HEADER HYDROLASE(ALPHA-AMINOACYLPEPTIDE) 01-AUG-90 1LAP
TITLE MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOSOL AMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.11.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE(ALPHA-AMINOACYLPEPTIDE)
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.BURLEY,P.R.DAVID,A.TAYLOR,W.N.LIPSCOMB
REVDAT 6 14-FEB-24 1LAP 1 REMARK
REVDAT 5 03-FEB-21 1LAP 1 AUTHOR JRNL REMARK SEQADV
REVDAT 5 2 1 LINK
REVDAT 4 13-JUL-11 1LAP 1 VERSN
REVDAT 3 24-FEB-09 1LAP 1 VERSN
REVDAT 2 01-APR-03 1LAP 1 JRNL
REVDAT 1 15-OCT-91 1LAP 0
JRNL AUTH S.K.BURLEY,P.R.DAVID,A.TAYLOR,W.N.LIPSCOMB
JRNL TITL MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-A
JRNL TITL 2 RESOLUTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 87 6878 1990
JRNL REFN ISSN 0027-8424
JRNL PMID 2395881
JRNL DOI 10.1073/PNAS.87.17.6878
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.JURNAK,A.RICH,L.VANLOON-KLAASSEN,H.BLOEMENDAL,A.TAYLOR,
REMARK 1 AUTH 2 F.H.CARPENTER
REMARK 1 TITL PRELIMINARY X-RAY STUDY OF LEUCINE AMINOPEPTIDASE (BOVINE
REMARK 1 TITL 2 LENS), AN OLIGOMERIC METALLOENZYME
REMARK 1 REF J.MOL.BIOL. V. 112 149 1977
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 3671
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 3.188
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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: NULL
REMARK 4
REMARK 4 1LAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 60.90000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 60.90000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.90000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 60.90000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 60.90000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 60.90000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 23270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 93520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -607.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 132.50000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 66.25000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 114.74837
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 66.25000
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 114.74837
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 60.90000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 132.50000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 60.90000
REMARK 350 BIOMT1 6 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 60.90000
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 GLU A 12
REMARK 465 LYS A 13
REMARK 465 GLU A 14
REMARK 465 ASP A 485
REMARK 465 SER A 486
REMARK 465 ALA A 487
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 HZ3 LYS A 250 ZN ZN A 489 1.22
REMARK 500 HE21 GLN A 101 HH22 ARG A 464 1.24
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 HIS A 83 NE2 HIS A 83 CD2 -0.078
REMARK 500 HIS A 405 NE2 HIS A 405 CD2 -0.071
REMARK 500 HIS A 442 NE2 HIS A 442 CD2 -0.080
REMARK 500 HIS A 447 NE2 HIS A 447 CD2 -0.081
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 30 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 TYR A 55 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TRP A 82 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 82 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 82 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 115 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR A 128 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 GLU A 129 CB - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 GLU A 129 N - CA - C ANGL. DEV. = 24.1 DEGREES
REMARK 500 GLU A 129 CA - C - O ANGL. DEV. = -12.9 DEGREES
REMARK 500 TYR A 130 CA - CB - CG ANGL. DEV. = -11.6 DEGREES
REMARK 500 TYR A 130 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 137 CG - CD - NE ANGL. DEV. = 19.0 DEGREES
REMARK 500 ARG A 137 CD - NE - CZ ANGL. DEV. = -12.1 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 168 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 169 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 203 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP A 207 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 207 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 255 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 CYS A 303 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A 336 NH1 - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 336 NE - CZ - NH2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ILE A 338 CA - CB - CG1 ANGL. DEV. = -14.3 DEGREES
REMARK 500 THR A 361 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 TRP A 381 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 381 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 TRP A 383 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 383 CE2 - CD2 - CG ANGL. DEV. = -7.0 DEGREES
REMARK 500 LEU A 386 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG A 396 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 VAL A 397 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 VAL A 397 N - CA - CB ANGL. DEV. = -17.0 DEGREES
REMARK 500 TRP A 398 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 398 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 399 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 399 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 LEU A 402 CB - CG - CD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP A 412 CA - C - N ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU A 415 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 TRP A 445 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 445 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 MET A 454 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 470 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 470 NE - CZ - NH2 ANGL. DEV. = 7.3 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 ASP A 16 -70.04 -77.04
REMARK 500 ASP A 115 86.01 -156.20
REMARK 500 TYR A 130 78.29 52.92
REMARK 500 LYS A 197 38.10 -83.55
REMARK 500 ASP A 291 48.70 37.88
REMARK 500 ALA A 333 52.60 -98.11
REMARK 500 LEU A 402 79.77 -109.94
REMARK 500 ASP A 412 69.94 -49.02
REMARK 500 CYS A 413 -79.96 -29.70
REMARK 500 GLN A 414 -117.62 51.78
REMARK 500 PRO A 443 2.44 -68.15
REMARK 500 LYS A 444 82.42 -152.50
REMARK 500 LYS A 457 -72.15 -122.41
REMARK 500 PRO A 471 45.04 -102.96
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 TYR A 128 0.08 SIDE CHAIN
REMARK 500 TYR A 130 0.07 SIDE CHAIN
REMARK 500 ARG A 137 0.27 SIDE CHAIN
REMARK 500 PHE A 247 0.08 SIDE CHAIN
REMARK 500 PHE A 478 0.10 SIDE CHAIN
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 489 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 250 NZ
REMARK 620 2 ASP A 255 OD1 166.8
REMARK 620 3 ASP A 273 OD1 84.9 86.4
REMARK 620 4 GLU A 334 OE1 101.5 90.3 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 488 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255 OD1
REMARK 620 2 ASP A 332 OD2 93.1
REMARK 620 3 ASP A 332 O 173.8 82.8
REMARK 620 4 GLU A 334 OE2 102.7 125.3 83.4
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 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 489
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AT THE TIME OF DEPOSITION THE SEQUENCE PRESENTED IN PIR
REMARK 999 ENTRY APBOL DIFFERS FROM THE SEQUENCE PRESENTED IN THIS
REMARK 999 ENTRY. THE SEQUENCE WAS REVISED USING INFORMATION FROM
REMARK 999 THE C-DNA CLONE OF BOVINE KIDNEY LEUCINE AMINOPEPTIDASE
REMARK 999 (B. WALLNER, A. TAYLOR (1991) SUBMITTED).
DBREF 1LAP A 1 487 UNP P00727 AMPL_BOVIN 1 487
SEQADV 1LAP PRO A 45 UNP P00727 SER 45 CONFLICT
SEQRES 1 A 487 THR LYS GLY LEU VAL LEU GLY ILE TYR SER LYS GLU LYS
SEQRES 2 A 487 GLU GLU ASP GLU PRO GLN PHE THR SER ALA GLY GLU ASN
SEQRES 3 A 487 PHE ASN LYS LEU VAL SER GLY LYS LEU ARG GLU ILE LEU
SEQRES 4 A 487 ASN ILE SER GLY PRO PRO LEU LYS ALA GLY LYS THR ARG
SEQRES 5 A 487 THR PHE TYR GLY LEU HIS GLU ASP PHE PRO SER VAL VAL
SEQRES 6 A 487 VAL VAL GLY LEU GLY LYS LYS THR ALA GLY ILE ASP GLU
SEQRES 7 A 487 GLN GLU ASN TRP HIS GLU GLY LYS GLU ASN ILE ARG ALA
SEQRES 8 A 487 ALA VAL ALA ALA GLY CYS ARG GLN ILE GLN ASP LEU GLU
SEQRES 9 A 487 ILE PRO SER VAL GLU VAL ASP PRO CYS GLY ASP ALA GLN
SEQRES 10 A 487 ALA ALA ALA GLU GLY ALA VAL LEU GLY LEU TYR GLU TYR
SEQRES 11 A 487 ASP ASP LEU LYS GLN LYS ARG LYS VAL VAL VAL SER ALA
SEQRES 12 A 487 LYS LEU HIS GLY SER GLU ASP GLN GLU ALA TRP GLN ARG
SEQRES 13 A 487 GLY VAL LEU PHE ALA SER GLY GLN ASN LEU ALA ARG ARG
SEQRES 14 A 487 LEU MET GLU THR PRO ALA ASN GLU MET THR PRO THR LYS
SEQRES 15 A 487 PHE ALA GLU ILE VAL GLU GLU ASN LEU LYS SER ALA SER
SEQRES 16 A 487 ILE LYS THR ASP VAL PHE ILE ARG PRO LYS SER TRP ILE
SEQRES 17 A 487 GLU GLU GLN GLU MET GLY SER PHE LEU SER VAL ALA LYS
SEQRES 18 A 487 GLY SER GLU GLU PRO PRO VAL PHE LEU GLU ILE HIS TYR
SEQRES 19 A 487 LYS GLY SER PRO ASN ALA SER GLU PRO PRO LEU VAL PHE
SEQRES 20 A 487 VAL GLY LYS GLY ILE THR PHE ASP SER GLY GLY ILE SER
SEQRES 21 A 487 ILE LYS ALA ALA ALA ASN MET ASP LEU MET ARG ALA ASP
SEQRES 22 A 487 MET GLY GLY ALA ALA THR ILE CYS SER ALA ILE VAL SER
SEQRES 23 A 487 ALA ALA LYS LEU ASP LEU PRO ILE ASN ILE VAL GLY LEU
SEQRES 24 A 487 ALA PRO LEU CYS GLU ASN MET PRO SER GLY LYS ALA ASN
SEQRES 25 A 487 LYS PRO GLY ASP VAL VAL ARG ALA ARG ASN GLY LYS THR
SEQRES 26 A 487 ILE GLN VAL ASP ASN THR ASP ALA GLU GLY ARG LEU ILE
SEQRES 27 A 487 LEU ALA ASP ALA LEU CYS TYR ALA HIS THR PHE ASN PRO
SEQRES 28 A 487 LYS VAL ILE ILE ASN ALA ALA THR LEU THR GLY ALA MET
SEQRES 29 A 487 ASP ILE ALA LEU GLY SER GLY ALA THR GLY VAL PHE THR
SEQRES 30 A 487 ASN SER SER TRP LEU TRP ASN LYS LEU PHE GLU ALA SER
SEQRES 31 A 487 ILE GLU THR GLY ASP ARG VAL TRP ARG MET PRO LEU PHE
SEQRES 32 A 487 GLU HIS TYR THR ARG GLN VAL ILE ASP CYS GLN LEU ALA
SEQRES 33 A 487 ASP VAL ASN ASN ILE GLY LYS TYR ARG SER ALA GLY ALA
SEQRES 34 A 487 CYS THR ALA ALA ALA PHE LEU LYS GLU PHE VAL THR HIS
SEQRES 35 A 487 PRO LYS TRP ALA HIS LEU ASP ILE ALA GLY VAL MET THR
SEQRES 36 A 487 ASN LYS ASP GLU VAL PRO TYR LEU ARG LYS GLY MET ALA
SEQRES 37 A 487 GLY ARG PRO THR ARG THR LEU ILE GLU PHE LEU PHE ARG
SEQRES 38 A 487 PHE SER GLN ASP SER ALA
HET ZN A 488 1
HET ZN A 489 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 THR A 21 VAL A 31 1 11
HELIX 2 2 GLY A 33 GLY A 43 1 11
HELIX 3 3 GLU A 84 LEU A 103 1 20
HELIX 4 4 ASP A 115 LEU A 127 1 13
HELIX 5 5 ASP A 150 THR A 173 1 24
HELIX 6 6 THR A 179 SER A 195 1 17
HELIX 7 7 PRO A 204 GLN A 211 1 8
HELIX 8 8 MET A 213 LYS A 221 1 9
HELIX 9 9 ASN A 266 ASP A 273 5 8
HELIX 10 10 MET A 274 LEU A 290 1 17
HELIX 11 11 ALA A 333 PHE A 349 1 17
HELIX 12 12 THR A 361 GLY A 369 1 9
HELIX 13 13 SER A 379 GLY A 394 1 16
HELIX 14 14 PHE A 403 ILE A 411 1 9
HELIX 15 15 ALA A 427 GLU A 438 1 12
HELIX 16 16 ALA A 451 VAL A 453 5 3
HELIX 17 17 PRO A 471 GLN A 484 1 14
SHEET 1 A 5 THR A 51 HIS A 58 0
SHEET 2 A 5 PHE A 61 GLY A 68 -1 O PHE A 61 N HIS A 58
SHEET 3 A 5 GLY A 3 ILE A 8 1 O LEU A 4 N VAL A 65
SHEET 4 A 5 SER A 107 VAL A 110 1 O SER A 107 N GLY A 3
SHEET 5 A 5 SER A 142 LEU A 145 1 O SER A 142 N VAL A 108
SHEET 1 B 2 ILE A 76 ASP A 77 0
SHEET 2 B 2 TRP A 82 HIS A 83 -1 O TRP A 82 N ASP A 77
SHEET 1 C 8 THR A 198 ARG A 203 0
SHEET 2 C 8 VAL A 228 LYS A 235 -1 O PHE A 229 N ARG A 203
SHEET 3 C 8 ASN A 295 ASN A 305 -1 N ILE A 296 O TYR A 234
SHEET 4 C 8 LEU A 245 GLY A 249 1 O LEU A 245 N VAL A 297
SHEET 5 C 8 VAL A 353 ALA A 358 1 O VAL A 353 N VAL A 246
SHEET 6 C 8 TRP A 445 ASP A 449 1 O ALA A 446 N ASN A 356
SHEET 7 C 8 THR A 373 THR A 377 -1 O GLY A 374 N ASP A 449
SHEET 8 C 8 VAL A 397 ARG A 399 1 N TRP A 398 O THR A 373
SHEET 1 D 4 THR A 198 ARG A 203 0
SHEET 2 D 4 VAL A 228 LYS A 235 -1 O PHE A 229 N ARG A 203
SHEET 3 D 4 ASN A 295 ASN A 305 -1 N ILE A 296 O TYR A 234
SHEET 4 D 4 GLY A 251 ASP A 255 1 O GLY A 251 N CYS A 303
SHEET 1 E 3 ASP A 316 ARG A 319 0
SHEET 2 E 3 THR A 325 VAL A 328 -1 O ILE A 326 N VAL A 318
SHEET 3 E 3 VAL A 418 ASN A 419 1 O VAL A 418 N GLN A 327
SHEET 1 F 2 THR A 455 ASN A 456 0
SHEET 2 F 2 GLY A 466 MET A 467 -1 O GLY A 466 N ASN A 456
LINK NZ LYS A 250 ZN ZN A 489 1555 1555 2.26
LINK OD1 ASP A 255 ZN ZN A 488 1555 1555 2.13
LINK OD1 ASP A 255 ZN ZN A 489 1555 1555 2.69
LINK OD1 ASP A 273 ZN ZN A 489 1555 1555 2.05
LINK OD2 ASP A 332 ZN ZN A 488 1555 1555 2.33
LINK O ASP A 332 ZN ZN A 488 1555 1555 2.42
LINK OE2 GLU A 334 ZN ZN A 488 1555 1555 2.00
LINK OE1 GLU A 334 ZN ZN A 489 1555 1555 1.97
CISPEP 1 ARG A 470 PRO A 471 0 4.77
SITE 1 AC1 4 ASP A 255 ASP A 332 GLU A 334 ZN A 489
SITE 1 AC2 5 LYS A 250 ASP A 255 ASP A 273 GLU A 334
SITE 2 AC2 5 ZN A 488
CRYST1 132.500 132.500 121.800 90.00 90.00 120.00 P 63 2 2 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007547 0.004357 0.000000 0.00000
SCALE2 0.000000 0.008715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008210 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
