HEADER HYDROLASE 05-JUL-12 4FYQ
TITLE HUMAN AMINOPEPTIDASE N (CD13)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE N;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 66-967;
COMPND 5 SYNONYM: AP-N, HAPN, ALANYL AMINOPEPTIDASE, AMINOPEPTIDASE M, AP-M,
COMPND 6 MICROSOMAL AMINOPEPTIDASE, MYELOID PLASMA MEMBRANE GLYCOPROTEIN CD13,
COMPND 7 GP150;
COMPND 8 EC: 3.4.11.2;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ANPEP, APN, CD13, PEPN;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS METALLOPROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.H.WONG,J.M.RINI
REVDAT 4 29-JUL-20 4FYQ 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 15-NOV-17 4FYQ 1 REMARK
REVDAT 2 14-NOV-12 4FYQ 1 JRNL
REVDAT 1 05-SEP-12 4FYQ 0
JRNL AUTH A.H.WONG,D.ZHOU,J.M.RINI
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF HUMAN AMINOPEPTIDASE N
JRNL TITL 2 REVEALS A NOVEL DIMER AND THE BASIS FOR PEPTIDE PROCESSING.
JRNL REF J.BIOL.CHEM. V. 287 36804 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22932899
JRNL DOI 10.1074/JBC.M112.398842
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 121323
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6417
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8904
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.1920
REMARK 3 BIN FREE R VALUE SET COUNT : 474
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7206
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 211
REMARK 3 SOLVENT ATOMS : 693
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.963
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7687 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10498 ; 1.323 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 908 ; 5.894 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 373 ;37.584 ;24.584
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1240 ;12.081 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;15.057 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1175 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5877 ; 0.007 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4FYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-12.
REMARK 100 THE DEPOSITION ID IS D_1000073519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127785
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27400
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: SAD
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 (%): 69.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE, 10% GLYCEROL, PH 5.0, HANGING DROP VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 38.34900
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 76.69800
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 0.00000
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 38.34900
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 76.69800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 BIOMT1 2 -1.000000 0.000000 0.000000 157.90100
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1749 LIES ON A SPECIAL POSITION.
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 PRO A 65
REMARK 465 ASP A 66
REMARK 465 GLN A 67
REMARK 465 TYR A 891
REMARK 465 GLY A 892
REMARK 465 GLY A 893
REMARK 465 GLY A 894
REMARK 465 SER A 895
REMARK 465 PHE A 896
REMARK 465 SER A 897
REMARK 465 PHE A 898
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 188 40.66 -89.91
REMARK 500 ASP A 261 95.02 -166.30
REMARK 500 PRO A 262 2.88 -67.96
REMARK 500 GLU A 355 31.60 -80.89
REMARK 500 SER A 452 -169.61 -76.59
REMARK 500 SER A 492 144.67 80.00
REMARK 500 THR A 534 -166.51 -162.39
REMARK 500 ASN A 623 63.37 71.92
REMARK 500 ASP A 649 91.64 -161.91
REMARK 500 ASN A 823 -8.84 87.04
REMARK 500 SER A 910 15.91 -148.42
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 A1012 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 HIS A 392 NE2 102.9
REMARK 620 3 GLU A 411 OE1 113.0 101.4
REMARK 620 4 ACY A1024 OXT 107.9 136.4 94.1
REMARK 620 5 ACY A1024 O 90.2 94.3 147.8 56.2
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FYR RELATED DB: PDB
REMARK 900 RELATED ID: 4FYS RELATED DB: PDB
REMARK 900 RELATED ID: 4FYT RELATED DB: PDB
DBREF 4FYQ A 66 967 UNP P15144 AMPN_HUMAN 66 967
SEQADV 4FYQ PRO A 65 UNP P15144 EXPRESSION TAG
SEQRES 1 A 903 PRO ASP GLN SER LYS ALA TRP ASN ARG TYR ARG LEU PRO
SEQRES 2 A 903 ASN THR LEU LYS PRO ASP SER TYR ARG VAL THR LEU ARG
SEQRES 3 A 903 PRO TYR LEU THR PRO ASN ASP ARG GLY LEU TYR VAL PHE
SEQRES 4 A 903 LYS GLY SER SER THR VAL ARG PHE THR CYS LYS GLU ALA
SEQRES 5 A 903 THR ASP VAL ILE ILE ILE HIS SER LYS LYS LEU ASN TYR
SEQRES 6 A 903 THR LEU SER GLN GLY HIS ARG VAL VAL LEU ARG GLY VAL
SEQRES 7 A 903 GLY GLY SER GLN PRO PRO ASP ILE ASP LYS THR GLU LEU
SEQRES 8 A 903 VAL GLU PRO THR GLU TYR LEU VAL VAL HIS LEU LYS GLY
SEQRES 9 A 903 SER LEU VAL LYS ASP SER GLN TYR GLU MET ASP SER GLU
SEQRES 10 A 903 PHE GLU GLY GLU LEU ALA ASP ASP LEU ALA GLY PHE TYR
SEQRES 11 A 903 ARG SER GLU TYR MET GLU GLY ASN VAL ARG LYS VAL VAL
SEQRES 12 A 903 ALA THR THR GLN MET GLN ALA ALA ASP ALA ARG LYS SER
SEQRES 13 A 903 PHE PRO CYS PHE ASP GLU PRO ALA MET LYS ALA GLU PHE
SEQRES 14 A 903 ASN ILE THR LEU ILE HIS PRO LYS ASP LEU THR ALA LEU
SEQRES 15 A 903 SER ASN MET LEU PRO LYS GLY PRO SER THR PRO LEU PRO
SEQRES 16 A 903 GLU ASP PRO ASN TRP ASN VAL THR GLU PHE HIS THR THR
SEQRES 17 A 903 PRO LYS MET SER THR TYR LEU LEU ALA PHE ILE VAL SER
SEQRES 18 A 903 GLU PHE ASP TYR VAL GLU LYS GLN ALA SER ASN GLY VAL
SEQRES 19 A 903 LEU ILE ARG ILE TRP ALA ARG PRO SER ALA ILE ALA ALA
SEQRES 20 A 903 GLY HIS GLY ASP TYR ALA LEU ASN VAL THR GLY PRO ILE
SEQRES 21 A 903 LEU ASN PHE PHE ALA GLY HIS TYR ASP THR PRO TYR PRO
SEQRES 22 A 903 LEU PRO LYS SER ASP GLN ILE GLY LEU PRO ASP PHE ASN
SEQRES 23 A 903 ALA GLY ALA MET GLU ASN TRP GLY LEU VAL THR TYR ARG
SEQRES 24 A 903 GLU ASN SER LEU LEU PHE ASP PRO LEU SER SER SER SER
SEQRES 25 A 903 SER ASN LYS GLU ARG VAL VAL THR VAL ILE ALA HIS GLU
SEQRES 26 A 903 LEU ALA HIS GLN TRP PHE GLY ASN LEU VAL THR ILE GLU
SEQRES 27 A 903 TRP TRP ASN ASP LEU TRP LEU ASN GLU GLY PHE ALA SER
SEQRES 28 A 903 TYR VAL GLU TYR LEU GLY ALA ASP TYR ALA GLU PRO THR
SEQRES 29 A 903 TRP ASN LEU LYS ASP LEU MET VAL LEU ASN ASP VAL TYR
SEQRES 30 A 903 ARG VAL MET ALA VAL ASP ALA LEU ALA SER SER HIS PRO
SEQRES 31 A 903 LEU SER THR PRO ALA SER GLU ILE ASN THR PRO ALA GLN
SEQRES 32 A 903 ILE SER GLU LEU PHE ASP ALA ILE SER TYR SER LYS GLY
SEQRES 33 A 903 ALA SER VAL LEU ARG MET LEU SER SER PHE LEU SER GLU
SEQRES 34 A 903 ASP VAL PHE LYS GLN GLY LEU ALA SER TYR LEU HIS THR
SEQRES 35 A 903 PHE ALA TYR GLN ASN THR ILE TYR LEU ASN LEU TRP ASP
SEQRES 36 A 903 HIS LEU GLN GLU ALA VAL ASN ASN ARG SER ILE GLN LEU
SEQRES 37 A 903 PRO THR THR VAL ARG ASP ILE MET ASN ARG TRP THR LEU
SEQRES 38 A 903 GLN MET GLY PHE PRO VAL ILE THR VAL ASP THR SER THR
SEQRES 39 A 903 GLY THR LEU SER GLN GLU HIS PHE LEU LEU ASP PRO ASP
SEQRES 40 A 903 SER ASN VAL THR ARG PRO SER GLU PHE ASN TYR VAL TRP
SEQRES 41 A 903 ILE VAL PRO ILE THR SER ILE ARG ASP GLY ARG GLN GLN
SEQRES 42 A 903 GLN ASP TYR TRP LEU ILE ASP VAL ARG ALA GLN ASN ASP
SEQRES 43 A 903 LEU PHE SER THR SER GLY ASN GLU TRP VAL LEU LEU ASN
SEQRES 44 A 903 LEU ASN VAL THR GLY TYR TYR ARG VAL ASN TYR ASP GLU
SEQRES 45 A 903 GLU ASN TRP ARG LYS ILE GLN THR GLN LEU GLN ARG ASP
SEQRES 46 A 903 HIS SER ALA ILE PRO VAL ILE ASN ARG ALA GLN ILE ILE
SEQRES 47 A 903 ASN ASP ALA PHE ASN LEU ALA SER ALA HIS LYS VAL PRO
SEQRES 48 A 903 VAL THR LEU ALA LEU ASN ASN THR LEU PHE LEU ILE GLU
SEQRES 49 A 903 GLU ARG GLN TYR MET PRO TRP GLU ALA ALA LEU SER SER
SEQRES 50 A 903 LEU SER TYR PHE LYS LEU MET PHE ASP ARG SER GLU VAL
SEQRES 51 A 903 TYR GLY PRO MET LYS ASN TYR LEU LYS LYS GLN VAL THR
SEQRES 52 A 903 PRO LEU PHE ILE HIS PHE ARG ASN ASN THR ASN ASN TRP
SEQRES 53 A 903 ARG GLU ILE PRO GLU ASN LEU MET ASP GLN TYR SER GLU
SEQRES 54 A 903 VAL ASN ALA ILE SER THR ALA CYS SER ASN GLY VAL PRO
SEQRES 55 A 903 GLU CYS GLU GLU MET VAL SER GLY LEU PHE LYS GLN TRP
SEQRES 56 A 903 MET GLU ASN PRO ASN ASN ASN PRO ILE HIS PRO ASN LEU
SEQRES 57 A 903 ARG SER THR VAL TYR CYS ASN ALA ILE ALA GLN GLY GLY
SEQRES 58 A 903 GLU GLU GLU TRP ASP PHE ALA TRP GLU GLN PHE ARG ASN
SEQRES 59 A 903 ALA THR LEU VAL ASN GLU ALA ASP LYS LEU ARG ALA ALA
SEQRES 60 A 903 LEU ALA CYS SER LYS GLU LEU TRP ILE LEU ASN ARG TYR
SEQRES 61 A 903 LEU SER TYR THR LEU ASN PRO ASP LEU ILE ARG LYS GLN
SEQRES 62 A 903 ASP ALA THR SER THR ILE ILE SER ILE THR ASN ASN VAL
SEQRES 63 A 903 ILE GLY GLN GLY LEU VAL TRP ASP PHE VAL GLN SER ASN
SEQRES 64 A 903 TRP LYS LYS LEU PHE ASN ASP TYR GLY GLY GLY SER PHE
SEQRES 65 A 903 SER PHE SER ASN LEU ILE GLN ALA VAL THR ARG ARG PHE
SEQRES 66 A 903 SER THR GLU TYR GLU LEU GLN GLN LEU GLU GLN PHE LYS
SEQRES 67 A 903 LYS ASP ASN GLU GLU THR GLY PHE GLY SER GLY THR ARG
SEQRES 68 A 903 ALA LEU GLU GLN ALA LEU GLU LYS THR LYS ALA ASN ILE
SEQRES 69 A 903 LYS TRP VAL LYS GLU ASN LYS GLU VAL VAL LEU GLN TRP
SEQRES 70 A 903 PHE THR GLU ASN SER LYS
MODRES 4FYQ ASN A 625 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 527 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 681 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 818 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 234 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 319 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 265 ASN GLYCOSYLATION SITE
MODRES 4FYQ ASN A 128 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET NAG C 1 14
HET NAG C 2 14
HET NAG A1001 14
HET NAG A1005 14
HET NAG A1006 14
HET NAG A1009 14
HET NAG A1010 14
HET NAG A1011 14
HET ZN A1012 1
HET SO4 A1013 5
HET SO4 A1014 5
HET SO4 A1015 5
HET SO4 A1016 5
HET SO4 A1017 5
HET SO4 A1018 5
HET SO4 A1019 5
HET SO4 A1020 5
HET SO4 A1021 5
HET SO4 A1022 5
HET SO4 A1023 5
HET ACY A1024 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM ACY ACETIC ACID
FORMUL 2 NAG 10(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 10 ZN ZN 2+
FORMUL 11 SO4 11(O4 S 2-)
FORMUL 22 ACY C2 H4 O2
FORMUL 23 HOH *693(H2 O)
HELIX 1 1 LYS A 69 ARG A 73 5 5
HELIX 2 2 ASP A 216 SER A 220 5 5
HELIX 3 3 SER A 276 LEU A 280 5 5
HELIX 4 4 ARG A 305 ALA A 311 1 7
HELIX 5 5 GLY A 314 TYR A 332 1 19
HELIX 6 6 GLU A 364 LEU A 368 1 5
HELIX 7 7 SER A 375 PHE A 395 1 21
HELIX 8 8 TRP A 403 ASP A 406 5 4
HELIX 9 9 LEU A 407 GLU A 426 1 20
HELIX 10 10 ASN A 430 ASP A 433 5 4
HELIX 11 11 LEU A 434 ASP A 439 1 6
HELIX 12 12 ASP A 439 ALA A 448 1 10
HELIX 13 13 PRO A 458 ILE A 462 5 5
HELIX 14 14 THR A 464 LEU A 471 1 8
HELIX 15 15 ASP A 473 SER A 492 1 20
HELIX 16 16 SER A 492 ALA A 508 1 17
HELIX 17 17 ILE A 513 ARG A 528 1 16
HELIX 18 18 THR A 535 LEU A 545 1 11
HELIX 19 19 ASP A 610 SER A 613 5 4
HELIX 20 20 LEU A 624 THR A 627 5 4
HELIX 21 21 ASP A 635 HIS A 650 1 16
HELIX 22 22 SER A 651 ILE A 653 5 3
HELIX 23 23 PRO A 654 ALA A 671 1 18
HELIX 24 24 PRO A 675 ASN A 682 1 8
HELIX 25 25 THR A 683 GLU A 689 5 7
HELIX 26 26 GLN A 691 ASP A 710 1 20
HELIX 27 27 VAL A 714 THR A 737 1 24
HELIX 28 28 ASN A 746 ASN A 763 1 18
HELIX 29 29 VAL A 765 ASN A 782 1 18
HELIX 30 30 HIS A 789 ASN A 791 5 3
HELIX 31 31 LEU A 792 GLY A 804 1 13
HELIX 32 32 GLY A 805 ASN A 818 1 14
HELIX 33 33 LEU A 821 LEU A 832 1 12
HELIX 34 34 ALA A 833 SER A 835 5 3
HELIX 35 35 GLU A 837 LEU A 849 1 13
HELIX 36 36 ARG A 855 GLN A 857 5 3
HELIX 37 37 ASP A 858 ASN A 869 1 12
HELIX 38 38 ILE A 871 ASP A 890 1 20
HELIX 39 39 ASN A 900 ARG A 907 1 8
HELIX 40 40 THR A 911 GLU A 926 1 16
HELIX 41 41 PHE A 930 SER A 932 5 3
HELIX 42 42 GLY A 933 SER A 966 1 34
SHEET 1 A 3 ASN A 128 TYR A 129 0
SHEET 2 A 3 SER A 174 GLU A 185 -1 O GLU A 183 N ASN A 128
SHEET 3 A 3 VAL A 137 GLY A 141 -1 N ARG A 140 O GLU A 177
SHEET 1 B 7 ASN A 128 TYR A 129 0
SHEET 2 B 7 SER A 174 GLU A 185 -1 O GLU A 183 N ASN A 128
SHEET 3 B 7 VAL A 102 CYS A 113 -1 N CYS A 113 O SER A 174
SHEET 4 B 7 LEU A 80 PRO A 91 -1 N ASP A 83 O ARG A 110
SHEET 5 B 7 GLU A 232 PRO A 240 1 O THR A 236 N VAL A 87
SHEET 6 B 7 TRP A 264 GLU A 268 -1 O ASN A 265 N HIS A 239
SHEET 7 B 7 THR A 256 PRO A 257 -1 N THR A 256 O VAL A 266
SHEET 1 C 3 VAL A 119 HIS A 123 0
SHEET 2 C 3 TYR A 161 LEU A 166 -1 O LEU A 162 N ILE A 122
SHEET 3 C 3 ILE A 150 VAL A 156 -1 N GLU A 154 O VAL A 163
SHEET 1 D 2 GLY A 192 GLU A 200 0
SHEET 2 D 2 VAL A 203 GLN A 211 -1 O LYS A 205 N TYR A 198
SHEET 1 E 2 THR A 244 SER A 247 0
SHEET 2 E 2 PHE A 282 SER A 285 -1 O ILE A 283 N LEU A 246
SHEET 1 F 5 ASP A 288 GLN A 293 0
SHEET 2 F 5 LEU A 299 ALA A 304 -1 O ILE A 302 N VAL A 290
SHEET 3 F 5 LYS A 340 LEU A 346 1 O GLN A 343 N TRP A 303
SHEET 4 F 5 LEU A 359 ARG A 363 1 O TYR A 362 N LEU A 346
SHEET 5 F 5 ALA A 353 MET A 354 -1 N MET A 354 O THR A 361
SHEET 1 G 2 VAL A 399 ILE A 401 0
SHEET 2 G 2 GLN A 510 THR A 512 1 O THR A 512 N THR A 400
SHEET 1 H 4 ARG A 606 GLN A 608 0
SHEET 2 H 4 THR A 560 HIS A 565 -1 N LEU A 561 O ALA A 607
SHEET 3 H 4 PRO A 550 ASP A 555 -1 N ASP A 555 O THR A 560
SHEET 4 H 4 ARG A 631 TYR A 634 1 O ARG A 631 N ILE A 552
SHEET 1 I 2 VAL A 586 ILE A 588 0
SHEET 2 I 2 TYR A 600 LEU A 602 -1 O TYR A 600 N ILE A 588
SHEET 1 J 3 ARG A 595 GLN A 596 0
SHEET 2 J 3 SER A 590 ARG A 592 -1 N ARG A 592 O ARG A 595
SHEET 3 J 3 VAL A 620 LEU A 622 -1 O LEU A 621 N ILE A 591
SSBOND 1 CYS A 761 CYS A 768 1555 1555 2.12
SSBOND 2 CYS A 798 CYS A 834 1555 1555 2.09
LINK ND2 ASN A 128 C1 NAG A1001 1555 1555 1.45
LINK ND2 ASN A 234 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 265 C1 NAG A1005 1555 1555 1.44
LINK ND2 ASN A 319 C1 NAG A1006 1555 1555 1.44
LINK ND2 ASN A 527 C1 NAG A1010 1555 1555 1.44
LINK ND2 ASN A 625 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 681 C1 NAG A1009 1555 1555 1.44
LINK ND2 ASN A 818 C1 NAG A1011 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK NE2 HIS A 388 ZN ZN A1012 1555 1555 2.02
LINK NE2 HIS A 392 ZN ZN A1012 1555 1555 2.05
LINK OE1 GLU A 411 ZN ZN A1012 1555 1555 1.94
LINK ZN ZN A1012 OXT ACY A1024 1555 1555 2.01
LINK ZN ZN A1012 O ACY A1024 1555 1555 2.49
CISPEP 1 GLN A 213 ALA A 214 0 1.50
CRYST1 157.901 157.901 115.047 90.00 90.00 120.00 P 64 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 0.006333 0.003656 0.000000 0.00000
SCALE2 0.000000 0.007313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008692 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
