HEADER TRANSFERASE 05-DEC-05 2F9I
TITLE CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE SUBUNIT OF ACC FROM
TITLE 2 STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT
COMPND 3 ALPHA;
COMPND 4 CHAIN: A, C;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT
COMPND 8 BETA;
COMPND 9 CHAIN: B, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: ACCA,ACCD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST-T7-202;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 13 ORGANISM_TAXID: 1280;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PDEST-T7-202
KEYWDS ZINC RIBBON, CROTONASE SUPERFAMILY, SPIRAL DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.BILDER
REVDAT 5 30-AUG-23 2F9I 1 REMARK SEQADV LINK
REVDAT 4 24-JUL-19 2F9I 1 REMARK
REVDAT 3 18-OCT-17 2F9I 1 REMARK
REVDAT 2 24-FEB-09 2F9I 1 VERSN
REVDAT 1 05-DEC-06 2F9I 0
JRNL AUTH P.BILDER,S.LIGHTLE,G.BAINBRIDGE,J.OHREN,B.FINZEL,F.SUN,
JRNL AUTH 2 S.HOLLEY,L.AL-KASSIM,C.SPESSARD,M.MELNICK,M.NEWCOMER,
JRNL AUTH 3 G.L.WALDROP
JRNL TITL THE STRUCTURE OF THE CARBOXYLTRANSFERASE COMPONENT OF
JRNL TITL 2 ACETYL-COA CARBOXYLASE REVEALS A ZINC-BINDING MOTIF UNIQUE
JRNL TITL 3 TO THE BACTERIAL ENZYME.
JRNL REF BIOCHEMISTRY V. 45 1712 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16460018
JRNL DOI 10.1021/BI0520479
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 90017
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9030
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) : 1.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5073
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 558
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8685
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 583
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.434
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8639 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11570 ; 1.606 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1110 ; 4.884 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 364 ;37.848 ;24.176
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1501 ;12.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;14.619 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1285 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6408 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4456 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6012 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 624 ; 0.141 ; 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): 55 ; 0.378 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.158 ; 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): 5689 ; 1.332 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8763 ; 1.562 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3312 ; 2.595 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2807 ; 3.835 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 34 A 307 1
REMARK 3 1 C 34 C 307 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2075 ; 0.200 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 2075 ; 1.180 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 29 B 283 2
REMARK 3 1 D 29 D 283 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1019 ; 0.120 ; 0.050
REMARK 3 MEDIUM POSITIONAL 2 B (A): 919 ; 0.340 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 1019 ; 1.220 ; 0.500
REMARK 3 MEDIUM THERMAL 2 B (A**2): 919 ; 1.570 ; 2.000
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: NULL
REMARK 4
REMARK 4 2F9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90018
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: DM 4.2, CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ON3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG-400, 0.1M HEPES, PH 8.0, 0.2M
REMARK 280 MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 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 95.48950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.42950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 95.48950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.42950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER IN THE ASYMMETRIC UNIT
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 SER A 21
REMARK 465 GLN A 22
REMARK 465 ASP A 23
REMARK 465 LYS A 24
REMARK 465 ASN A 25
REMARK 465 ASP A 26
REMARK 465 VAL A 27
REMARK 465 ASP A 28
REMARK 465 LEU A 29
REMARK 465 MET B 1
REMARK 465 PHE B 2
REMARK 465 LYS B 3
REMARK 465 ASP B 4
REMARK 465 PHE B 5
REMARK 465 PHE B 6
REMARK 465 ASN B 7
REMARK 465 ARG B 8
REMARK 465 THR B 9
REMARK 465 LYS B 10
REMARK 465 LYS B 11
REMARK 465 LYS B 12
REMARK 465 LYS B 13
REMARK 465 TYR B 14
REMARK 465 LEU B 15
REMARK 465 THR B 16
REMARK 465 VAL B 17
REMARK 465 GLN B 18
REMARK 465 ASP B 19
REMARK 465 SER B 20
REMARK 465 LYS B 21
REMARK 465 ASN B 22
REMARK 465 ASN B 23
REMARK 465 ASP B 24
REMARK 465 VAL B 25
REMARK 465 MET C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 LEU C -5
REMARK 465 VAL C -4
REMARK 465 PRO C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 SER C 17
REMARK 465 LEU C 18
REMARK 465 LYS C 19
REMARK 465 GLU C 20
REMARK 465 SER C 21
REMARK 465 GLN C 22
REMARK 465 ASP C 23
REMARK 465 LYS C 24
REMARK 465 ASN C 25
REMARK 465 ASP C 26
REMARK 465 VAL C 27
REMARK 465 ASP C 28
REMARK 465 LEU C 29
REMARK 465 GLN C 30
REMARK 465 GLU C 31
REMARK 465 GLU C 32
REMARK 465 ILE C 33
REMARK 465 MET D 1
REMARK 465 PHE D 2
REMARK 465 LYS D 3
REMARK 465 ASP D 4
REMARK 465 PHE D 5
REMARK 465 PHE D 6
REMARK 465 ASN D 7
REMARK 465 ARG D 8
REMARK 465 THR D 9
REMARK 465 LYS D 10
REMARK 465 LYS D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 TYR D 14
REMARK 465 LEU D 15
REMARK 465 THR D 16
REMARK 465 VAL D 17
REMARK 465 GLN D 18
REMARK 465 ASP D 19
REMARK 465 SER D 20
REMARK 465 LYS D 21
REMARK 465 ASN D 22
REMARK 465 ASN D 23
REMARK 465 ASP D 24
REMARK 465 VAL D 25
REMARK 465 PRO D 26
REMARK 465 ALA D 27
REMARK 465 GLY D 28
REMARK 465 THR D 284
REMARK 465 LYS D 285
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 MET A 1 CG SD CE
REMARK 470 GLU A 16 CG CD OE1 OE2
REMARK 470 LEU A 18 CG CD1 CD2
REMARK 470 GLN A 30 CG CD OE1 NE2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 MET C 1 CG SD CE
REMARK 470 LYS C 6 CG CD CE NZ
REMARK 470 PHE C 9 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 ILE C 11 CG1 CG2 CD1
REMARK 470 ARG C 12 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 13 CG OD1 ND2
REMARK 470 LYS C 14 CG CD CE NZ
REMARK 470 ILE C 15 CG1 CG2 CD1
REMARK 470 GLU C 16 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LEU A -5 CB
REMARK 480 VAL A -4 CB
REMARK 480 PRO A -3 CB
REMARK 480 ARG A -2 CB
REMARK 480 SER A 0 CB
REMARK 480 MET A 1 CB
REMARK 480 PHE A 9 O
REMARK 480 GLU A 10 CB
REMARK 480 ARG A 12 CB
REMARK 480 ASN A 13 O
REMARK 480 LYS A 14 O
REMARK 480 ILE A 15 C O
REMARK 480 GLU A 16 O
REMARK 480 SER A 17 N
REMARK 480 LEU A 18 C O
REMARK 480 LYS A 46 CD CE
REMARK 480 THR A 49 CG2
REMARK 480 ASN A 50 ND2
REMARK 480 GLN A 63 NE2
REMARK 480 LYS A 115 CD
REMARK 480 LYS A 118 CD CE NZ
REMARK 480 MET A 127 CE
REMARK 480 LEU A 230 CD1
REMARK 480 LYS A 232 CG CD CE
REMARK 480 ASP A 233 CB OD1
REMARK 480 ASN A 235 CB CG ND2
REMARK 480 LEU A 236 CD2
REMARK 480 GLN A 253 CG
REMARK 480 LEU A 265 CD2
REMARK 480 LEU A 277 CD1
REMARK 480 ALA A 285 CB
REMARK 480 GLU A 291 CB CG CD OE1
REMARK 480 LYS B 43 CG CD
REMARK 480 LYS B 97 CD
REMARK 480 GLU B 99 CG
REMARK 480 LYS B 100 CG CD
REMARK 480 GLU B 154 CG CD OE2
REMARK 480 ARG B 234 CG CD NE
REMARK 480 VAL B 235 CG1
REMARK 480 GLN B 238 CG NE2
REMARK 480 GLU B 242 CG
REMARK 480 LYS B 243 CE NZ
REMARK 480 VAL B 283 CG1
REMARK 480 THR B 284 CG2
REMARK 480 MET C 1 CB
REMARK 480 PHE C 9 O
REMARK 480 GLU C 10 CB
REMARK 480 ARG C 12 CB
REMARK 480 ASN C 13 O
REMARK 480 LYS C 14 O
REMARK 480 ILE C 15 C O
REMARK 480 GLU C 16 O
REMARK 480 LEU C 36 CB
REMARK 480 GLU C 37 CB CG CD OE1
REMARK 480 ALA C 38 CB
REMARK 480 SER C 39 O
REMARK 480 LEU C 40 O CD1
REMARK 480 LYS C 45 CD NZ
REMARK 480 LYS C 46 CG CD CE
REMARK 480 THR C 49 CG2
REMARK 480 LYS C 52 CG CD
REMARK 480 ASP C 55 CB
REMARK 480 ASP C 116 O OD1
REMARK 480 LYS C 118 CB CG CD CE
REMARK 480 GLU C 131 OE1
REMARK 480 LYS C 163 CE NZ
REMARK 480 LYS C 185 CE NZ
REMARK 480 LEU C 230 CD2
REMARK 480 TRP C 231 CD1
REMARK 480 LYS C 232 CD
REMARK 480 ASN C 235 CB
REMARK 480 GLN C 253 CG CD NE2
REMARK 480 LEU C 265 CD2
REMARK 480 GLU C 291 CG
REMARK 480 ILE C 298 CG2
REMARK 480 MET D 30 CE
REMARK 480 LYS D 32 CE NZ
REMARK 480 LYS D 38 CG CD
REMARK 480 ILE D 39 CG2
REMARK 480 LYS D 43 CG CD CE
REMARK 480 GLU D 44 OE2
REMARK 480 CYS D 55 N
REMARK 480 GLU D 68 CG
REMARK 480 LYS D 81 NZ
REMARK 480 GLU D 96 CG
REMARK 480 GLU D 99 CB
REMARK 480 LYS D 108 NZ
REMARK 480 MET D 137 CE
REMARK 480 ARG D 234 NH1
REMARK 480 GLU D 242 CB CG
REMARK 480 LYS D 243 CB CD
REMARK 480 ASN D 267 OD1 ND2
REMARK 480 GLN D 281 CD NE2
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 OD2 ASP C 119 O HOH C 473 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A -5 CA LEU A -5 CB 0.351
REMARK 500 VAL A -4 CB VAL A -4 CG1 0.554
REMARK 500 VAL A -4 CB VAL A -4 CG2 0.681
REMARK 500 ARG A -2 CA ARG A -2 CB -0.147
REMARK 500 ARG A -2 CB ARG A -2 CG 0.597
REMARK 500 ARG A 12 CB ARG A 12 CG 0.411
REMARK 500 ILE A 15 CA ILE A 15 C 0.325
REMARK 500 GLU A 16 C GLU A 16 O -0.277
REMARK 500 GLU A 16 C SER A 17 N 0.309
REMARK 500 SER A 17 N SER A 17 CA 0.324
REMARK 500 LEU A 18 CA LEU A 18 C 0.406
REMARK 500 ASP A 34 CB ASP A 34 CG 0.191
REMARK 500 ARG A 42 NE ARG A 42 CZ 0.081
REMARK 500 ARG A 42 CZ ARG A 42 NH1 0.121
REMARK 500 LYS A 46 CE LYS A 46 NZ 0.258
REMARK 500 LYS A 52 CD LYS A 52 CE 0.212
REMARK 500 LYS A 52 CE LYS A 52 NZ -0.217
REMARK 500 GLU A 64 CD GLU A 64 OE2 -0.096
REMARK 500 LYS A 115 CD LYS A 115 CE 0.234
REMARK 500 LYS A 232 CE LYS A 232 NZ -0.847
REMARK 500 ASP A 233 CB ASP A 233 CG 0.321
REMARK 500 ASP A 233 CG ASP A 233 OD1 -0.348
REMARK 500 ASN A 235 CG ASN A 235 OD1 -0.152
REMARK 500 GLN A 253 CG GLN A 253 CD 0.336
REMARK 500 GLU A 291 CD GLU A 291 OE2 -0.572
REMARK 500 LYS B 43 CD LYS B 43 CE 0.208
REMARK 500 LYS B 97 CD LYS B 97 CE 0.420
REMARK 500 GLU B 99 CG GLU B 99 CD 0.290
REMARK 500 LYS B 100 CD LYS B 100 CE 0.203
REMARK 500 GLU B 154 CD GLU B 154 OE1 0.111
REMARK 500 ARG B 234 CB ARG B 234 CG 0.189
REMARK 500 GLN B 238 CG GLN B 238 CD 0.281
REMARK 500 GLU B 242 CB GLU B 242 CG -0.318
REMARK 500 GLU B 242 CG GLU B 242 CD 0.155
REMARK 500 VAL B 283 N VAL B 283 CA 0.148
REMARK 500 LYS C 14 C LYS C 14 O 0.245
REMARK 500 LYS C 14 C ILE C 15 N 0.206
REMARK 500 ILE C 15 CA ILE C 15 C 0.229
REMARK 500 ASP C 34 CA ASP C 34 C 0.216
REMARK 500 LEU C 36 CA LEU C 36 CB 0.437
REMARK 500 LEU C 36 CB LEU C 36 CG 0.662
REMARK 500 LEU C 36 CG LEU C 36 CD1 0.460
REMARK 500 LEU C 36 CG LEU C 36 CD2 0.245
REMARK 500 GLU C 37 CD GLU C 37 OE2 -0.171
REMARK 500 ARG C 42 CZ ARG C 42 NH1 0.101
REMARK 500 LYS C 45 CD LYS C 45 CE 0.435
REMARK 500 LYS C 45 CE LYS C 45 NZ -0.348
REMARK 500 LYS C 46 CE LYS C 46 NZ -0.248
REMARK 500 LYS C 52 CD LYS C 52 CE -0.536
REMARK 500 LYS C 52 CE LYS C 52 NZ -0.344
REMARK 500
REMARK 500 THIS ENTRY HAS 69 BOND DEVIATIONS.
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 LEU A -5 CB - CA - C ANGL. DEV. = -13.4 DEGREES
REMARK 500 LEU A -5 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU A -5 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 VAL A -4 CA - CB - CG2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 ILE A 15 CB - CA - C ANGL. DEV. = -19.3 DEGREES
REMARK 500 GLU A 16 CA - C - O ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU A 16 CA - C - N ANGL. DEV. = -21.0 DEGREES
REMARK 500 SER A 17 N - CA - CB ANGL. DEV. = -18.9 DEGREES
REMARK 500 LEU A 18 CB - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU A 18 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 ASP A 34 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP A 34 CB - CG - OD1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP A 34 CB - CG - OD2 ANGL. DEV. = -18.2 DEGREES
REMARK 500 LEU A 36 CB - CG - CD1 ANGL. DEV. = -14.1 DEGREES
REMARK 500 LYS A 46 CD - CE - NZ ANGL. DEV. = -20.4 DEGREES
REMARK 500 ASN A 50 OD1 - CG - ND2 ANGL. DEV. = -29.7 DEGREES
REMARK 500 ASN A 50 CB - CG - ND2 ANGL. DEV. = 30.2 DEGREES
REMARK 500 GLU A 64 OE1 - CD - OE2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LYS A 232 CD - CE - NZ ANGL. DEV. = -20.6 DEGREES
REMARK 500 ASP A 233 OD1 - CG - OD2 ANGL. DEV. = 29.1 DEGREES
REMARK 500 ASP A 233 CB - CG - OD2 ANGL. DEV. = -29.4 DEGREES
REMARK 500 GLN A 253 CG - CD - OE1 ANGL. DEV. = -17.8 DEGREES
REMARK 500 ASP A 288 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 GLU A 291 OE1 - CD - OE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 LYS B 97 CD - CE - NZ ANGL. DEV. = -14.3 DEGREES
REMARK 500 GLU B 99 CG - CD - OE1 ANGL. DEV. = -30.6 DEGREES
REMARK 500 GLU B 99 CG - CD - OE2 ANGL. DEV. = -18.4 DEGREES
REMARK 500 GLU B 154 OE1 - CD - OE2 ANGL. DEV. = -14.2 DEGREES
REMARK 500 GLU B 154 CG - CD - OE1 ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG B 234 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG B 234 NE - CZ - NH2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 GLN B 238 CG - CD - OE1 ANGL. DEV. = -24.3 DEGREES
REMARK 500 GLN B 238 CG - CD - NE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 GLU B 242 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 MET C 1 N - CA - CB ANGL. DEV. = 22.2 DEGREES
REMARK 500 LYS C 14 CA - C - O ANGL. DEV. = -18.4 DEGREES
REMARK 500 LYS C 14 CA - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 LYS C 14 O - C - N ANGL. DEV. = -24.2 DEGREES
REMARK 500 ILE C 15 N - CA - C ANGL. DEV. = -23.8 DEGREES
REMARK 500 ILE C 15 CA - C - N ANGL. DEV. = 18.5 DEGREES
REMARK 500 ILE C 15 O - C - N ANGL. DEV. = -21.8 DEGREES
REMARK 500 GLU C 16 C - N - CA ANGL. DEV. = 20.3 DEGREES
REMARK 500 GLU C 16 CA - C - O ANGL. DEV. = -28.6 DEGREES
REMARK 500 ASP C 34 CB - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 ASP C 34 CA - C - O ANGL. DEV. = 13.4 DEGREES
REMARK 500 LEU C 36 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU C 36 CA - CB - CG ANGL. DEV. = -34.4 DEGREES
REMARK 500 LEU C 36 CD1 - CG - CD2 ANGL. DEV. = -23.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 90 ANGLE DEVIATIONS.
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 31 -29.47 -37.90
REMARK 500 ASN A 87 -42.56 -135.54
REMARK 500 PHE A 88 -47.85 -153.14
REMARK 500 ASP A 155 79.32 -159.94
REMARK 500 SER A 198 -138.11 48.93
REMARK 500 LYS A 232 15.45 53.11
REMARK 500 LYS A 245 69.90 64.54
REMARK 500 ASP A 259 148.83 -173.72
REMARK 500 ASP A 271 81.00 -156.45
REMARK 500 ALA B 27 130.59 63.63
REMARK 500 MET B 134 15.07 59.44
REMARK 500 ALA B 164 108.40 -163.86
REMARK 500 SER B 212 -117.49 -134.89
REMARK 500 LYS C 14 38.09 -99.07
REMARK 500 ILE C 15 -77.41 -132.50
REMARK 500 ASN C 87 -41.41 -142.01
REMARK 500 PHE C 88 -48.79 -151.17
REMARK 500 ASP C 155 79.40 -160.35
REMARK 500 SER C 198 -142.69 55.17
REMARK 500 LYS C 232 17.27 57.18
REMARK 500 LYS C 245 70.00 63.84
REMARK 500 ASP C 271 85.98 -157.67
REMARK 500 SER D 93 -1.63 70.21
REMARK 500 SER D 212 -118.40 -135.90
REMARK 500 LYS D 225 -0.90 69.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASP A 34 0.07 SIDE CHAIN
REMARK 500 GLN A 253 0.18 SIDE CHAIN
REMARK 500 GLU B 99 0.24 SIDE CHAIN
REMARK 500 ARG B 234 0.15 SIDE CHAIN
REMARK 500 GLN B 238 0.22 SIDE CHAIN
REMARK 500 GLU C 131 0.08 SIDE CHAIN
REMARK 500 ASN C 235 0.18 SIDE CHAIN
REMARK 500 GLU C 291 0.09 SIDE CHAIN
REMARK 500 GLU D 68 0.25 SIDE CHAIN
REMARK 500 GLU D 96 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 15 -12.43
REMARK 500 GLU A 16 -11.99
REMARK 500 ASN C 13 -18.15
REMARK 500 LYS C 14 -45.38
REMARK 500 ILE C 15 14.25
REMARK 500 SER C 39 10.62
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 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 33 SG
REMARK 620 2 CYS B 36 SG 107.4
REMARK 620 3 CYS B 52 SG 107.3 104.6
REMARK 620 4 CYS B 55 SG 114.3 109.2 113.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 33 SG
REMARK 620 2 CYS D 36 SG 111.6
REMARK 620 3 CYS D 52 SG 106.4 108.6
REMARK 620 4 CYS D 55 SG 108.5 105.9 116.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CARBOXYLTRANSFERASE SUBUNIT OF ACC FROM
REMARK 900 ESCHERICHIA COLI
DBREF 2F9I A 1 314 GB 49244968 CAG43429 1 314
DBREF 2F9I C 1 314 GB 49244968 CAG43429 1 314
DBREF 2F9I B 1 285 GB 49242071 CAG40770 1 285
DBREF 2F9I D 1 285 GB 49242071 CAG40770 1 285
SEQADV 2F9I MET A -12 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I HIS A -11 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS A -10 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS A -9 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS A -8 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS A -7 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS A -6 GB 49244968 EXPRESSION TAG
SEQADV 2F9I LEU A -5 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I VAL A -4 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I PRO A -3 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I ARG A -2 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I GLY A -1 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I SER A 0 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I MET C -12 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I HIS C -11 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS C -10 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS C -9 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS C -8 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS C -7 GB 49244968 EXPRESSION TAG
SEQADV 2F9I HIS C -6 GB 49244968 EXPRESSION TAG
SEQADV 2F9I LEU C -5 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I VAL C -4 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I PRO C -3 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I ARG C -2 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I GLY C -1 GB 49244968 CLONING ARTIFACT
SEQADV 2F9I SER C 0 GB 49244968 CLONING ARTIFACT
SEQRES 1 A 327 MET HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG GLY SER
SEQRES 2 A 327 MET LEU ASP PHE GLU LYS PRO LEU PHE GLU ILE ARG ASN
SEQRES 3 A 327 LYS ILE GLU SER LEU LYS GLU SER GLN ASP LYS ASN ASP
SEQRES 4 A 327 VAL ASP LEU GLN GLU GLU ILE ASP MET LEU GLU ALA SER
SEQRES 5 A 327 LEU GLU ARG GLU THR LYS LYS ILE TYR THR ASN LEU LYS
SEQRES 6 A 327 PRO TRP ASP ARG VAL GLN ILE ALA ARG LEU GLN GLU ARG
SEQRES 7 A 327 PRO THR THR LEU ASP TYR ILE PRO TYR ILE PHE ASP SER
SEQRES 8 A 327 PHE MET GLU LEU HIS GLY ASP ARG ASN PHE ARG ASP ASP
SEQRES 9 A 327 PRO ALA MET ILE GLY GLY ILE GLY PHE LEU ASN GLY ARG
SEQRES 10 A 327 ALA VAL THR VAL ILE GLY GLN GLN ARG GLY LYS ASP THR
SEQRES 11 A 327 LYS ASP ASN ILE TYR ARG ASN PHE GLY MET ALA HIS PRO
SEQRES 12 A 327 GLU GLY TYR ARG LYS ALA LEU ARG LEU MET LYS GLN ALA
SEQRES 13 A 327 GLU LYS PHE ASN ARG PRO ILE PHE THR PHE ILE ASP THR
SEQRES 14 A 327 LYS GLY ALA TYR PRO GLY LYS ALA ALA GLU GLU ARG GLY
SEQRES 15 A 327 GLN SER GLU SER ILE ALA THR ASN LEU ILE GLU MET ALA
SEQRES 16 A 327 SER LEU LYS VAL PRO VAL ILE ALA ILE VAL ILE GLY GLU
SEQRES 17 A 327 GLY GLY SER GLY GLY ALA LEU GLY ILE GLY ILE ALA ASN
SEQRES 18 A 327 LYS VAL LEU MET LEU GLU ASN SER THR TYR SER VAL ILE
SEQRES 19 A 327 SER PRO GLU GLY ALA ALA ALA LEU LEU TRP LYS ASP SER
SEQRES 20 A 327 ASN LEU ALA LYS ILE ALA ALA GLU THR MET LYS ILE THR
SEQRES 21 A 327 ALA HIS ASP ILE LYS GLN LEU GLY ILE ILE ASP ASP VAL
SEQRES 22 A 327 ILE SER GLU PRO LEU GLY GLY ALA HIS LYS ASP ILE GLU
SEQRES 23 A 327 GLN GLN ALA LEU ALA ILE LYS SER ALA PHE VAL ALA GLN
SEQRES 24 A 327 LEU ASP SER LEU GLU SER LEU SER ARG ASP GLU ILE ALA
SEQRES 25 A 327 ASN ASP ARG PHE GLU LYS PHE ARG ASN ILE GLY SER TYR
SEQRES 26 A 327 ILE GLU
SEQRES 1 B 285 MET PHE LYS ASP PHE PHE ASN ARG THR LYS LYS LYS LYS
SEQRES 2 B 285 TYR LEU THR VAL GLN ASP SER LYS ASN ASN ASP VAL PRO
SEQRES 3 B 285 ALA GLY ILE MET THR LYS CYS PRO LYS CYS LYS LYS ILE
SEQRES 4 B 285 MET TYR THR LYS GLU LEU ALA GLU ASN LEU ASN VAL CYS
SEQRES 5 B 285 PHE ASN CYS ASP HIS HIS ILE ALA LEU THR ALA TYR LYS
SEQRES 6 B 285 ARG ILE GLU ALA ILE SER ASP GLU GLY SER PHE THR GLU
SEQRES 7 B 285 PHE ASP LYS GLY MET THR SER ALA ASN PRO LEU ASP PHE
SEQRES 8 B 285 PRO SER TYR LEU GLU LYS ILE GLU LYS ASP GLN GLN LYS
SEQRES 9 B 285 THR GLY LEU LYS GLU ALA VAL VAL THR GLY THR ALA GLN
SEQRES 10 B 285 LEU ASP GLY MET LYS PHE GLY VAL ALA VAL MET ASP SER
SEQRES 11 B 285 ARG PHE ARG MET GLY SER MET GLY SER VAL ILE GLY GLU
SEQRES 12 B 285 LYS ILE CYS ARG ILE ILE ASP TYR CYS THR GLU ASN ARG
SEQRES 13 B 285 LEU PRO PHE ILE LEU PHE SER ALA SER GLY GLY ALA ARG
SEQRES 14 B 285 MET GLN GLU GLY ILE ILE SER LEU MET GLN MET GLY LYS
SEQRES 15 B 285 THR SER VAL SER LEU LYS ARG HIS SER ASP ALA GLY LEU
SEQRES 16 B 285 LEU TYR ILE SER TYR LEU THR HIS PRO THR THR GLY GLY
SEQRES 17 B 285 VAL SER ALA SER PHE ALA SER VAL GLY ASP ILE ASN LEU
SEQRES 18 B 285 SER GLU PRO LYS ALA LEU ILE GLY PHE ALA GLY ARG ARG
SEQRES 19 B 285 VAL ILE GLU GLN THR ILE ASN GLU LYS LEU PRO ASP ASP
SEQRES 20 B 285 PHE GLN THR ALA GLU PHE LEU LEU GLU HIS GLY GLN LEU
SEQRES 21 B 285 ASP LYS VAL VAL HIS ARG ASN ASP MET ARG GLN THR LEU
SEQRES 22 B 285 SER GLU ILE LEU LYS ILE HIS GLN GLU VAL THR LYS
SEQRES 1 C 327 MET HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG GLY SER
SEQRES 2 C 327 MET LEU ASP PHE GLU LYS PRO LEU PHE GLU ILE ARG ASN
SEQRES 3 C 327 LYS ILE GLU SER LEU LYS GLU SER GLN ASP LYS ASN ASP
SEQRES 4 C 327 VAL ASP LEU GLN GLU GLU ILE ASP MET LEU GLU ALA SER
SEQRES 5 C 327 LEU GLU ARG GLU THR LYS LYS ILE TYR THR ASN LEU LYS
SEQRES 6 C 327 PRO TRP ASP ARG VAL GLN ILE ALA ARG LEU GLN GLU ARG
SEQRES 7 C 327 PRO THR THR LEU ASP TYR ILE PRO TYR ILE PHE ASP SER
SEQRES 8 C 327 PHE MET GLU LEU HIS GLY ASP ARG ASN PHE ARG ASP ASP
SEQRES 9 C 327 PRO ALA MET ILE GLY GLY ILE GLY PHE LEU ASN GLY ARG
SEQRES 10 C 327 ALA VAL THR VAL ILE GLY GLN GLN ARG GLY LYS ASP THR
SEQRES 11 C 327 LYS ASP ASN ILE TYR ARG ASN PHE GLY MET ALA HIS PRO
SEQRES 12 C 327 GLU GLY TYR ARG LYS ALA LEU ARG LEU MET LYS GLN ALA
SEQRES 13 C 327 GLU LYS PHE ASN ARG PRO ILE PHE THR PHE ILE ASP THR
SEQRES 14 C 327 LYS GLY ALA TYR PRO GLY LYS ALA ALA GLU GLU ARG GLY
SEQRES 15 C 327 GLN SER GLU SER ILE ALA THR ASN LEU ILE GLU MET ALA
SEQRES 16 C 327 SER LEU LYS VAL PRO VAL ILE ALA ILE VAL ILE GLY GLU
SEQRES 17 C 327 GLY GLY SER GLY GLY ALA LEU GLY ILE GLY ILE ALA ASN
SEQRES 18 C 327 LYS VAL LEU MET LEU GLU ASN SER THR TYR SER VAL ILE
SEQRES 19 C 327 SER PRO GLU GLY ALA ALA ALA LEU LEU TRP LYS ASP SER
SEQRES 20 C 327 ASN LEU ALA LYS ILE ALA ALA GLU THR MET LYS ILE THR
SEQRES 21 C 327 ALA HIS ASP ILE LYS GLN LEU GLY ILE ILE ASP ASP VAL
SEQRES 22 C 327 ILE SER GLU PRO LEU GLY GLY ALA HIS LYS ASP ILE GLU
SEQRES 23 C 327 GLN GLN ALA LEU ALA ILE LYS SER ALA PHE VAL ALA GLN
SEQRES 24 C 327 LEU ASP SER LEU GLU SER LEU SER ARG ASP GLU ILE ALA
SEQRES 25 C 327 ASN ASP ARG PHE GLU LYS PHE ARG ASN ILE GLY SER TYR
SEQRES 26 C 327 ILE GLU
SEQRES 1 D 285 MET PHE LYS ASP PHE PHE ASN ARG THR LYS LYS LYS LYS
SEQRES 2 D 285 TYR LEU THR VAL GLN ASP SER LYS ASN ASN ASP VAL PRO
SEQRES 3 D 285 ALA GLY ILE MET THR LYS CYS PRO LYS CYS LYS LYS ILE
SEQRES 4 D 285 MET TYR THR LYS GLU LEU ALA GLU ASN LEU ASN VAL CYS
SEQRES 5 D 285 PHE ASN CYS ASP HIS HIS ILE ALA LEU THR ALA TYR LYS
SEQRES 6 D 285 ARG ILE GLU ALA ILE SER ASP GLU GLY SER PHE THR GLU
SEQRES 7 D 285 PHE ASP LYS GLY MET THR SER ALA ASN PRO LEU ASP PHE
SEQRES 8 D 285 PRO SER TYR LEU GLU LYS ILE GLU LYS ASP GLN GLN LYS
SEQRES 9 D 285 THR GLY LEU LYS GLU ALA VAL VAL THR GLY THR ALA GLN
SEQRES 10 D 285 LEU ASP GLY MET LYS PHE GLY VAL ALA VAL MET ASP SER
SEQRES 11 D 285 ARG PHE ARG MET GLY SER MET GLY SER VAL ILE GLY GLU
SEQRES 12 D 285 LYS ILE CYS ARG ILE ILE ASP TYR CYS THR GLU ASN ARG
SEQRES 13 D 285 LEU PRO PHE ILE LEU PHE SER ALA SER GLY GLY ALA ARG
SEQRES 14 D 285 MET GLN GLU GLY ILE ILE SER LEU MET GLN MET GLY LYS
SEQRES 15 D 285 THR SER VAL SER LEU LYS ARG HIS SER ASP ALA GLY LEU
SEQRES 16 D 285 LEU TYR ILE SER TYR LEU THR HIS PRO THR THR GLY GLY
SEQRES 17 D 285 VAL SER ALA SER PHE ALA SER VAL GLY ASP ILE ASN LEU
SEQRES 18 D 285 SER GLU PRO LYS ALA LEU ILE GLY PHE ALA GLY ARG ARG
SEQRES 19 D 285 VAL ILE GLU GLN THR ILE ASN GLU LYS LEU PRO ASP ASP
SEQRES 20 D 285 PHE GLN THR ALA GLU PHE LEU LEU GLU HIS GLY GLN LEU
SEQRES 21 D 285 ASP LYS VAL VAL HIS ARG ASN ASP MET ARG GLN THR LEU
SEQRES 22 D 285 SER GLU ILE LEU LYS ILE HIS GLN GLU VAL THR LYS
HET ZN B 601 1
HET ZN D 602 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 HOH *583(H2 O)
HELIX 1 1 LEU A 2 PHE A 4 5 3
HELIX 2 2 GLU A 5 SER A 17 1 13
HELIX 3 3 GLU A 32 ASN A 50 1 19
HELIX 4 4 LYS A 52 ARG A 61 1 10
HELIX 5 5 THR A 67 PHE A 76 1 10
HELIX 6 6 ASP A 116 ARG A 123 1 8
HELIX 7 7 ASN A 124 MET A 127 5 4
HELIX 8 8 HIS A 129 PHE A 146 1 18
HELIX 9 9 GLY A 162 ARG A 168 1 7
HELIX 10 10 GLY A 169 SER A 183 1 15
HELIX 11 11 GLY A 197 GLY A 203 1 7
HELIX 12 12 SER A 222 TRP A 231 1 10
HELIX 13 13 ASP A 233 ASN A 235 5 3
HELIX 14 14 LEU A 236 LYS A 245 1 10
HELIX 15 15 THR A 247 LEU A 254 1 8
HELIX 16 16 GLY A 267 LYS A 270 5 4
HELIX 17 17 ASP A 271 SER A 289 1 19
HELIX 18 18 SER A 294 ASN A 308 1 15
HELIX 19 19 THR B 42 ASN B 48 1 7
HELIX 20 20 THR B 62 ILE B 70 1 9
HELIX 21 21 SER B 93 GLY B 106 1 14
HELIX 22 22 PHE B 132 SER B 136 5 5
HELIX 23 23 GLY B 138 ASN B 155 1 18
HELIX 24 24 ARG B 169 GLN B 171 5 3
HELIX 25 25 GLU B 172 ALA B 193 1 22
HELIX 26 26 GLY B 207 ALA B 211 1 5
HELIX 27 27 SER B 212 VAL B 216 5 5
HELIX 28 28 GLY B 232 ASN B 241 1 10
HELIX 29 29 THR B 250 HIS B 257 1 8
HELIX 30 30 HIS B 265 ASN B 267 5 3
HELIX 31 31 ASP B 268 HIS B 280 1 13
HELIX 32 32 GLU C 5 GLU C 16 1 12
HELIX 33 33 ASP C 34 ASN C 50 1 17
HELIX 34 34 LYS C 52 ARG C 61 1 10
HELIX 35 35 THR C 67 PHE C 76 1 10
HELIX 36 36 ASP C 116 ARG C 123 1 8
HELIX 37 37 ASN C 124 MET C 127 5 4
HELIX 38 38 HIS C 129 PHE C 146 1 18
HELIX 39 39 GLY C 162 ARG C 168 1 7
HELIX 40 40 GLY C 169 SER C 183 1 15
HELIX 41 41 GLY C 197 GLY C 203 1 7
HELIX 42 42 SER C 222 TRP C 231 1 10
HELIX 43 43 ASP C 233 ASN C 235 5 3
HELIX 44 44 LEU C 236 LYS C 245 1 10
HELIX 45 45 THR C 247 LEU C 254 1 8
HELIX 46 46 GLY C 267 LYS C 270 5 4
HELIX 47 47 ASP C 271 SER C 289 1 19
HELIX 48 48 SER C 294 ASN C 308 1 15
HELIX 49 49 THR D 42 ASN D 48 1 7
HELIX 50 50 THR D 62 ILE D 70 1 9
HELIX 51 51 SER D 93 GLY D 106 1 14
HELIX 52 52 PHE D 132 SER D 136 5 5
HELIX 53 53 GLY D 138 ASN D 155 1 18
HELIX 54 54 ARG D 169 GLN D 171 5 3
HELIX 55 55 GLU D 172 ALA D 193 1 22
HELIX 56 56 GLY D 207 ALA D 211 1 5
HELIX 57 57 SER D 212 VAL D 216 5 5
HELIX 58 58 GLY D 232 ASN D 241 1 10
HELIX 59 59 THR D 250 HIS D 257 1 8
HELIX 60 60 HIS D 265 HIS D 280 1 16
SHEET 1 A 7 ASP A 77 GLU A 81 0
SHEET 2 A 7 MET A 94 LEU A 101 -1 O ILE A 98 N MET A 80
SHEET 3 A 7 ARG A 104 GLN A 111 -1 O GLY A 110 N ILE A 95
SHEET 4 A 7 ILE A 150 THR A 156 1 O PHE A 151 N ILE A 109
SHEET 5 A 7 VAL A 188 GLY A 196 1 O ILE A 189 N ILE A 150
SHEET 6 A 7 LYS A 209 LEU A 213 1 O LEU A 211 N ALA A 190
SHEET 7 A 7 ASP A 259 ILE A 261 1 O ILE A 261 N MET A 212
SHEET 1 B 2 TYR A 312 ILE A 313 0
SHEET 2 B 2 THR B 84 SER B 85 -1 O THR B 84 N ILE A 313
SHEET 1 C 2 MET B 30 LYS B 32 0
SHEET 2 C 2 ILE B 39 TYR B 41 -1 O MET B 40 N THR B 31
SHEET 1 D 6 THR B 77 PHE B 79 0
SHEET 2 D 6 VAL B 111 LEU B 118 -1 O THR B 115 N THR B 77
SHEET 3 D 6 MET B 121 MET B 128 -1 O VAL B 125 N GLY B 114
SHEET 4 D 6 PHE B 159 SER B 165 1 O PHE B 162 N ALA B 126
SHEET 5 D 6 TYR B 197 THR B 206 1 O TYR B 200 N LEU B 161
SHEET 6 D 6 ILE B 228 GLY B 229 1 O GLY B 229 N THR B 205
SHEET 1 E 7 THR B 77 PHE B 79 0
SHEET 2 E 7 VAL B 111 LEU B 118 -1 O THR B 115 N THR B 77
SHEET 3 E 7 MET B 121 MET B 128 -1 O VAL B 125 N GLY B 114
SHEET 4 E 7 PHE B 159 SER B 165 1 O PHE B 162 N ALA B 126
SHEET 5 E 7 TYR B 197 THR B 206 1 O TYR B 200 N LEU B 161
SHEET 6 E 7 ILE B 219 SER B 222 1 O LEU B 221 N SER B 199
SHEET 7 E 7 LYS B 262 VAL B 263 1 O LYS B 262 N SER B 222
SHEET 1 F 7 ASP C 77 GLU C 81 0
SHEET 2 F 7 MET C 94 LEU C 101 -1 O ILE C 98 N MET C 80
SHEET 3 F 7 ARG C 104 GLN C 111 -1 O GLY C 110 N ILE C 95
SHEET 4 F 7 ILE C 150 THR C 156 1 O PHE C 151 N THR C 107
SHEET 5 F 7 VAL C 188 GLY C 196 1 O ILE C 189 N ILE C 150
SHEET 6 F 7 LYS C 209 LEU C 213 1 O LEU C 211 N ALA C 190
SHEET 7 F 7 ASP C 259 ILE C 261 1 O ILE C 261 N MET C 212
SHEET 1 G 2 TYR C 312 ILE C 313 0
SHEET 2 G 2 THR D 84 SER D 85 -1 O THR D 84 N ILE C 313
SHEET 1 H 2 MET D 30 LYS D 32 0
SHEET 2 H 2 ILE D 39 TYR D 41 -1 O MET D 40 N THR D 31
SHEET 1 I 6 THR D 77 PHE D 79 0
SHEET 2 I 6 VAL D 111 LEU D 118 -1 O THR D 113 N PHE D 79
SHEET 3 I 6 MET D 121 MET D 128 -1 O VAL D 125 N GLY D 114
SHEET 4 I 6 PHE D 159 SER D 165 1 O PHE D 162 N ALA D 126
SHEET 5 I 6 TYR D 197 THR D 206 1 O TYR D 200 N LEU D 161
SHEET 6 I 6 ILE D 228 GLY D 229 1 O GLY D 229 N THR D 205
SHEET 1 J 7 THR D 77 PHE D 79 0
SHEET 2 J 7 VAL D 111 LEU D 118 -1 O THR D 113 N PHE D 79
SHEET 3 J 7 MET D 121 MET D 128 -1 O VAL D 125 N GLY D 114
SHEET 4 J 7 PHE D 159 SER D 165 1 O PHE D 162 N ALA D 126
SHEET 5 J 7 TYR D 197 THR D 206 1 O TYR D 200 N LEU D 161
SHEET 6 J 7 ILE D 219 SER D 222 1 O LEU D 221 N SER D 199
SHEET 7 J 7 LYS D 262 VAL D 263 1 O LYS D 262 N SER D 222
LINK SG CYS B 33 ZN ZN B 601 1555 1555 2.24
LINK SG CYS B 36 ZN ZN B 601 1555 1555 2.42
LINK SG CYS B 52 ZN ZN B 601 1555 1555 2.24
LINK SG CYS B 55 ZN ZN B 601 1555 1555 2.24
LINK SG CYS D 33 ZN ZN D 602 1555 1555 2.25
LINK SG CYS D 36 ZN ZN D 602 1555 1555 2.45
LINK SG CYS D 52 ZN ZN D 602 1555 1555 2.24
LINK SG CYS D 55 ZN ZN D 602 1555 1555 2.31
CISPEP 1 HIS B 203 PRO B 204 0 -11.04
CISPEP 2 HIS D 203 PRO D 204 0 -11.26
SITE 1 AC1 4 CYS B 33 CYS B 36 CYS B 52 CYS B 55
SITE 1 AC2 4 CYS D 33 CYS D 36 CYS D 52 CYS D 55
CRYST1 190.979 50.859 149.639 90.00 113.51 90.00 C 1 2 1 8
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 0.005236 0.000000 0.002278 0.00000
SCALE2 0.000000 0.019662 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
