HEADER HYDROLASE/HYDROLASE INHIBITOR 13-JUN-12 4FKK
TITLE CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N COMPLEXED WITH BESTATIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE N;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 62-963;
COMPND 5 SYNONYM: AP-N, PAPN, ALANYL AMINOPEPTIDASE, AMINOPEPTIDASE M, AP-M,
COMPND 6 MICROSOMAL AMINOPEPTIDASE, GP130;
COMPND 7 EC: 3.4.11.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: ANPEP;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS ZINC AMINOPEPTIDASE-N, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CHEN,Y.L.LIN,G.PENG,F.LI
REVDAT 5 29-JUL-20 4FKK 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 17-JUL-19 4FKK 1 REMARK LINK
REVDAT 3 14-NOV-12 4FKK 1 JRNL
REVDAT 2 31-OCT-12 4FKK 1 JRNL REMARK
REVDAT 1 17-OCT-12 4FKK 0
JRNL AUTH L.CHEN,Y.L.LIN,G.PENG,F.LI
JRNL TITL STRUCTURAL BASIS FOR MULTIFUNCTIONAL ROLES OF MAMMALIAN
JRNL TITL 2 AMINOPEPTIDASE N.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 17966 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 23071329
JRNL DOI 10.1073/PNAS.1210123109
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 37227
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1969
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 263
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7241
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 345
REMARK 3 SOLVENT ATOMS : 848
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : -0.92000
REMARK 3 B33 (A**2) : 0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.352
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.238
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.624
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7799 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10654 ; 1.471 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 901 ; 6.132 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;41.633 ;24.973
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1217 ;14.778 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;16.745 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1220 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5914 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 7799 ; 3.199 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 453 ;33.615 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 8017 ;23.220 ; 5.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 63 A 281
REMARK 3 RESIDUE RANGE : A 282 A 543
REMARK 3 RESIDUE RANGE : A 544 A 632
REMARK 3 RESIDUE RANGE : A 633 A 964
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4621 18.4375 59.6890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0270 T22: 0.0742
REMARK 3 T33: 0.0450 T12: -0.0229
REMARK 3 T13: 0.0134 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.3950 L22: 0.1024
REMARK 3 L33: 0.2055 L12: -0.0090
REMARK 3 L13: 0.0233 L23: -0.0454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.0063 S13: 0.1128
REMARK 3 S21: -0.0029 S22: -0.0285 S23: 0.0071
REMARK 3 S31: 0.0642 S32: -0.0781 S33: 0.0417
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4FKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-ID; 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL; NULL
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH RESOLUTION
REMARK 200 DOUBLE CRYSTAL SI(111); SINGLE
REMARK 200 CRYSTAL SI(220) SIDE BOUNCE
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39425
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
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: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 200 MM LITHIUM SULFATE,
REMARK 280 100 MM HEPES, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 130.30550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.50700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 130.30550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.50700
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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 ASP A 62
REMARK 465 HIS A 965
REMARK 465 HIS A 966
REMARK 465 HIS A 967
REMARK 465 HIS A 968
REMARK 465 HIS A 969
REMARK 465 HIS A 970
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 O6 NAG E 1 O HOH A 1699 1.81
REMARK 500 O HOH A 1439 O HOH A 1785 1.82
REMARK 500 O HOH A 1600 O HOH A 1946 1.87
REMARK 500 O HOH A 1520 O HOH A 1746 1.96
REMARK 500 O HOH A 1664 O HOH A 1785 2.01
REMARK 500 O HOH A 1285 O HOH A 1643 2.03
REMARK 500 O HOH A 1485 O HOH A 1486 2.03
REMARK 500 O HOH A 1372 O HOH A 1650 2.03
REMARK 500 O HOH A 1715 O HOH A 1836 2.05
REMARK 500 ND2 ASN A 506 O5 NAG G 1 2.06
REMARK 500 SD MET A 194 O HOH A 1886 2.07
REMARK 500 O HOH A 1448 O HOH A 1460 2.09
REMARK 500 O HOH A 1698 O HOH A 1814 2.13
REMARK 500 O HOH A 1128 O HOH A 1429 2.14
REMARK 500 NE ARG A 147 O HOH A 1838 2.15
REMARK 500 O HOH A 1568 O HOH A 1915 2.15
REMARK 500 O HOH A 1118 O HOH A 1580 2.16
REMARK 500 O HOH A 1413 O HOH A 1894 2.18
REMARK 500 O HOH A 1715 O HOH A 1821 2.19
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 ALA A 93 -34.15 78.35
REMARK 500 PHE A 216 147.44 -171.21
REMARK 500 ASP A 256 94.04 -162.38
REMARK 500 ARG A 300 137.15 -39.11
REMARK 500 GLU A 350 31.19 -78.83
REMARK 500 LEU A 354 82.28 -153.24
REMARK 500 ASP A 434 -53.57 -127.51
REMARK 500 ALA A 443 33.83 -90.21
REMARK 500 ASN A 458 -39.73 -133.40
REMARK 500 THR A 487 143.43 68.45
REMARK 500 GLN A 505 -163.79 -128.09
REMARK 500 SER A 586 147.68 -176.05
REMARK 500 THR A 732 -74.12 -56.46
REMARK 500 ASN A 782 78.20 -115.61
REMARK 500 LYS A 882 36.95 -67.83
REMARK 500 TYR A 888 -27.11 -153.00
REMARK 500 PHE A 893 -35.14 93.03
REMARK 500 SER A 894 60.58 64.76
REMARK 500 MET A 923 93.26 -35.39
REMARK 500 ASP A 924 -145.68 40.04
REMARK 500 VAL A 925 -22.57 42.81
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 A1025 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 383 NE2
REMARK 620 2 HIS A 387 NE2 98.8
REMARK 620 3 GLU A 406 OE2 100.7 104.3
REMARK 620 4 BES A1024 O2 108.9 107.2 132.1
REMARK 620 N 1 2 3
REMARK 630
REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE INHIBITOR
REMARK 630 MOLECULE NAME: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 NAG A 1020
REMARK 630 NAG A 1023
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: NULL
REMARK 630 DETAILS: OLIGOSACCHARIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FKE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N
REMARK 900 RELATED ID: 4HOL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N COMPLEXED WITH POLY-
REMARK 900 ALANINE
REMARK 900 RELATED ID: 4FKH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N COMPLEXED WITH ALANINE
REMARK 900 RELATED ID: 4HOM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PORCINE AMINOPEPTIDASE-N COMPLEXED WITH
REMARK 900 SUBSTANCE P
DBREF 4FKK A 62 963 UNP P15145 AMPN_PIG 62 963
SEQADV 4FKK ASN A 82 UNP P15145 PHE 82 CONFLICT
SEQADV 4FKK PHE A 107 UNP P15145 LEU 107 CONFLICT
SEQADV 4FKK SER A 964 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 965 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 966 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 967 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 968 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 969 UNP P15145 EXPRESSION TAG
SEQADV 4FKK HIS A 970 UNP P15145 EXPRESSION TAG
SEQRES 1 A 909 ASP GLN SER LYS PRO TRP ASN ARG TYR ARG LEU PRO THR
SEQRES 2 A 909 THR LEU LEU PRO ASP SER TYR ASN VAL THR LEU ARG PRO
SEQRES 3 A 909 TYR LEU THR PRO ASN ALA ASP GLY LEU TYR ILE PHE LYS
SEQRES 4 A 909 GLY LYS SER ILE VAL ARG PHE LEU CYS GLN GLU PRO THR
SEQRES 5 A 909 ASP VAL ILE ILE ILE HIS SER LYS LYS LEU ASN TYR THR
SEQRES 6 A 909 THR GLN GLY HIS MET VAL VAL LEU ARG GLY VAL GLY ASP
SEQRES 7 A 909 SER GLN VAL PRO GLU ILE ASP ARG THR GLU LEU VAL GLU
SEQRES 8 A 909 LEU THR GLU TYR LEU VAL VAL HIS LEU LYS GLY SER LEU
SEQRES 9 A 909 GLN PRO GLY HIS MET TYR GLU MET GLU SER GLU PHE GLN
SEQRES 10 A 909 GLY GLU LEU ALA ASP ASP LEU ALA GLY PHE TYR ARG SER
SEQRES 11 A 909 GLU TYR MET GLU GLY ASN VAL LYS LYS VAL LEU ALA THR
SEQRES 12 A 909 THR GLN MET GLN SER THR ASP ALA ARG LYS SER PHE PRO
SEQRES 13 A 909 CYS PHE ASP GLU PRO ALA MET LYS ALA THR PHE ASN ILE
SEQRES 14 A 909 THR LEU ILE HIS PRO ASN ASN LEU THR ALA LEU SER ASN
SEQRES 15 A 909 MET PRO PRO LYS GLY SER SER THR PRO LEU ALA GLU ASP
SEQRES 16 A 909 PRO ASN TRP SER VAL THR GLU PHE GLU THR THR PRO VAL
SEQRES 17 A 909 MET SER THR TYR LEU LEU ALA TYR ILE VAL SER GLU PHE
SEQRES 18 A 909 GLN SER VAL ASN GLU THR ALA GLN ASN GLY VAL LEU ILE
SEQRES 19 A 909 ARG ILE TRP ALA ARG PRO ASN ALA ILE ALA GLU GLY HIS
SEQRES 20 A 909 GLY MET TYR ALA LEU ASN VAL THR GLY PRO ILE LEU ASN
SEQRES 21 A 909 PHE PHE ALA ASN HIS TYR ASN THR SER TYR PRO LEU PRO
SEQRES 22 A 909 LYS SER ASP GLN ILE ALA LEU PRO ASP PHE ASN ALA GLY
SEQRES 23 A 909 ALA MET GLU ASN TRP GLY LEU VAL THR TYR ARG GLU ASN
SEQRES 24 A 909 ALA LEU LEU PHE ASP PRO GLN SER SER SER ILE SER ASN
SEQRES 25 A 909 LYS GLU ARG VAL VAL THR VAL ILE ALA HIS GLU LEU ALA
SEQRES 26 A 909 HIS GLN TRP PHE GLY ASN LEU VAL THR LEU ALA TRP TRP
SEQRES 27 A 909 ASN ASP LEU TRP LEU ASN GLU GLY PHE ALA SER TYR VAL
SEQRES 28 A 909 GLU TYR LEU GLY ALA ASP HIS ALA GLU PRO THR TRP ASN
SEQRES 29 A 909 LEU LYS ASP LEU ILE VAL PRO GLY ASP VAL TYR ARG VAL
SEQRES 30 A 909 MET ALA VAL ASP ALA LEU ALA SER SER HIS PRO LEU THR
SEQRES 31 A 909 THR PRO ALA GLU GLU VAL ASN THR PRO ALA GLN ILE SER
SEQRES 32 A 909 GLU MET PHE ASP SER ILE SER TYR SER LYS GLY ALA SER
SEQRES 33 A 909 VAL ILE ARG MET LEU SER ASN PHE LEU THR GLU ASP LEU
SEQRES 34 A 909 PHE LYS GLU GLY LEU ALA SER TYR LEU HIS ALA PHE ALA
SEQRES 35 A 909 TYR GLN ASN THR THR TYR LEU ASP LEU TRP GLU HIS LEU
SEQRES 36 A 909 GLN LYS ALA VAL ASP ALA GLN THR SER ILE ARG LEU PRO
SEQRES 37 A 909 ASP THR VAL ARG ALA ILE MET ASP ARG TRP THR LEU GLN
SEQRES 38 A 909 MET GLY PHE PRO VAL ILE THR VAL ASP THR LYS THR GLY
SEQRES 39 A 909 ASN ILE SER GLN LYS HIS PHE LEU LEU ASP SER GLU SER
SEQRES 40 A 909 ASN VAL THR ARG SER SER ALA PHE ASP TYR LEU TRP ILE
SEQRES 41 A 909 VAL PRO ILE SER SER ILE LYS ASN GLY VAL MET GLN ASP
SEQRES 42 A 909 HIS TYR TRP LEU ARG ASP VAL SER GLN ALA GLN ASN ASP
SEQRES 43 A 909 LEU PHE LYS THR ALA SER ASP ASP TRP VAL LEU LEU ASN
SEQRES 44 A 909 VAL ASN VAL THR GLY TYR PHE GLN VAL ASN TYR ASP GLU
SEQRES 45 A 909 ASP ASN TRP ARG MET ILE GLN HIS GLN LEU GLN THR ASN
SEQRES 46 A 909 LEU SER VAL ILE PRO VAL ILE ASN ARG ALA GLN VAL ILE
SEQRES 47 A 909 TYR ASP SER PHE ASN LEU ALA THR ALA HIS MET VAL PRO
SEQRES 48 A 909 VAL THR LEU ALA LEU ASP ASN THR LEU PHE LEU ASN GLY
SEQRES 49 A 909 GLU LYS GLU TYR MET PRO TRP GLN ALA ALA LEU SER SER
SEQRES 50 A 909 LEU SER TYR PHE SER LEU MET PHE ASP ARG SER GLU VAL
SEQRES 51 A 909 TYR GLY PRO MET LYS LYS TYR LEU ARG LYS GLN VAL GLU
SEQRES 52 A 909 PRO LEU PHE GLN HIS PHE GLU THR LEU THR LYS ASN TRP
SEQRES 53 A 909 THR GLU ARG PRO GLU ASN LEU MET ASP GLN TYR SER GLU
SEQRES 54 A 909 ILE ASN ALA ILE SER THR ALA CYS SER ASN GLY LEU PRO
SEQRES 55 A 909 GLN CYS GLU ASN LEU ALA LYS THR LEU PHE ASP GLN TRP
SEQRES 56 A 909 MET SER ASP PRO GLU ASN ASN PRO ILE HIS PRO ASN LEU
SEQRES 57 A 909 ARG SER THR ILE TYR CYS ASN ALA ILE ALA GLN GLY GLY
SEQRES 58 A 909 GLN ASP GLN TRP ASP PHE ALA TRP GLY GLN LEU GLN GLN
SEQRES 59 A 909 ALA GLN LEU VAL ASN GLU ALA ASP LYS LEU ARG SER ALA
SEQRES 60 A 909 LEU ALA CYS SER ASN GLU VAL TRP LEU LEU ASN ARG TYR
SEQRES 61 A 909 LEU GLY TYR THR LEU ASN PRO ASP LEU ILE ARG LYS GLN
SEQRES 62 A 909 ASP ALA THR SER THR ILE ASN SER ILE ALA SER ASN VAL
SEQRES 63 A 909 ILE GLY GLN PRO LEU ALA TRP ASP PHE VAL GLN SER ASN
SEQRES 64 A 909 TRP LYS LYS LEU PHE GLN ASP TYR GLY GLY GLY SER PHE
SEQRES 65 A 909 SER PHE SER ASN LEU ILE GLN GLY VAL THR ARG ARG PHE
SEQRES 66 A 909 SER SER GLU PHE GLU LEU GLN GLN LEU GLU GLN PHE LYS
SEQRES 67 A 909 LYS ASN ASN MET ASP VAL GLY PHE GLY SER GLY THR ARG
SEQRES 68 A 909 ALA LEU GLU GLN ALA LEU GLU LYS THR LYS ALA ASN ILE
SEQRES 69 A 909 LYS TRP VAL LYS GLU ASN LYS GLU VAL VAL LEU ASN TRP
SEQRES 70 A 909 PHE ILE GLU HIS SER SER HIS HIS HIS HIS HIS HIS
MODRES 4FKK ASN A 506 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 328 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 569 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 124 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 622 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 556 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 237 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 314 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 646 ASN GLYCOSYLATION SITE
MODRES 4FKK ASN A 82 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG B 3 14
HET NAG C 1 14
HET NAG C 2 14
HET NAG C 3 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG F 3 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG A1020 14
HET NAG A1023 14
HET BES A1024 22
HET ZN A1025 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BES 2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-
HETNAM 2 BES PENTANOIC ACID
HETNAM ZN ZINC ION
HETSYN BES BESTATIN
FORMUL 2 NAG 23(C8 H15 N O6)
FORMUL 13 BES C16 H24 N2 O4
FORMUL 14 ZN ZN 2+
FORMUL 15 HOH *848(H2 O)
HELIX 1 1 LYS A 65 ARG A 69 5 5
HELIX 2 2 ASP A 211 SER A 215 5 5
HELIX 3 3 SER A 271 LEU A 275 5 5
HELIX 4 4 ARG A 300 GLU A 306 1 7
HELIX 5 5 GLY A 309 TYR A 327 1 19
HELIX 6 6 GLU A 359 LEU A 363 1 5
HELIX 7 7 SER A 370 GLN A 388 1 19
HELIX 8 8 TRP A 398 ASN A 400 5 3
HELIX 9 9 ASP A 401 GLU A 421 1 21
HELIX 10 10 ASN A 425 ASP A 428 5 4
HELIX 11 11 LEU A 429 ASP A 434 1 6
HELIX 12 12 ASP A 434 ALA A 443 1 10
HELIX 13 13 PRO A 453 VAL A 457 5 5
HELIX 14 14 THR A 459 GLU A 465 1 7
HELIX 15 15 ASP A 468 THR A 487 1 20
HELIX 16 16 THR A 487 ALA A 503 1 17
HELIX 17 17 THR A 508 ALA A 522 1 15
HELIX 18 18 THR A 531 LEU A 541 1 11
HELIX 19 19 ASP A 607 LYS A 610 5 4
HELIX 20 20 VAL A 621 THR A 624 5 4
HELIX 21 21 ASP A 632 ASN A 646 1 15
HELIX 22 22 LEU A 647 ILE A 650 5 4
HELIX 23 23 PRO A 651 ALA A 668 1 18
HELIX 24 24 PRO A 672 ASN A 679 1 8
HELIX 25 25 THR A 680 GLU A 686 5 7
HELIX 26 26 GLU A 688 ASP A 707 1 20
HELIX 27 27 VAL A 711 THR A 734 1 24
HELIX 28 28 ASN A 743 ASN A 760 1 18
HELIX 29 29 LEU A 762 SER A 778 1 17
HELIX 30 30 HIS A 786 ASN A 788 5 3
HELIX 31 31 LEU A 789 GLY A 801 1 13
HELIX 32 32 GLY A 802 ALA A 816 1 15
HELIX 33 33 LEU A 818 LEU A 829 1 12
HELIX 34 34 ALA A 830 SER A 832 5 3
HELIX 35 35 GLU A 834 LEU A 846 1 13
HELIX 36 36 ARG A 852 ASN A 866 1 15
HELIX 37 37 ILE A 868 TRP A 881 1 14
HELIX 38 38 SER A 894 THR A 903 1 10
HELIX 39 39 SER A 908 LYS A 920 1 13
HELIX 40 40 ASN A 921 MET A 923 5 3
HELIX 41 41 PHE A 927 THR A 931 5 5
HELIX 42 42 ARG A 932 SER A 963 1 32
SHEET 1 A 3 LEU A 123 TYR A 125 0
SHEET 2 A 3 MET A 170 GLU A 180 -1 O GLN A 178 N ASN A 124
SHEET 3 A 3 VAL A 133 GLY A 136 -1 N ARG A 135 O GLU A 172
SHEET 1 B 7 LEU A 123 TYR A 125 0
SHEET 2 B 7 MET A 170 GLU A 180 -1 O GLN A 178 N ASN A 124
SHEET 3 B 7 ILE A 98 CYS A 109 -1 N GLY A 101 O PHE A 177
SHEET 4 B 7 LEU A 76 PRO A 87 -1 N SER A 80 O ARG A 106
SHEET 5 B 7 THR A 227 PRO A 235 1 O THR A 231 N LEU A 85
SHEET 6 B 7 TRP A 259 GLU A 263 -1 O SER A 260 N HIS A 234
SHEET 7 B 7 THR A 251 PRO A 252 -1 N THR A 251 O VAL A 261
SHEET 1 C 3 THR A 113 HIS A 119 0
SHEET 2 C 3 TYR A 156 LEU A 165 -1 O LEU A 157 N ILE A 118
SHEET 3 C 3 ILE A 145 VAL A 151 -1 N GLU A 149 O VAL A 158
SHEET 1 D 2 GLY A 187 GLU A 195 0
SHEET 2 D 2 VAL A 198 GLN A 206 -1 O LYS A 200 N TYR A 193
SHEET 1 E 2 THR A 239 SER A 242 0
SHEET 2 E 2 TYR A 277 SER A 280 -1 O SER A 280 N THR A 239
SHEET 1 F 5 GLN A 283 THR A 288 0
SHEET 2 F 5 LEU A 294 ALA A 299 -1 O ILE A 295 N GLU A 287
SHEET 3 F 5 LYS A 335 LEU A 341 1 O GLN A 338 N TRP A 298
SHEET 4 F 5 LEU A 354 ARG A 358 1 O TYR A 357 N LEU A 341
SHEET 5 F 5 ALA A 348 MET A 349 -1 N MET A 349 O THR A 356
SHEET 1 G 2 VAL A 394 LEU A 396 0
SHEET 2 G 2 GLN A 505 THR A 507 1 O THR A 507 N THR A 395
SHEET 1 H 4 GLN A 603 GLN A 605 0
SHEET 2 H 4 ASN A 556 HIS A 561 -1 N ILE A 557 O ALA A 604
SHEET 3 H 4 PRO A 546 ASP A 551 -1 N VAL A 547 O LYS A 560
SHEET 4 H 4 GLN A 628 ASN A 630 1 O GLN A 628 N ILE A 548
SHEET 1 I 2 VAL A 582 ILE A 584 0
SHEET 2 I 2 TYR A 596 LEU A 598 -1 O TYR A 596 N ILE A 584
SHEET 1 J 3 VAL A 591 MET A 592 0
SHEET 2 J 3 SER A 586 LYS A 588 -1 N LYS A 588 O VAL A 591
SHEET 3 J 3 VAL A 617 LEU A 619 -1 O LEU A 618 N ILE A 587
SSBOND 1 CYS A 758 CYS A 765 1555 1555 2.06
SSBOND 2 CYS A 795 CYS A 831 1555 1555 2.05
LINK ND2 ASN A 82 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 124 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 237 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 314 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 328 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN A 506 C1 NAG G 1 1555 1555 1.40
LINK ND2 ASN A 556 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN A 569 C1 NAG A1020 1555 1555 1.43
LINK ND2 ASN A 622 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN A 646 C1 NAG A1023 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O4 NAG B 2 C1 NAG B 3 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG C 2 C1 NAG C 3 1555 1555 1.47
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG F 2 C1 NAG F 3 1555 1555 1.47
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.46
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK NE2 HIS A 383 ZN ZN A1025 1555 1555 2.16
LINK NE2 HIS A 387 ZN ZN A1025 1555 1555 2.20
LINK OE2 GLU A 406 ZN ZN A1025 1555 1555 2.03
LINK O2 BES A1024 ZN ZN A1025 1555 1555 2.20
CISPEP 1 GLN A 208 SER A 209 0 -5.46
CRYST1 260.611 63.014 81.705 90.00 100.83 90.00 C 1 2 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 0.003837 0.000000 0.000734 0.00000
SCALE2 0.000000 0.015869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012461 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
