HEADER HYDROLASE 02-SEP-03 1QWN
TITLE GOLGI ALPHA-MANNOSIDASE II COVALENT INTERMEDIATE COMPLEX WITH 5-
TITLE 2 FLUORO-GULOSYL-FLUORIDE
CAVEAT 1QWN MPD A 2002 HAS WRONG CHIRALITY AT ATOM C4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-MANNOSIDASE II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FAMILY 38 CATALYTIC DOMAIN (RESIDUES 94-1108);
COMPND 5 SYNONYM: MANNOSYL-OLIGOSACCHARIDE 1,3-1,6-ALPHA-MANNOSIDASE, MAN II,
COMPND 6 GOLGI ALPHA-MANNOSIDASE II, AMAN II;
COMPND 7 EC: 3.2.1.114;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: ALPHA-MAN-II OR GMII OR CG18474/CG18802/CG8139;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: S2
KEYWDS N-TERMINAL ALPHA-BETA DOMAIN, THREE HELIX BUNDLE, 2 C-TERMINAL BETA
KEYWDS 2 BARRELS, FAMILY 38 GLYCOSYL HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.NUMAO,D.A.KUNTZ,S.G.WITHERS,D.R.ROSE
REVDAT 6 16-AUG-23 1QWN 1 HETSYN
REVDAT 5 29-JUL-20 1QWN 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE ATOM
REVDAT 4 13-JUL-11 1QWN 1 VERSN
REVDAT 3 24-FEB-09 1QWN 1 VERSN
REVDAT 2 27-JAN-04 1QWN 1 JRNL
REVDAT 1 07-OCT-03 1QWN 0
JRNL AUTH S.NUMAO,D.A.KUNTZ,S.G.WITHERS,D.R.ROSE
JRNL TITL INSIGHTS INTO THE MECHANISM OF DROSOPHILA MELANOGASTER GOLGI
JRNL TITL 2 ALPHA-MANNOSIDASE II THROUGH THE STRUCTURAL ANALYSIS OF
JRNL TITL 3 COVALENT REACTION INTERMEDIATES.
JRNL REF J.BIOL.CHEM. V. 278 48074 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12960159
JRNL DOI 10.1074/JBC.M309249200
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 317663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : AS 1HTY
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2225
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 : 8181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 1034
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.80
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) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
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: NULL
REMARK 4
REMARK 4 1QWN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 317663
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.42900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
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: 1HTY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, MPD, TRIS, PH 7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 34.50950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.48050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.00950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.48050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.50950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.00950
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 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 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 ARG A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 GLY A 10
REMARK 465 GLU A 11
REMARK 465 PHE A 12
REMARK 465 ASP A 13
REMARK 465 ASP A 14
REMARK 465 PRO A 15
REMARK 465 ILE A 16
REMARK 465 ARG A 17
REMARK 465 PRO A 18
REMARK 465 PRO A 19
REMARK 465 LEU A 20
REMARK 465 LYS A 21
REMARK 465 VAL A 22
REMARK 465 ALA A 23
REMARK 465 ARG A 24
REMARK 465 SER A 25
REMARK 465 PRO A 26
REMARK 465 ARG A 27
REMARK 465 PRO A 28
REMARK 465 GLY A 29
REMARK 465 GLN A 30
REMARK 465 SER A 1045
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 OH TYR A 506 O HOH A 2904 1.70
REMARK 500 OH TYR A 138 O HOH A 2347 1.85
REMARK 500 OH TYR A 75 O HOH A 3037 2.01
REMARK 500 O HOH A 2301 O HOH A 3030 2.10
REMARK 500 N ASP A 37 O HOH A 3030 2.13
REMARK 500 O ASP A 33 O HOH A 3030 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN A 346 O ASP A 548 4465 2.07
REMARK 500 OG SER A 53 O HOH A 2447 1455 2.16
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 MET A 501 SD MET A 501 CE -0.369
REMARK 500 GLN A 742 CD GLN A 742 OE1 0.134
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 MET A 501 CG - SD - CE ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG A 818 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 963 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 963 NE - CZ - NH2 ANGL. DEV. = -4.6 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 56 75.59 -100.42
REMARK 500 ASP A 56 75.44 -100.42
REMARK 500 TRP A 95 -84.30 -171.17
REMARK 500 ASP A 106 -58.91 -132.82
REMARK 500 THR A 162 -64.39 66.15
REMARK 500 GLN A 227 -52.87 -133.30
REMARK 500 ARG A 289 33.12 -97.43
REMARK 500 LYS A 345 -71.75 -91.35
REMARK 500 LYS A 345 -71.75 -91.35
REMARK 500 SER A 411 -122.94 38.84
REMARK 500 SER A 411 -122.94 38.84
REMARK 500 ILE A 549 -48.74 -143.94
REMARK 500 LEU A 550 117.57 -166.48
REMARK 500 PRO A 562 40.37 -82.72
REMARK 500 ASN A 732 58.57 -93.25
REMARK 500 SER A 762 -3.17 71.01
REMARK 500 ILE A 798 130.96 -35.37
REMARK 500 SER A 833 -15.71 -148.50
REMARK 500 ASP A 839 -161.73 -125.21
REMARK 500 GLU A 991 102.84 18.54
REMARK 500 GLU A 992 -150.31 -123.55
REMARK 500 HIS A 993 94.70 13.60
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 102 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 155 -13.56
REMARK 500 HIS A 797 11.03
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 A2005 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 90 NE2
REMARK 620 2 ASP A 92 OD1 98.4
REMARK 620 3 ASP A 204 OD1 90.2 162.0
REMARK 620 4 HIS A 471 NE2 105.4 101.9 91.0
REMARK 620 5 GUL A2003 O4 87.8 96.0 68.4 155.9
REMARK 620 6 GUL A2003 O3 161.2 91.3 76.4 88.2 75.1
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HTY RELATED DB: PDB
REMARK 900 RELATED ID: 1HWW RELATED DB: PDB
REMARK 900 RELATED ID: 1HXK RELATED DB: PDB
REMARK 900 RELATED ID: 1PS3 RELATED DB: PDB
REMARK 900 RELATED ID: 1QX1 RELATED DB: PDB
REMARK 900 RELATED ID: 1QWU RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE E -> K CONFLICT FOR RESIDUE 970
REMARK 999 IS NOTED IN SWISS-PROT ENTRY Q24451.
DBREF 1QWN A 13 1045 UNP Q24451 MAN2_DROME 76 1108
SEQADV 1QWN ARG A 1 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN SER A 2 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN SER A 3 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN HIS A 4 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN HIS A 5 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN HIS A 6 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN HIS A 7 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN HIS A 8 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN HIS A 9 UNP Q24451 EXPRESSION TAG
SEQADV 1QWN GLY A 10 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN GLU A 11 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN PHE A 12 UNP Q24451 CLONING ARTIFACT
SEQADV 1QWN LYS A 907 UNP Q24451 GLU 970 SEE REMARK 999
SEQRES 1 A 1045 ARG SER SER HIS HIS HIS HIS HIS HIS GLY GLU PHE ASP
SEQRES 2 A 1045 ASP PRO ILE ARG PRO PRO LEU LYS VAL ALA ARG SER PRO
SEQRES 3 A 1045 ARG PRO GLY GLN CYS GLN ASP VAL VAL GLN ASP VAL PRO
SEQRES 4 A 1045 ASN VAL ASP VAL GLN MET LEU GLU LEU TYR ASP ARG MET
SEQRES 5 A 1045 SER PHE LYS ASP ILE ASP GLY GLY VAL TRP LYS GLN GLY
SEQRES 6 A 1045 TRP ASN ILE LYS TYR ASP PRO LEU LYS TYR ASN ALA HIS
SEQRES 7 A 1045 HIS LYS LEU LYS VAL PHE VAL VAL PRO HIS SER HIS ASN
SEQRES 8 A 1045 ASP PRO GLY TRP ILE GLN THR PHE GLU GLU TYR TYR GLN
SEQRES 9 A 1045 HIS ASP THR LYS HIS ILE LEU SER ASN ALA LEU ARG HIS
SEQRES 10 A 1045 LEU HIS ASP ASN PRO GLU MET LYS PHE ILE TRP ALA GLU
SEQRES 11 A 1045 ILE SER TYR PHE ALA ARG PHE TYR HIS ASP LEU GLY GLU
SEQRES 12 A 1045 ASN LYS LYS LEU GLN MET LYS SER ILE VAL LYS ASN GLY
SEQRES 13 A 1045 GLN LEU GLU PHE VAL THR GLY GLY TRP VAL MET PRO ASP
SEQRES 14 A 1045 GLU ALA ASN SER HIS TRP ARG ASN VAL LEU LEU GLN LEU
SEQRES 15 A 1045 THR GLU GLY GLN THR TRP LEU LYS GLN PHE MET ASN VAL
SEQRES 16 A 1045 THR PRO THR ALA SER TRP ALA ILE ASP PRO PHE GLY HIS
SEQRES 17 A 1045 SER PRO THR MET PRO TYR ILE LEU GLN LYS SER GLY PHE
SEQRES 18 A 1045 LYS ASN MET LEU ILE GLN ARG THR HIS TYR SER VAL LYS
SEQRES 19 A 1045 LYS GLU LEU ALA GLN GLN ARG GLN LEU GLU PHE LEU TRP
SEQRES 20 A 1045 ARG GLN ILE TRP ASP ASN LYS GLY ASP THR ALA LEU PHE
SEQRES 21 A 1045 THR HIS MET MET PRO PHE TYR SER TYR ASP ILE PRO HIS
SEQRES 22 A 1045 THR CYS GLY PRO ASP PRO LYS VAL CYS CYS GLN PHE ASP
SEQRES 23 A 1045 PHE LYS ARG MET GLY SER PHE GLY LEU SER CYS PRO TRP
SEQRES 24 A 1045 LYS VAL PRO PRO ARG THR ILE SER ASP GLN ASN VAL ALA
SEQRES 25 A 1045 ALA ARG SER ASP LEU LEU VAL ASP GLN TRP LYS LYS LYS
SEQRES 26 A 1045 ALA GLU LEU TYR ARG THR ASN VAL LEU LEU ILE PRO LEU
SEQRES 27 A 1045 GLY ASP ASP PHE ARG PHE LYS GLN ASN THR GLU TRP ASP
SEQRES 28 A 1045 VAL GLN ARG VAL ASN TYR GLU ARG LEU PHE GLU HIS ILE
SEQRES 29 A 1045 ASN SER GLN ALA HIS PHE ASN VAL GLN ALA GLN PHE GLY
SEQRES 30 A 1045 THR LEU GLN GLU TYR PHE ASP ALA VAL HIS GLN ALA GLU
SEQRES 31 A 1045 ARG ALA GLY GLN ALA GLU PHE PRO THR LEU SER GLY ASP
SEQRES 32 A 1045 PHE PHE THR TYR ALA ASP ARG SER ASP ASN TYR TRP SER
SEQRES 33 A 1045 GLY TYR TYR THR SER ARG PRO TYR HIS LYS ARG MET ASP
SEQRES 34 A 1045 ARG VAL LEU MET HIS TYR VAL ARG ALA ALA GLU MET LEU
SEQRES 35 A 1045 SER ALA TRP HIS SER TRP ASP GLY MET ALA ARG ILE GLU
SEQRES 36 A 1045 GLU ARG LEU GLU GLN ALA ARG ARG GLU LEU SER LEU PHE
SEQRES 37 A 1045 GLN HIS HIS ASP GLY ILE THR GLY THR ALA LYS THR HIS
SEQRES 38 A 1045 VAL VAL VAL ASP TYR GLU GLN ARG MET GLN GLU ALA LEU
SEQRES 39 A 1045 LYS ALA CYS GLN MET VAL MET GLN GLN SER VAL TYR ARG
SEQRES 40 A 1045 LEU LEU THR LYS PRO SER ILE TYR SER PRO ASP PHE SER
SEQRES 41 A 1045 PHE SER TYR PHE THR LEU ASP ASP SER ARG TRP PRO GLY
SEQRES 42 A 1045 SER GLY VAL GLU ASP SER ARG THR THR ILE ILE LEU GLY
SEQRES 43 A 1045 GLU ASP ILE LEU PRO SER LYS HIS VAL VAL MET HIS ASN
SEQRES 44 A 1045 THR LEU PRO HIS TRP ARG GLU GLN LEU VAL ASP PHE TYR
SEQRES 45 A 1045 VAL SER SER PRO PHE VAL SER VAL THR ASP LEU ALA ASN
SEQRES 46 A 1045 ASN PRO VAL GLU ALA GLN VAL SER PRO VAL TRP SER TRP
SEQRES 47 A 1045 HIS HIS ASP THR LEU THR LYS THR ILE HIS PRO GLN GLY
SEQRES 48 A 1045 SER THR THR LYS TYR ARG ILE ILE PHE LYS ALA ARG VAL
SEQRES 49 A 1045 PRO PRO MET GLY LEU ALA THR TYR VAL LEU THR ILE SER
SEQRES 50 A 1045 ASP SER LYS PRO GLU HIS THR SER TYR ALA SER ASN LEU
SEQRES 51 A 1045 LEU LEU ARG LYS ASN PRO THR SER LEU PRO LEU GLY GLN
SEQRES 52 A 1045 TYR PRO GLU ASP VAL LYS PHE GLY ASP PRO ARG GLU ILE
SEQRES 53 A 1045 SER LEU ARG VAL GLY ASN GLY PRO THR LEU ALA PHE SER
SEQRES 54 A 1045 GLU GLN GLY LEU LEU LYS SER ILE GLN LEU THR GLN ASP
SEQRES 55 A 1045 SER PRO HIS VAL PRO VAL HIS PHE LYS PHE LEU LYS TYR
SEQRES 56 A 1045 GLY VAL ARG SER HIS GLY ASP ARG SER GLY ALA TYR LEU
SEQRES 57 A 1045 PHE LEU PRO ASN GLY PRO ALA SER PRO VAL GLU LEU GLY
SEQRES 58 A 1045 GLN PRO VAL VAL LEU VAL THR LYS GLY LYS LEU GLU SER
SEQRES 59 A 1045 SER VAL SER VAL GLY LEU PRO SER VAL VAL HIS GLN THR
SEQRES 60 A 1045 ILE MET ARG GLY GLY ALA PRO GLU ILE ARG ASN LEU VAL
SEQRES 61 A 1045 ASP ILE GLY SER LEU ASP ASN THR GLU ILE VAL MET ARG
SEQRES 62 A 1045 LEU GLU THR HIS ILE ASP SER GLY ASP ILE PHE TYR THR
SEQRES 63 A 1045 ASP LEU ASN GLY LEU GLN PHE ILE LYS ARG ARG ARG LEU
SEQRES 64 A 1045 ASP LYS LEU PRO LEU GLN ALA ASN TYR TYR PRO ILE PRO
SEQRES 65 A 1045 SER GLY MET PHE ILE GLU ASP ALA ASN THR ARG LEU THR
SEQRES 66 A 1045 LEU LEU THR GLY GLN PRO LEU GLY GLY SER SER LEU ALA
SEQRES 67 A 1045 SER GLY GLU LEU GLU ILE MET GLN ASP ARG ARG LEU ALA
SEQRES 68 A 1045 SER ASP ASP GLU ARG GLY LEU GLY GLN GLY VAL LEU ASP
SEQRES 69 A 1045 ASN LYS PRO VAL LEU HIS ILE TYR ARG LEU VAL LEU GLU
SEQRES 70 A 1045 LYS VAL ASN ASN CYS VAL ARG PRO SER LYS LEU HIS PRO
SEQRES 71 A 1045 ALA GLY TYR LEU THR SER ALA ALA HIS LYS ALA SER GLN
SEQRES 72 A 1045 SER LEU LEU ASP PRO LEU ASP LYS PHE ILE PHE ALA GLU
SEQRES 73 A 1045 ASN GLU TRP ILE GLY ALA GLN GLY GLN PHE GLY GLY ASP
SEQRES 74 A 1045 HIS PRO SER ALA ARG GLU ASP LEU ASP VAL SER VAL MET
SEQRES 75 A 1045 ARG ARG LEU THR LYS SER SER ALA LYS THR GLN ARG VAL
SEQRES 76 A 1045 GLY TYR VAL LEU HIS ARG THR ASN LEU MET GLN CYS GLY
SEQRES 77 A 1045 THR PRO GLU GLU HIS THR GLN LYS LEU ASP VAL CYS HIS
SEQRES 78 A 1045 LEU LEU PRO ASN VAL ALA ARG CYS GLU ARG THR THR LEU
SEQRES 79 A 1045 THR PHE LEU GLN ASN LEU GLU HIS LEU ASP GLY MET VAL
SEQRES 80 A 1045 ALA PRO GLU VAL CYS PRO MET GLU THR ALA ALA TYR VAL
SEQRES 81 A 1045 SER SER HIS SER SER
MODRES 1QWN ASN A 194 ASN GLYCOSYLATION SITE
HET NAG A2001 14
HET ZN A2005 1
HET GUL A2003 12
HET TRS A2004 8
HET MPD A2002 8
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM GUL (2R,3S,4R,5S)-2,6-DIFLUORO-2-(HYDROXYMETHYL)OXANE-3,4,
HETNAM 2 GUL 5-TRIOL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GUL 5-FLUORO-BETA-L-GULOSYL FLUORIDE
HETSYN TRS TRIS BUFFER
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 ZN ZN 2+
FORMUL 4 GUL C6 H10 F2 O5
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 6 MPD C6 H14 O2
FORMUL 7 HOH *1034(H2 O)
HELIX 1 1 MET A 45 MET A 52 1 8
HELIX 2 2 ASP A 71 TYR A 75 5 5
HELIX 3 3 THR A 98 ASP A 106 1 9
HELIX 4 4 ASP A 106 ASN A 121 1 16
HELIX 5 5 GLU A 130 LEU A 141 1 12
HELIX 6 6 GLY A 142 ASN A 155 1 14
HELIX 7 7 HIS A 174 ASN A 194 1 21
HELIX 8 8 PRO A 210 LYS A 218 1 9
HELIX 9 9 HIS A 230 GLN A 240 1 11
HELIX 10 10 ASP A 270 THR A 274 5 5
HELIX 11 11 ASP A 278 CYS A 283 1 6
HELIX 12 12 GLN A 284 MET A 290 5 7
HELIX 13 13 ASN A 310 GLU A 327 1 18
HELIX 14 14 GLN A 346 GLN A 367 1 22
HELIX 15 15 ALA A 368 PHE A 370 5 3
HELIX 16 16 THR A 378 ALA A 392 1 15
HELIX 17 17 SER A 416 THR A 420 5 5
HELIX 18 18 ARG A 422 TRP A 445 1 24
HELIX 19 19 ASP A 449 ALA A 452 5 4
HELIX 20 20 ARG A 453 GLN A 469 1 17
HELIX 21 21 LYS A 479 LEU A 509 1 31
HELIX 22 22 PRO A 823 TYR A 828 5 6
HELIX 23 23 THR A 915 ASP A 927 1 13
HELIX 24 24 ASP A 998 LEU A 1002 5 5
HELIX 25 25 ASP A 1024 VAL A 1027 5 4
SHEET 1 A 6 VAL A 43 GLN A 44 0
SHEET 2 A 6 THR A 399 SER A 401 1 O SER A 401 N VAL A 43
SHEET 3 A 6 GLU A 244 TRP A 247 1 N LEU A 246 O LEU A 400
SHEET 4 A 6 LEU A 259 MET A 263 -1 O THR A 261 N PHE A 245
SHEET 5 A 6 ASN A 223 ILE A 226 1 N MET A 224 O HIS A 262
SHEET 6 A 6 ALA A 199 ALA A 202 1 N ALA A 202 O LEU A 225
SHEET 1 B 3 VAL A 333 ASP A 341 0
SHEET 2 B 3 LEU A 81 HIS A 90 1 N LYS A 82 O LEU A 334
SHEET 3 B 3 VAL A 372 PHE A 376 1 O GLN A 375 N VAL A 85
SHEET 1 C 2 PHE A 126 TRP A 128 0
SHEET 2 C 2 LEU A 158 PHE A 160 1 O GLU A 159 N PHE A 126
SHEET 1 D 6 PHE A 524 ASP A 527 0
SHEET 2 D 6 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 D 6 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 D 6 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 D 6 VAL A 578 ASP A 582 -1 N THR A 581 O VAL A 633
SHEET 6 D 6 PRO A 587 VAL A 588 -1 O VAL A 588 N VAL A 580
SHEET 1 E 5 PHE A 524 ASP A 527 0
SHEET 2 E 5 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 E 5 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 E 5 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 E 5 GLN A 945 PHE A 946 -1 O PHE A 946 N LEU A 629
SHEET 1 F 4 ARG A 565 VAL A 573 0
SHEET 2 F 4 THR A 606 VAL A 624 -1 O ALA A 622 N GLN A 567
SHEET 3 F 4 ALA A 590 ASP A 601 -1 N SER A 597 O GLN A 610
SHEET 4 F 4 THR A 644 TYR A 646 1 O SER A 645 N VAL A 592
SHEET 1 G12 LYS A 669 GLY A 671 0
SHEET 2 G12 SER A 648 LEU A 652 1 N LEU A 651 O LYS A 669
SHEET 3 G12 VAL A 745 LYS A 749 -1 O VAL A 745 N LEU A 652
SHEET 4 G12 SER A 754 LEU A 760 -1 O SER A 757 N LEU A 746
SHEET 5 G12 VAL A 763 MET A 769 -1 O MET A 769 N SER A 754
SHEET 6 G12 GLU A 775 VAL A 780 -1 O GLU A 775 N ILE A 768
SHEET 7 G12 VAL A 888 LYS A 898 -1 O VAL A 888 N VAL A 780
SHEET 8 G12 THR A 842 THR A 848 -1 N THR A 845 O VAL A 895
SHEET 9 G12 GLY A 834 GLU A 838 -1 N MET A 835 O LEU A 846
SHEET 10 G12 ILE A 803 LEU A 808 -1 N TYR A 805 O PHE A 836
SHEET 11 G12 GLN A 812 ARG A 817 -1 O ARG A 816 N PHE A 804
SHEET 12 G12 ALA A 911 GLY A 912 -1 O GLY A 912 N PHE A 813
SHEET 1 H 5 ILE A 676 ARG A 679 0
SHEET 2 H 5 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 H 5 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 H 5 HIS A 705 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 H 5 SER A 736 PRO A 737 -1 O SER A 736 N LYS A 714
SHEET 1 I 8 ILE A 676 ARG A 679 0
SHEET 2 I 8 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 I 8 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 I 8 HIS A 705 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 I 8 THR A 788 THR A 796 -1 O ARG A 793 N LYS A 711
SHEET 6 I 8 GLU A 861 ARG A 869 -1 O LEU A 862 N LEU A 794
SHEET 7 I 8 LEU A 852 SER A 855 -1 N SER A 855 O GLU A 863
SHEET 8 I 8 TYR A 829 ILE A 831 -1 N TYR A 829 O GLY A 854
SHEET 1 J 5 LEU A 957 ARG A 964 0
SHEET 2 J 5 GLN A 973 ARG A 981 -1 O GLY A 976 N ARG A 963
SHEET 3 J 5 THR A1036 HIS A1043 -1 O ALA A1037 N LEU A 979
SHEET 4 J 5 VAL A1006 THR A1012 -1 N ARG A1008 O SER A1042
SHEET 5 J 5 ASN A1019 HIS A1022 -1 O LEU A1020 N ARG A1011
SSBOND 1 CYS A 31 CYS A 1032 1555 1555 2.06
SSBOND 2 CYS A 275 CYS A 282 1555 1555 2.03
SSBOND 3 CYS A 283 CYS A 297 1555 1555 2.09
SSBOND 4 CYS A 902 CYS A 987 1555 1555 2.06
SSBOND 5 CYS A 1000 CYS A 1009 1555 1555 2.03
LINK ND2 ASN A 194 C1 NAG A2001 1555 1555 1.37
LINK OD1 ASP A 204 C5 GUL A2003 1555 1555 1.50
LINK NE2 HIS A 90 ZN ZN A2005 1555 1555 2.10
LINK OD1 ASP A 92 ZN ZN A2005 1555 1555 2.04
LINK OD1 ASP A 204 ZN ZN A2005 1555 1555 2.61
LINK NE2 HIS A 471 ZN ZN A2005 1555 1555 2.07
LINK O4 GUL A2003 ZN ZN A2005 1555 1555 2.19
LINK O3 GUL A2003 ZN ZN A2005 1555 1555 2.12
CISPEP 1 PHE A 405 THR A 406 0 -2.48
CISPEP 2 TRP A 531 PRO A 532 0 -1.81
CRYST1 69.019 110.019 138.961 90.00 90.00 90.00 P 21 21 21 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 0.014489 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007196 0.00000
(ATOM LINES ARE NOT SHOWN.)
END