
REMARK 500 ASN B 375 1.86 84.22
REMARK 500 PRO B 380 33.79 -81.52
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 = 6.45 ANGSTROMS
REMARK 525 HOH B2044 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B2051 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B2056 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B2163 DISTANCE = 6.50 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (ANP): ATP
REMARK 600 ANALOG
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 A1450 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 274 OE2
REMARK 620 2 GLU A 274 OE1 57.3
REMARK 620 3 GLU A 288 OE1 111.3 86.5
REMARK 620 4 ANP A1449 O1G 101.2 156.1 93.1
REMARK 620 5 ANP A1449 O2A 146.5 97.7 86.5 106.1
REMARK 620 6 HOH A2417 O 85.4 97.6 162.0 90.1 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1451 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 288 OE1
REMARK 620 2 GLU A 288 OE2 57.2
REMARK 620 3 ANP A1449 O2G 88.3 143.9
REMARK 620 4 ANP A1449 O1B 92.0 87.2 83.5
REMARK 620 5 HOH A2172 O 156.7 101.0 114.5 95.4
REMARK 620 6 HOH A2266 O 93.0 95.2 96.9 175.1 80.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1451 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 274 OE1
REMARK 620 2 GLU B 274 OE2 50.1
REMARK 620 3 GLU B 288 OE1 75.7 98.6
REMARK 620 4 ANP B1450 O2A 108.7 155.2 85.7
REMARK 620 5 ANP B1450 O3G 128.9 91.3 80.0 113.5
REMARK 620 6 HOH B2398 O 102.4 78.7 177.4 96.7 100.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1452 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 288 OE2
REMARK 620 2 GLU B 288 OE1 54.2
REMARK 620 3 ANP B1450 O1G 142.2 88.4
REMARK 620 4 ANP B1450 O1B 84.0 90.0 91.1
REMARK 620 5 HOH B2155 O 103.3 157.5 114.0 87.7
REMARK 620 6 HOH B2243 O 94.6 98.3 96.7 168.8 81.7
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 ANP B1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1453
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C00 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 IN APO FORM
REMARK 900 RELATED ID: 2J9G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX
REMARK 900 WITH AMPPNP AND ADP
REMARK 900 RELATED ID: 2VQD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 COMPLEXED WITH AMPCP
REMARK 900 RELATED ID: 2VR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN COMPLEX
REMARK 900 WITH ATP ANALOG, ADPCF2P.
DBREF 2VPQ A 1 451 UNP Q99TW7 Q99TW7_STAAM 1 451
DBREF 2VPQ B 1 451 UNP Q99TW7 Q99TW7_STAAM 1 451
SEQRES 1 A 451 MET LYS LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE ALA
SEQRES 2 A 451 VAL ARG ILE ILE ARG ALA CYS ARG ASP LEU GLY ILE GLN
SEQRES 3 A 451 THR VAL ALA ILE TYR SER GLU GLY ASP LYS ASP ALA LEU
SEQRES 4 A 451 HIS THR GLN ILE ALA ASP GLU ALA TYR CYS VAL GLY PRO
SEQRES 5 A 451 THR LEU SER LYS ASP SER TYR LEU ASN ILE PRO ASN ILE
SEQRES 6 A 451 LEU SER ILE ALA THR SER THR GLY CYS ASP GLY VAL HIS
SEQRES 7 A 451 PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE ALA
SEQRES 8 A 451 GLU LEU CYS GLU ALA CYS GLN LEU LYS PHE ILE GLY PRO
SEQRES 9 A 451 SER TYR GLN SER ILE GLN LYS MET GLY ILE LYS ASP VAL
SEQRES 10 A 451 ALA LYS ALA GLU MET ILE LYS ALA ASN VAL PRO VAL VAL
SEQRES 11 A 451 PRO GLY SER ASP GLY LEU MET LYS ASP VAL SER GLU ALA
SEQRES 12 A 451 LYS LYS ILE ALA LYS LYS ILE GLY TYR PRO VAL ILE ILE
SEQRES 13 A 451 LYS ALA THR ALA GLY GLY GLY GLY LYS GLY ILE ARG VAL
SEQRES 14 A 451 ALA ARG ASP GLU LYS GLU LEU GLU THR GLY PHE ARG MET
SEQRES 15 A 451 THR GLU GLN GLU ALA GLN THR ALA PHE GLY ASN GLY GLY
SEQRES 16 A 451 LEU TYR MET GLU LYS PHE ILE GLU ASN PHE ARG HIS ILE
SEQRES 17 A 451 GLU ILE GLN ILE VAL GLY ASP SER TYR GLY ASN VAL ILE
SEQRES 18 A 451 HIS LEU GLY GLU ARG ASP CYS THR ILE GLN ARG ARG MET
SEQRES 19 A 451 GLN LYS LEU VAL GLU GLU ALA PRO SER PRO ILE LEU ASP
SEQRES 20 A 451 ASP GLU THR ARG ARG GLU MET GLY ASN ALA ALA VAL ARG
SEQRES 21 A 451 ALA ALA LYS ALA VAL ASN TYR GLU ASN ALA GLY THR ILE
SEQRES 22 A 451 GLU PHE ILE TYR ASP LEU ASN ASP ASN LYS PHE TYR PHE
SEQRES 23 A 451 MET GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL
SEQRES 24 A 451 THR GLU MET VAL THR GLY ILE ASP LEU VAL LYS LEU GLN
SEQRES 25 A 451 LEU GLN VAL ALA MET GLY ASP VAL LEU PRO TYR LYS GLN
SEQRES 26 A 451 GLU ASP ILE LYS LEU THR GLY HIS ALA ILE GLU PHE ARG
SEQRES 27 A 451 ILE ASN ALA GLU ASN PRO TYR LYS ASN PHE MET PRO SER
SEQRES 28 A 451 PRO GLY LYS ILE GLU GLN TYR LEU ALA PRO GLY GLY TYR
SEQRES 29 A 451 GLY VAL ARG ILE GLU SER ALA CYS TYR THR ASN TYR THR
SEQRES 30 A 451 ILE PRO PRO TYR TYR ASP SER MET VAL ALA LYS LEU ILE
SEQRES 31 A 451 ILE HIS GLU PRO THR ARG ASP GLU ALA ILE MET ALA GLY
SEQRES 32 A 451 ILE ARG ALA LEU SER GLU PHE VAL VAL LEU GLY ILE ASP
SEQRES 33 A 451 THR THR ILE PRO PHE HIS ILE LYS LEU LEU ASN ASN ASP
SEQRES 34 A 451 ILE PHE ARG SER GLY LYS PHE ASN THR ASN PHE LEU GLU
SEQRES 35 A 451 GLN ASN SER ILE MET ASN ASP GLU GLY
SEQRES 1 B 451 MET LYS LYS VAL LEU ILE ALA ASN ARG GLY GLU ILE ALA
SEQRES 2 B 451 VAL ARG ILE ILE ARG ALA CYS ARG ASP LEU GLY ILE GLN
SEQRES 3 B 451 THR VAL ALA ILE TYR SER GLU GLY ASP LYS ASP ALA LEU
SEQRES 4 B 451 HIS THR GLN ILE ALA ASP GLU ALA TYR CYS VAL GLY PRO
SEQRES 5 B 451 THR LEU SER LYS ASP SER TYR LEU ASN ILE PRO ASN ILE
SEQRES 6 B 451 LEU SER ILE ALA THR SER THR GLY CYS ASP GLY VAL HIS
SEQRES 7 B 451 PRO GLY TYR GLY PHE LEU ALA GLU ASN ALA ASP PHE ALA
SEQRES 8 B 451 GLU LEU CYS GLU ALA CYS GLN LEU LYS PHE ILE GLY PRO
SEQRES 9 B 451 SER TYR GLN SER ILE GLN LYS MET GLY ILE LYS ASP VAL
SEQRES 10 B 451 ALA LYS ALA GLU MET ILE LYS ALA ASN VAL PRO VAL VAL
SEQRES 11 B 451 PRO GLY SER ASP GLY LEU MET LYS ASP VAL SER GLU ALA
SEQRES 12 B 451 LYS LYS ILE ALA LYS LYS ILE GLY TYR PRO VAL ILE ILE
SEQRES 13 B 451 LYS ALA THR ALA GLY GLY GLY GLY LYS GLY ILE ARG VAL
SEQRES 14 B 451 ALA ARG ASP GLU LYS GLU LEU GLU THR GLY PHE ARG MET
SEQRES 15 B 451 THR GLU GLN GLU ALA GLN THR ALA PHE GLY ASN GLY GLY
SEQRES 16 B 451 LEU TYR MET GLU LYS PHE ILE GLU ASN PHE ARG HIS ILE
SEQRES 17 B 451 GLU ILE GLN ILE VAL GLY ASP SER TYR GLY ASN VAL ILE
SEQRES 18 B 451 HIS LEU GLY GLU ARG ASP CYS THR ILE GLN ARG ARG MET
SEQRES 19 B 451 GLN LYS LEU VAL GLU GLU ALA PRO SER PRO ILE LEU ASP
SEQRES 20 B 451 ASP GLU THR ARG ARG GLU MET GLY ASN ALA ALA VAL ARG
SEQRES 21 B 451 ALA ALA LYS ALA VAL ASN TYR GLU ASN ALA GLY THR ILE
SEQRES 22 B 451 GLU PHE ILE TYR ASP LEU ASN ASP ASN LYS PHE TYR PHE
SEQRES 23 B 451 MET GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL
SEQRES 24 B 451 THR GLU MET VAL THR GLY ILE ASP LEU VAL LYS LEU GLN
SEQRES 25 B 451 LEU GLN VAL ALA MET GLY ASP VAL LEU PRO TYR LYS GLN
SEQRES 26 B 451 GLU ASP ILE LYS LEU THR GLY HIS ALA ILE GLU PHE ARG
SEQRES 27 B 451 ILE ASN ALA GLU ASN PRO TYR LYS ASN PHE MET PRO SER
SEQRES 28 B 451 PRO GLY LYS ILE GLU GLN TYR LEU ALA PRO GLY GLY TYR
SEQRES 29 B 451 GLY VAL ARG ILE GLU SER ALA CYS TYR THR ASN TYR THR
SEQRES 30 B 451 ILE PRO PRO TYR TYR ASP SER MET VAL ALA LYS LEU ILE
SEQRES 31 B 451 ILE HIS GLU PRO THR ARG ASP GLU ALA ILE MET ALA GLY
SEQRES 32 B 451 ILE ARG ALA LEU SER GLU PHE VAL VAL LEU GLY ILE ASP
SEQRES 33 B 451 THR THR ILE PRO PHE HIS ILE LYS LEU LEU ASN ASN ASP
SEQRES 34 B 451 ILE PHE ARG SER GLY LYS PHE ASN THR ASN PHE LEU GLU
SEQRES 35 B 451 GLN ASN SER ILE MET ASN ASP GLU GLY
HET ANP A1449 31
HET MG A1450 1
HET MG A1451 1
HET CL A1452 1
HET ANP B1450 31
HET MG B1451 1
HET MG B1452 1
HET CL B1453 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
FORMUL 4 MG 4(MG 2+)
FORMUL 6 CL 2(CL 1-)
FORMUL 11 HOH *817(H2 O)
HELIX 1 1 ARG A 9 LEU A 23 1 15
HELIX 2 2 GLY A 34 LYS A 36 5 3
HELIX 3 3 ALA A 38 ALA A 44 1 7
HELIX 4 4 LEU A 54 SER A 58 5 5
HELIX 5 5 ASN A 61 THR A 72 1 12
HELIX 6 6 ASN A 87 ALA A 96 1 10
HELIX 7 7 SER A 105 ILE A 114 1 10
HELIX 8 8 ILE A 114 ALA A 125 1 12
HELIX 9 9 ASP A 139 GLY A 151 1 13
HELIX 10 10 ASP A 172 GLY A 192 1 21
HELIX 11 11 ASP A 247 VAL A 265 1 19
HELIX 12 12 GLU A 296 GLY A 305 1 10
HELIX 13 13 ASP A 307 MET A 317 1 11
HELIX 14 14 LYS A 324 ILE A 328 5 5
HELIX 15 15 ASN A 343 ASN A 347 5 5
HELIX 16 16 THR A 395 GLU A 409 1 15
HELIX 17 17 THR A 418 ASN A 427 1 10
HELIX 18 18 ASN A 428 GLY A 434 1 7
HELIX 19 19 ARG B 9 LEU B 23 1 15
HELIX 20 20 GLY B 34 LYS B 36 5 3
HELIX 21 21 ALA B 38 ALA B 44 1 7
HELIX 22 22 LEU B 54 SER B 58 5 5
HELIX 23 23 ASN B 61 THR B 72 1 12
HELIX 24 24 ASN B 87 CYS B 97 1 11
HELIX 25 25 SER B 105 ILE B 114 1 10
HELIX 26 26 ILE B 114 ALA B 125 1 12
HELIX 27 27 ASP B 139 GLY B 151 1 13
HELIX 28 28 ASP B 172 GLY B 192 1 21
HELIX 29 29 ASP B 247 VAL B 265 1 19
HELIX 30 30 GLU B 296 GLY B 305 1 10
HELIX 31 31 ASP B 307 MET B 317 1 11
HELIX 32 32 LYS B 324 ILE B 328 5 5
HELIX 33 33 ASN B 343 ASN B 347 5 5
HELIX 34 34 THR B 395 PHE B 410 1 16
HELIX 35 35 THR B 418 ASN B 427 1 10
HELIX 36 36 ASN B 428 GLY B 434 1 7
HELIX 37 37 ASN B 439 ASN B 444 1 6
HELIX 38 38 SER B 445 ASP B 449 5 5
SHEET 1 AA 5 GLU A 46 GLY A 51 0
SHEET 2 AA 5 GLN A 26 SER A 32 1 O THR A 27 N GLU A 46
SHEET 3 AA 5 LYS A 3 ILE A 6 1 O VAL A 4 N VAL A 28
SHEET 4 AA 5 GLY A 76 HIS A 78 1 O GLY A 76 N LEU A 5
SHEET 5 AA 5 LYS A 100 PHE A 101 1 O LYS A 100 N VAL A 77
SHEET 1 AB 3 ILE A 167 ALA A 170 0
SHEET 2 AB 3 VAL A 154 ALA A 158 -1 O VAL A 154 N ALA A 170
SHEET 3 AB 3 LEU A 196 LYS A 200 -1 O TYR A 197 N LYS A 157
SHEET 1 AC 8 PHE A 284 ASN A 290 0
SHEET 2 AC 8 ASN A 269 ASP A 278 -1 O THR A 272 N ASN A 290
SHEET 3 AC 8 PHE A 205 GLY A 214 -1 O ARG A 206 N TYR A 277
SHEET 4 AC 8 VAL A 220 ARG A 232 -1 O ILE A 221 N VAL A 213
SHEET 5 AC 8 GLN A 235 ALA A 241 -1 O GLN A 235 N ARG A 232
SHEET 6 AC 8 HIS A 333 ASN A 340 -1 O ALA A 334 N ALA A 241
SHEET 7 AC 8 MET A 385 GLU A 393 -1 N VAL A 386 O ILE A 339
SHEET 8 AC 8 VAL A 366 GLU A 369 -1 O ARG A 367 N ILE A 390
SHEET 1 AD 2 GLN A 357 LEU A 359 0
SHEET 2 AD 2 VAL A 411 LEU A 413 -1 O VAL A 411 N LEU A 359
SHEET 1 BA 5 GLU B 46 GLY B 51 0
SHEET 2 BA 5 GLN B 26 SER B 32 1 O THR B 27 N GLU B 46
SHEET 3 BA 5 LYS B 3 ILE B 6 1 O VAL B 4 N VAL B 28
SHEET 4 BA 5 GLY B 76 HIS B 78 1 O GLY B 76 N LEU B 5
SHEET 5 BA 5 LYS B 100 PHE B 101 1 O LYS B 100 N VAL B 77
SHEET 1 BB 3 ILE B 167 ALA B 170 0
SHEET 2 BB 3 VAL B 154 ALA B 158 -1 O VAL B 154 N ALA B 170
SHEET 3 BB 3 LEU B 196 LYS B 200 -1 O TYR B 197 N LYS B 157
SHEET 1 BC 8 LYS B 283 ASN B 290 0
SHEET 2 BC 8 ASN B 269 ASP B 278 -1 O THR B 272 N ASN B 290
SHEET 3 BC 8 PHE B 205 GLY B 214 -1 O ARG B 206 N TYR B 277
SHEET 4 BC 8 VAL B 220 ARG B 232 -1 O ILE B 221 N VAL B 213
SHEET 5 BC 8 GLN B 235 ALA B 241 -1 O GLN B 235 N ARG B 232
SHEET 6 BC 8 HIS B 333 ASN B 340 -1 O ALA B 334 N ALA B 241
SHEET 7 BC 8 MET B 385 GLU B 393 -1 N VAL B 386 O ILE B 339
SHEET 8 BC 8 VAL B 366 SER B 370 -1 O ARG B 367 N ILE B 390
SHEET 1 BD 2 GLN B 357 LEU B 359 0
SHEET 2 BD 2 VAL B 411 LEU B 413 -1 O VAL B 411 N LEU B 359
LINK OE2 GLU A 274 MG MG A1450 1555 1555 2.46
LINK OE1 GLU A 274 MG MG A1450 1555 1555 2.05
LINK OE1 GLU A 288 MG MG A1450 1555 1555 2.40
LINK OE1 GLU A 288 MG MG A1451 1555 1555 2.24
LINK OE2 GLU A 288 MG MG A1451 1555 1555 2.27
LINK O1G ANP A1449 MG MG A1450 1555 1555 1.95
LINK O2A ANP A1449 MG MG A1450 1555 1555 2.14
LINK O2G ANP A1449 MG MG A1451 1555 1555 1.76
LINK O1B ANP A1449 MG MG A1451 1555 1555 2.06
LINK MG MG A1450 O HOH A2417 1555 1555 2.23
LINK MG MG A1451 O HOH A2172 1555 1555 2.00
LINK MG MG A1451 O HOH A2266 1555 1555 1.93
LINK OE1 GLU B 274 MG MG B1451 1555 1555 1.98
LINK OE2 GLU B 274 MG MG B1451 1555 1555 2.84
LINK OE1 GLU B 288 MG MG B1451 1555 1555 2.58
LINK OE2 GLU B 288 MG MG B1452 1555 1555 2.39
LINK OE1 GLU B 288 MG MG B1452 1555 1555 2.38
LINK O2A ANP B1450 MG MG B1451 1555 1555 1.94
LINK O3G ANP B1450 MG MG B1451 1555 1555 1.91
LINK O1G ANP B1450 MG MG B1452 1555 1555 1.75
LINK O1B ANP B1450 MG MG B1452 1555 1555 1.90
LINK MG MG B1451 O HOH B2398 1555 1555 2.04
LINK MG MG B1452 O HOH B2155 1555 1555 2.15
LINK MG MG B1452 O HOH B2243 1555 1555 1.83
CISPEP 1 TYR A 152 PRO A 153 0 5.95
CISPEP 2 ALA A 241 PRO A 242 0 -12.33
CISPEP 3 TYR B 152 PRO B 153 0 3.04
CISPEP 4 ALA B 241 PRO B 242 0 -8.78
SITE 1 AC1 28 LYS B 115 ILE B 155 LYS B 157 GLY B 161
SITE 2 AC1 28 GLY B 162 GLY B 163 GLY B 164 ILE B 167
SITE 3 AC1 28 GLU B 199 LYS B 200 PHE B 201 ILE B 202
SITE 4 AC1 28 HIS B 207 GLN B 231 MET B 234 GLU B 274
SITE 5 AC1 28 ILE B 276 MET B 287 GLU B 288 ASN B 290
SITE 6 AC1 28 MG B1451 MG B1452 HOH B2155 HOH B2243
SITE 7 AC1 28 HOH B2393 HOH B2394 HOH B2397 HOH B2398
SITE 1 AC2 26 LYS A 115 ILE A 155 LYS A 157 GLY A 161
SITE 2 AC2 26 GLY A 162 GLY A 163 GLY A 164 ILE A 167
SITE 3 AC2 26 GLU A 199 LYS A 200 PHE A 201 ILE A 202
SITE 4 AC2 26 HIS A 207 GLN A 231 GLU A 274 ILE A 276
SITE 5 AC2 26 MET A 287 GLU A 288 ASN A 290 MG A1450
SITE 6 AC2 26 MG A1451 HOH A2172 HOH A2180 HOH A2266
SITE 7 AC2 26 HOH A2416 HOH A2417
SITE 1 AC3 4 GLU B 274 GLU B 288 ANP B1450 HOH B2398
SITE 1 AC4 4 GLU A 274 GLU A 288 ANP A1449 HOH A2417
SITE 1 AC5 5 GLU B 288 ASN B 290 ANP B1450 HOH B2155
SITE 2 AC5 5 HOH B2243
SITE 1 AC6 5 GLU A 288 ASN A 290 ANP A1449 HOH A2172
SITE 2 AC6 5 HOH A2266
SITE 1 AC7 4 ARG A 292 GLN A 294 VAL A 295 HOH A2270
SITE 1 AC8 4 ARG B 292 GLN B 294 VAL B 295 HOH B2247
CRYST1 78.247 63.318 105.142 90.00 103.82 90.00 P 1 21 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 0.012780 0.000000 0.003144 0.00000
SCALE2 0.000000 0.015793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009794 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
