HEADER HYDROLASE 20-JAN-09 3FX6
TITLE X-RAY CRYSTALLOGRAPHIC STUDIES ON THE COMPLEX OF CARBOXYPEPTIDASE A
TITLE 2 WITH THE INHIBITOR USING ALPHA-NITRO KETONE AS THE ZINC-BINDING GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYPEPTIDASE A1;
COMPND 3 CHAIN: A, C, E;
COMPND 4 EC: 3.4.17.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 TISSUE: BOVINE PANCREAS
KEYWDS ALPHA-NITRO KETONE, INHIBITOR, HYDROLASE, CARBOXYPEPTIDASE, METAL-
KEYWDS 2 BINDING, METALLOPROTEASE, POLYMORPHISM, PROTEASE, SECRETED, ZINC,
KEYWDS 3 ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.F.WANG,J.Y.JIN,G.R.TIAN
REVDAT 3 01-NOV-23 3FX6 1 REMARK SEQADV LINK
REVDAT 2 01-NOV-17 3FX6 1 REMARK
REVDAT 1 25-AUG-09 3FX6 0
JRNL AUTH S.F.WANG,G.R.TIAN,W.Z.ZHANG,J.Y.JIN
JRNL TITL CHARACTERIZATION OF ALPHA-NITROMETHYL KETONE AS A NEW
JRNL TITL 2 ZINC-BINDING GROUP BASED ON STRUCTURAL ANALYSIS OF ITS
JRNL TITL 3 COMPLEX WITH CARBOXYPEPTIDASE A
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 5009 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19646864
JRNL DOI 10.1016/J.BMCL.2009.07.060
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 60986
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 SET) : 0.207
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3261
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.27
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4504
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 238
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7320
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 544
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.20000
REMARK 3 B22 (A**2) : -0.76000
REMARK 3 B33 (A**2) : 0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.56000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.350
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.22
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MASK
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST SQUARES
REMARK 3 PROCEDURE
REMARK 4
REMARK 4 3FX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSCILLATION
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67762
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 36.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 49.1156
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.08100
REMARK 200 R SYM FOR SHELL (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 30.39
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1HDQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M LITHIUM CHLORIDE, 0.02%
REMARK 280 GLUTARALDEHYDE, 0.025M TRIS, PH7.5, MICRODIALYSIS, TEMPERATURE
REMARK 280 277K
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 29.87600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 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 PRO A 205 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG C 272 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 PRO E 205 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 129 -168.68 -79.59
REMARK 500 THR A 133 -93.38 -122.46
REMARK 500 SER A 134 -134.62 -84.99
REMARK 500 TYR A 198 121.82 68.24
REMARK 500 SER A 199 -19.18 141.47
REMARK 500 GLN A 200 71.50 54.71
REMARK 500 PRO A 205 139.11 -21.53
REMARK 500 TYR A 206 104.89 77.98
REMARK 500 TYR A 248 170.25 171.54
REMARK 500 LEU A 271 -173.98 -67.37
REMARK 500 ARG A 272 155.90 -38.97
REMARK 500 ASP A 273 135.31 80.50
REMARK 500 LEU A 280 50.07 -94.69
REMARK 500 THR C 133 -167.10 -70.16
REMARK 500 SER C 135 45.30 -92.93
REMARK 500 TYR C 198 122.23 67.98
REMARK 500 SER C 199 -16.42 138.60
REMARK 500 GLN C 200 72.70 52.97
REMARK 500 PRO C 205 140.35 -23.45
REMARK 500 TYR C 206 100.88 81.03
REMARK 500 ILE C 247 -85.75 -108.33
REMARK 500 LEU C 271 -172.93 -63.41
REMARK 500 ARG C 272 154.82 -41.56
REMARK 500 ASP C 273 137.93 81.30
REMARK 500 LEU C 280 47.09 -92.07
REMARK 500 SER E 134 -72.93 -44.09
REMARK 500 SER E 135 66.72 -102.12
REMARK 500 TYR E 198 127.36 61.40
REMARK 500 SER E 199 -20.42 137.11
REMARK 500 PRO E 205 136.98 -21.07
REMARK 500 TYR E 206 102.93 80.19
REMARK 500 TYR E 248 168.75 177.63
REMARK 500 ARG E 272 149.58 -34.48
REMARK 500 ASP E 273 138.14 82.35
REMARK 500 LEU E 280 50.21 -90.22
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 ZN A 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 ND1
REMARK 620 2 GLU A 72 OE1 118.3
REMARK 620 3 GLU A 72 OE2 93.7 57.4
REMARK 620 4 HIS A 196 ND1 96.6 101.3 158.7
REMARK 620 5 BPX A 311 OAQ 72.0 123.7 67.1 134.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 69 ND1
REMARK 620 2 GLU C 72 OE1 127.0
REMARK 620 3 GLU C 72 OE2 91.6 56.4
REMARK 620 4 HIS C 196 ND1 96.4 105.4 160.9
REMARK 620 5 BPX C 311 OAQ 71.2 123.1 71.7 127.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 69 ND1
REMARK 620 2 GLU E 72 OE1 125.3
REMARK 620 3 GLU E 72 OE2 94.5 56.7
REMARK 620 4 HIS E 196 ND1 98.1 100.0 156.5
REMARK 620 5 BPX E 311 OAQ 71.8 125.8 72.3 130.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPX A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPX C 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BPX E 311
DBREF 3FX6 A 1 307 UNP P00730 CBPA1_BOVIN 111 417
DBREF 3FX6 C 1 307 UNP P00730 CBPA1_BOVIN 111 417
DBREF 3FX6 E 1 307 UNP P00730 CBPA1_BOVIN 111 417
SEQADV 3FX6 VAL A 305 UNP P00730 LEU 415 CONFLICT
SEQADV 3FX6 VAL C 305 UNP P00730 LEU 415 CONFLICT
SEQADV 3FX6 VAL E 305 UNP P00730 LEU 415 CONFLICT
SEQRES 1 A 307 ALA ARG SER THR ASN THR PHE ASN TYR ALA THR TYR HIS
SEQRES 2 A 307 THR LEU ASP GLU ILE TYR ASP PHE MET ASP LEU LEU VAL
SEQRES 3 A 307 ALA GLU HIS PRO GLN LEU VAL SER LYS LEU GLN ILE GLY
SEQRES 4 A 307 ARG SER TYR GLU GLY ARG PRO ILE TYR VAL LEU LYS PHE
SEQRES 5 A 307 SER THR GLY GLY SER ASN ARG PRO ALA ILE TRP ILE ASP
SEQRES 6 A 307 LEU GLY ILE HIS SER ARG GLU TRP ILE THR GLN ALA THR
SEQRES 7 A 307 GLY VAL TRP PHE ALA LYS LYS PHE THR GLU ASP TYR GLY
SEQRES 8 A 307 GLN ASP PRO SER PHE THR ALA ILE LEU ASP SER MET ASP
SEQRES 9 A 307 ILE PHE LEU GLU ILE VAL THR ASN PRO ASP GLY PHE ALA
SEQRES 10 A 307 PHE THR HIS SER GLN ASN ARG LEU TRP ARG LYS THR ARG
SEQRES 11 A 307 SER VAL THR SER SER SER LEU CYS VAL GLY VAL ASP ALA
SEQRES 12 A 307 ASN ARG ASN TRP ASP ALA GLY PHE GLY LYS ALA GLY ALA
SEQRES 13 A 307 SER SER SER PRO CYS SER GLU THR TYR HIS GLY LYS TYR
SEQRES 14 A 307 ALA ASN SER GLU VAL GLU VAL LYS SER ILE VAL ASP PHE
SEQRES 15 A 307 VAL LYS ASP HIS GLY ASN PHE LYS ALA PHE LEU SER ILE
SEQRES 16 A 307 HIS SER TYR SER GLN LEU LEU LEU TYR PRO TYR GLY TYR
SEQRES 17 A 307 THR THR GLN SER ILE PRO ASP LYS THR GLU LEU ASN GLN
SEQRES 18 A 307 VAL ALA LYS SER ALA VAL GLU ALA LEU LYS SER LEU TYR
SEQRES 19 A 307 GLY THR SER TYR LYS TYR GLY SER ILE ILE THR THR ILE
SEQRES 20 A 307 TYR GLN ALA SER GLY GLY SER ILE ASP TRP SER TYR ASN
SEQRES 21 A 307 GLN GLY ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP
SEQRES 22 A 307 THR GLY ARG TYR GLY PHE LEU LEU PRO ALA SER GLN ILE
SEQRES 23 A 307 ILE PRO THR ALA GLN GLU THR TRP LEU GLY VAL LEU THR
SEQRES 24 A 307 ILE MET GLU HIS THR VAL ASN ASN
SEQRES 1 C 307 ALA ARG SER THR ASN THR PHE ASN TYR ALA THR TYR HIS
SEQRES 2 C 307 THR LEU ASP GLU ILE TYR ASP PHE MET ASP LEU LEU VAL
SEQRES 3 C 307 ALA GLU HIS PRO GLN LEU VAL SER LYS LEU GLN ILE GLY
SEQRES 4 C 307 ARG SER TYR GLU GLY ARG PRO ILE TYR VAL LEU LYS PHE
SEQRES 5 C 307 SER THR GLY GLY SER ASN ARG PRO ALA ILE TRP ILE ASP
SEQRES 6 C 307 LEU GLY ILE HIS SER ARG GLU TRP ILE THR GLN ALA THR
SEQRES 7 C 307 GLY VAL TRP PHE ALA LYS LYS PHE THR GLU ASP TYR GLY
SEQRES 8 C 307 GLN ASP PRO SER PHE THR ALA ILE LEU ASP SER MET ASP
SEQRES 9 C 307 ILE PHE LEU GLU ILE VAL THR ASN PRO ASP GLY PHE ALA
SEQRES 10 C 307 PHE THR HIS SER GLN ASN ARG LEU TRP ARG LYS THR ARG
SEQRES 11 C 307 SER VAL THR SER SER SER LEU CYS VAL GLY VAL ASP ALA
SEQRES 12 C 307 ASN ARG ASN TRP ASP ALA GLY PHE GLY LYS ALA GLY ALA
SEQRES 13 C 307 SER SER SER PRO CYS SER GLU THR TYR HIS GLY LYS TYR
SEQRES 14 C 307 ALA ASN SER GLU VAL GLU VAL LYS SER ILE VAL ASP PHE
SEQRES 15 C 307 VAL LYS ASP HIS GLY ASN PHE LYS ALA PHE LEU SER ILE
SEQRES 16 C 307 HIS SER TYR SER GLN LEU LEU LEU TYR PRO TYR GLY TYR
SEQRES 17 C 307 THR THR GLN SER ILE PRO ASP LYS THR GLU LEU ASN GLN
SEQRES 18 C 307 VAL ALA LYS SER ALA VAL GLU ALA LEU LYS SER LEU TYR
SEQRES 19 C 307 GLY THR SER TYR LYS TYR GLY SER ILE ILE THR THR ILE
SEQRES 20 C 307 TYR GLN ALA SER GLY GLY SER ILE ASP TRP SER TYR ASN
SEQRES 21 C 307 GLN GLY ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP
SEQRES 22 C 307 THR GLY ARG TYR GLY PHE LEU LEU PRO ALA SER GLN ILE
SEQRES 23 C 307 ILE PRO THR ALA GLN GLU THR TRP LEU GLY VAL LEU THR
SEQRES 24 C 307 ILE MET GLU HIS THR VAL ASN ASN
SEQRES 1 E 307 ALA ARG SER THR ASN THR PHE ASN TYR ALA THR TYR HIS
SEQRES 2 E 307 THR LEU ASP GLU ILE TYR ASP PHE MET ASP LEU LEU VAL
SEQRES 3 E 307 ALA GLU HIS PRO GLN LEU VAL SER LYS LEU GLN ILE GLY
SEQRES 4 E 307 ARG SER TYR GLU GLY ARG PRO ILE TYR VAL LEU LYS PHE
SEQRES 5 E 307 SER THR GLY GLY SER ASN ARG PRO ALA ILE TRP ILE ASP
SEQRES 6 E 307 LEU GLY ILE HIS SER ARG GLU TRP ILE THR GLN ALA THR
SEQRES 7 E 307 GLY VAL TRP PHE ALA LYS LYS PHE THR GLU ASP TYR GLY
SEQRES 8 E 307 GLN ASP PRO SER PHE THR ALA ILE LEU ASP SER MET ASP
SEQRES 9 E 307 ILE PHE LEU GLU ILE VAL THR ASN PRO ASP GLY PHE ALA
SEQRES 10 E 307 PHE THR HIS SER GLN ASN ARG LEU TRP ARG LYS THR ARG
SEQRES 11 E 307 SER VAL THR SER SER SER LEU CYS VAL GLY VAL ASP ALA
SEQRES 12 E 307 ASN ARG ASN TRP ASP ALA GLY PHE GLY LYS ALA GLY ALA
SEQRES 13 E 307 SER SER SER PRO CYS SER GLU THR TYR HIS GLY LYS TYR
SEQRES 14 E 307 ALA ASN SER GLU VAL GLU VAL LYS SER ILE VAL ASP PHE
SEQRES 15 E 307 VAL LYS ASP HIS GLY ASN PHE LYS ALA PHE LEU SER ILE
SEQRES 16 E 307 HIS SER TYR SER GLN LEU LEU LEU TYR PRO TYR GLY TYR
SEQRES 17 E 307 THR THR GLN SER ILE PRO ASP LYS THR GLU LEU ASN GLN
SEQRES 18 E 307 VAL ALA LYS SER ALA VAL GLU ALA LEU LYS SER LEU TYR
SEQRES 19 E 307 GLY THR SER TYR LYS TYR GLY SER ILE ILE THR THR ILE
SEQRES 20 E 307 TYR GLN ALA SER GLY GLY SER ILE ASP TRP SER TYR ASN
SEQRES 21 E 307 GLN GLY ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP
SEQRES 22 E 307 THR GLY ARG TYR GLY PHE LEU LEU PRO ALA SER GLN ILE
SEQRES 23 E 307 ILE PRO THR ALA GLN GLU THR TRP LEU GLY VAL LEU THR
SEQRES 24 E 307 ILE MET GLU HIS THR VAL ASN ASN
HET ZN A 309 1
HET BPX A 311 19
HET ZN C 309 1
HET BPX C 311 19
HET ZN E 309 1
HET BPX E 311 19
HETNAM ZN ZINC ION
HETNAM BPX (2R)-4,4-DIHYDROXY-5-NITRO-2-(PHENYLMETHYL)PENTANOIC
HETNAM 2 BPX ACID
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 BPX 3(C12 H15 N O6)
FORMUL 10 HOH *544(H2 O)
HELIX 1 1 THR A 14 HIS A 29 1 16
HELIX 2 2 GLU A 72 TYR A 90 1 19
HELIX 3 3 ASP A 93 MET A 103 1 11
HELIX 4 4 ASN A 112 GLN A 122 1 11
HELIX 5 5 ASP A 142 ASN A 146 5 5
HELIX 6 6 GLU A 173 GLY A 187 1 15
HELIX 7 7 ASP A 215 GLY A 235 1 21
HELIX 8 8 ILE A 243 ILE A 247 1 5
HELIX 9 9 GLY A 253 GLN A 261 1 9
HELIX 10 10 PRO A 282 SER A 284 5 3
HELIX 11 11 GLN A 285 ASN A 306 1 22
HELIX 12 12 THR C 14 HIS C 29 1 16
HELIX 13 13 GLU C 72 TYR C 90 1 19
HELIX 14 14 ASP C 93 MET C 103 1 11
HELIX 15 15 ASN C 112 GLN C 122 1 11
HELIX 16 16 ASP C 142 ASN C 146 5 5
HELIX 17 17 GLU C 173 GLY C 187 1 15
HELIX 18 18 ASP C 215 GLY C 235 1 21
HELIX 19 19 ILE C 243 ILE C 247 1 5
HELIX 20 20 GLY C 253 GLN C 261 1 9
HELIX 21 21 PRO C 282 SER C 284 5 3
HELIX 22 22 GLN C 285 ASN C 306 1 22
HELIX 23 23 THR E 14 HIS E 29 1 16
HELIX 24 24 GLU E 72 TYR E 90 1 19
HELIX 25 25 ASP E 93 MET E 103 1 11
HELIX 26 26 ASN E 112 GLN E 122 1 11
HELIX 27 27 ASP E 142 ASN E 146 5 5
HELIX 28 28 GLU E 173 GLY E 187 1 15
HELIX 29 29 ASP E 215 GLY E 235 1 21
HELIX 30 30 ILE E 243 ILE E 247 1 5
HELIX 31 31 GLY E 253 GLN E 261 1 9
HELIX 32 32 PRO E 282 SER E 284 5 3
HELIX 33 33 GLN E 285 ASN E 306 1 22
SHEET 1 A 8 VAL A 33 ARG A 40 0
SHEET 2 A 8 PRO A 46 PHE A 52 -1 O VAL A 49 N LEU A 36
SHEET 3 A 8 ASP A 104 GLU A 108 -1 O ILE A 105 N PHE A 52
SHEET 4 A 8 ALA A 61 LEU A 66 1 N ILE A 62 O PHE A 106
SHEET 5 A 8 PHE A 189 HIS A 196 1 O LEU A 193 N TRP A 63
SHEET 6 A 8 TYR A 265 GLU A 270 1 O PHE A 269 N HIS A 196
SHEET 7 A 8 LEU A 201 TYR A 204 -1 N LEU A 203 O THR A 268
SHEET 8 A 8 LYS A 239 SER A 242 1 O LYS A 239 N LEU A 202
SHEET 1 B 8 VAL C 33 ARG C 40 0
SHEET 2 B 8 PRO C 46 PHE C 52 -1 O LYS C 51 N SER C 34
SHEET 3 B 8 ASP C 104 GLU C 108 -1 O LEU C 107 N LEU C 50
SHEET 4 B 8 ALA C 61 LEU C 66 1 N ILE C 62 O PHE C 106
SHEET 5 B 8 PHE C 189 HIS C 196 1 O LYS C 190 N ALA C 61
SHEET 6 B 8 TYR C 265 GLU C 270 1 O PHE C 269 N HIS C 196
SHEET 7 B 8 LEU C 201 TYR C 204 -1 N LEU C 203 O THR C 268
SHEET 8 B 8 LYS C 239 SER C 242 1 O LYS C 239 N LEU C 202
SHEET 1 C 8 VAL E 33 ARG E 40 0
SHEET 2 C 8 PRO E 46 PHE E 52 -1 O LYS E 51 N SER E 34
SHEET 3 C 8 ASP E 104 GLU E 108 -1 O LEU E 107 N LEU E 50
SHEET 4 C 8 ALA E 61 LEU E 66 1 N ILE E 64 O GLU E 108
SHEET 5 C 8 PHE E 189 SER E 197 1 O LYS E 190 N ALA E 61
SHEET 6 C 8 TYR E 265 LEU E 271 1 O PHE E 269 N HIS E 196
SHEET 7 C 8 LEU E 201 TYR E 204 -1 N LEU E 201 O GLU E 270
SHEET 8 C 8 LYS E 239 SER E 242 1 O LYS E 239 N LEU E 202
SSBOND 1 CYS A 138 CYS A 161 1555 1555 2.03
SSBOND 2 CYS C 138 CYS C 161 1555 1555 2.03
SSBOND 3 CYS E 138 CYS E 161 1555 1555 2.03
LINK ND1 HIS A 69 ZN ZN A 309 1555 1555 2.06
LINK OE1 GLU A 72 ZN ZN A 309 1555 1555 2.21
LINK OE2 GLU A 72 ZN ZN A 309 1555 1555 2.34
LINK ND1 HIS A 196 ZN ZN A 309 1555 1555 2.11
LINK ZN ZN A 309 OAQ BPX A 311 1555 1555 2.23
LINK ND1 HIS C 69 ZN ZN C 309 1555 1555 2.17
LINK OE1 GLU C 72 ZN ZN C 309 1555 1555 2.25
LINK OE2 GLU C 72 ZN ZN C 309 1555 1555 2.38
LINK ND1 HIS C 196 ZN ZN C 309 1555 1555 2.19
LINK ZN ZN C 309 OAQ BPX C 311 1555 1555 2.31
LINK ND1 HIS E 69 ZN ZN E 309 1555 1555 2.14
LINK OE1 GLU E 72 ZN ZN E 309 1555 1555 2.28
LINK OE2 GLU E 72 ZN ZN E 309 1555 1555 2.34
LINK ND1 HIS E 196 ZN ZN E 309 1555 1555 2.15
LINK ZN ZN E 309 OAQ BPX E 311 1555 1555 2.32
SITE 1 AC1 4 HIS A 69 GLU A 72 HIS A 196 BPX A 311
SITE 1 AC2 13 HIS A 69 ARG A 71 GLU A 72 ARG A 127
SITE 2 AC2 13 ASN A 144 ARG A 145 HIS A 196 TYR A 248
SITE 3 AC2 13 THR A 268 GLU A 270 PHE A 279 ZN A 309
SITE 4 AC2 13 HOH A 334
SITE 1 AC3 4 HIS C 69 GLU C 72 HIS C 196 BPX C 311
SITE 1 AC4 13 HIS C 69 ARG C 71 GLU C 72 ARG C 127
SITE 2 AC4 13 ARG C 145 HIS C 196 ILE C 243 TYR C 248
SITE 3 AC4 13 THR C 268 GLU C 270 PHE C 279 ZN C 309
SITE 4 AC4 13 HOH C 363
SITE 1 AC5 4 HIS E 69 GLU E 72 HIS E 196 BPX E 311
SITE 1 AC6 14 HIS E 69 ARG E 71 GLU E 72 ARG E 127
SITE 2 AC6 14 ASN E 144 ARG E 145 HIS E 196 ILE E 243
SITE 3 AC6 14 TYR E 248 THR E 268 GLU E 270 PHE E 279
SITE 4 AC6 14 ZN E 309 HOH E 322
CRYST1 73.356 59.752 99.514 90.00 104.04 90.00 P 1 21 1 6
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 0.013632 0.000000 0.003409 0.00000
SCALE2 0.000000 0.016736 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010358 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
