HEADER HYDROLASE 24-AUG-00 1FO2
TITLE CRYSTAL STRUCTURE OF HUMAN CLASS I ALPHA1,2-MANNOSIDASE IN
TITLE 2 COMPLEX WITH 1-DEOXYMANNOJIRIMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA1,2-MANNOSIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL CATALYTIC DOMAIN;
COMPND 5 EC: 3.2.1.24;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS ALPHA-ALPHA7 BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VALLEE,K.KARAVEG,K.W.MOREMEN,A.HERSCOVICS,P.L.HOWELL
REVDAT 3 24-FEB-09 1FO2 1 VERSN
REVDAT 2 31-DEC-02 1FO2 1 REMARK
REVDAT 1 17-JAN-01 1FO2 0
JRNL AUTH F.VALLEE,K.KARAVEG,A.HERSCOVICS,K.W.MOREMEN,
JRNL AUTH 2 P.L.HOWELL
JRNL TITL STRUCTURAL BASIS FOR CATALYSIS AND INHIBITION OF
JRNL TITL 2 N-GLYCAN PROCESSING CLASS I ALPHA 1,2-MANNOSIDASES.
JRNL REF J.BIOL.CHEM. V. 275 41287 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10995765
JRNL DOI 10.1074/JBC.M006927200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.38 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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 164072.900
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 27901
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1357
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.38
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.53
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3979
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 224
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3685
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 399
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.27000
REMARK 3 B22 (A**2) : 7.27000
REMARK 3 B33 (A**2) : -14.54000
REMARK 3 B12 (A**2) : 1.51000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.81
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.020 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.890 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 60.38
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : DMNJ.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FO2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011758.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 129911
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.380
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES,AMMONIUM SULFATE,CALCIUM,DMNJ,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.70600
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 91.41200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.41200
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 45.70600
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 TRP A 389
REMARK 465 THR A 390
REMARK 465 PRO A 698
REMARK 465 ALA A 699
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 THR A 239 OG1 CG2
REMARK 470 ARG A 367 NH1 NH2
REMARK 470 LYS A 506 CG CD CE NZ
REMARK 470 LYS A 649 CG CD CE NZ
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 ARG A 367 NE ARG A 367 CZ 0.161
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 ARG A 367 CD - NE - CZ ANGL. DEV. = -11.8 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 SER A 280 -143.98 -127.25
REMARK 500 LYS A 371 -4.88 84.08
REMARK 500 ARG A 461 -3.28 79.33
REMARK 500 ALA A 462 -36.04 -145.74
REMARK 500 ASP A 463 -73.50 -30.73
REMARK 500 CYS A 527 2.25 -63.44
REMARK 500 PRO A 542 137.68 -38.60
REMARK 500 PRO A 578 111.51 -35.03
REMARK 500 PRO A 580 -95.89 -34.10
REMARK 500 GLU A 651 87.60 66.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 715 DISTANCE = 10.92 ANGSTROMS
REMARK 525 HOH A 731 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH A 734 DISTANCE = 22.27 ANGSTROMS
REMARK 525 HOH A 743 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A 751 DISTANCE = 11.32 ANGSTROMS
REMARK 525 HOH A 752 DISTANCE = 8.22 ANGSTROMS
REMARK 525 HOH A 759 DISTANCE = 11.47 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 8.63 ANGSTROMS
REMARK 525 HOH A 807 DISTANCE = 10.26 ANGSTROMS
REMARK 525 HOH A 816 DISTANCE = 11.46 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 14.13 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 12.94 ANGSTROMS
REMARK 525 HOH A 828 DISTANCE = 14.27 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 13.12 ANGSTROMS
REMARK 525 HOH A 851 DISTANCE = 8.81 ANGSTROMS
REMARK 525 HOH A 854 DISTANCE = 8.67 ANGSTROMS
REMARK 525 HOH A 855 DISTANCE = 10.88 ANGSTROMS
REMARK 525 HOH A 857 DISTANCE = 7.98 ANGSTROMS
REMARK 525 HOH A 861 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A 863 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH A 867 DISTANCE = 8.72 ANGSTROMS
REMARK 525 HOH A 878 DISTANCE = 11.57 ANGSTROMS
REMARK 525 HOH A 881 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A 904 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH A 907 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH A 913 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A 915 DISTANCE = 9.68 ANGSTROMS
REMARK 525 HOH A 948 DISTANCE = 10.39 ANGSTROMS
REMARK 525 HOH A 951 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH A 955 DISTANCE = 24.16 ANGSTROMS
REMARK 525 HOH A 964 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH A 979 DISTANCE = 17.38 ANGSTROMS
REMARK 525 HOH A1016 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A1024 DISTANCE = 10.76 ANGSTROMS
REMARK 525 HOH A1027 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH A1043 DISTANCE = 9.19 ANGSTROMS
REMARK 525 HOH A1046 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 8.48 ANGSTROMS
REMARK 525 HOH A1071 DISTANCE = 6.07 ANGSTROMS
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 CA A 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 688 O
REMARK 620 2 THR A 688 OG1 69.1
REMARK 620 3 DMJ A 704 O2 79.0 67.5
REMARK 620 4 HOH A 705 O 88.1 79.3 146.8
REMARK 620 5 HOH A 708 O 142.7 74.8 95.9 76.0
REMARK 620 6 HOH A 710 O 93.3 153.1 130.8 79.9 116.2
REMARK 620 7 HOH A 709 O 146.0 123.8 78.8 123.7 65.2 82.3
REMARK 620 8 DMJ A 704 O3 69.9 119.2 62.2 140.6 139.9 69.5 77.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMJ A 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FMI RELATED DB: PDB
REMARK 900 1FMI CONTAINS ALPHA 1,2-MANNOSIDASE.
REMARK 900 RELATED ID: 1FO3 RELATED DB: PDB
REMARK 900 1FO3 CONTAINS ALPHA 1,2-MANNOSIDASE COMPLEXED WITH
REMARK 900 KIFUNENSINE.
DBREF 1FO2 A 239 699 UNP Q9UKM7 MA1B1_HUMAN 239 699
SEQADV 1FO2 A UNP Q9UKM7 THR 242 DELETION
SEQRES 1 A 460 THR GLN GLY PRO VAL HIS LEU ASN TYR ARG GLN LYS GLY
SEQRES 2 A 460 VAL ILE ASP VAL PHE LEU HIS ALA TRP LYS GLY TYR ARG
SEQRES 3 A 460 LYS PHE ALA TRP GLY HIS ASP GLU LEU LYS PRO VAL SER
SEQRES 4 A 460 ARG SER PHE SER GLU TRP PHE GLY LEU GLY LEU THR LEU
SEQRES 5 A 460 ILE ASP ALA LEU ASP THR MET TRP ILE LEU GLY LEU ARG
SEQRES 6 A 460 LYS GLU PHE GLU GLU ALA ARG LYS TRP VAL SER LYS LYS
SEQRES 7 A 460 LEU HIS PHE GLU LYS ASP VAL ASP VAL ASN LEU PHE GLU
SEQRES 8 A 460 SER THR ILE ARG ILE LEU GLY GLY LEU LEU SER ALA TYR
SEQRES 9 A 460 HIS LEU SER GLY ASP SER LEU PHE LEU ARG LYS ALA GLU
SEQRES 10 A 460 ASP PHE GLY ASN ARG LEU MET PRO ALA PHE ARG THR PRO
SEQRES 11 A 460 SER LYS ILE PRO TYR SER ASP VAL ASN ILE GLY THR GLY
SEQRES 12 A 460 VAL ALA HIS PRO PRO ARG TRP THR SER ASP SER THR VAL
SEQRES 13 A 460 ALA GLU VAL THR SER ILE GLN LEU GLU PHE ARG GLU LEU
SEQRES 14 A 460 SER ARG LEU THR GLY ASP LYS LYS PHE GLN GLU ALA VAL
SEQRES 15 A 460 GLU LYS VAL THR GLN HIS ILE HIS GLY LEU SER GLY LYS
SEQRES 16 A 460 LYS ASP GLY LEU VAL PRO MET PHE ILE ASN THR HIS SER
SEQRES 17 A 460 GLY LEU PHE THR HIS LEU GLY VAL PHE THR LEU GLY ALA
SEQRES 18 A 460 ARG ALA ASP SER TYR TYR GLU TYR LEU LEU LYS GLN TRP
SEQRES 19 A 460 ILE GLN GLY GLY LYS GLN GLU THR GLN LEU LEU GLU ASP
SEQRES 20 A 460 TYR VAL GLU ALA ILE GLU GLY VAL ARG THR HIS LEU LEU
SEQRES 21 A 460 ARG HIS SER GLU PRO SER LYS LEU THR PHE VAL GLY GLU
SEQRES 22 A 460 LEU ALA HIS GLY ARG PHE SER ALA LYS MET ASP HIS LEU
SEQRES 23 A 460 VAL CYS PHE LEU PRO GLY THR LEU ALA LEU GLY VAL TYR
SEQRES 24 A 460 HIS GLY LEU PRO ALA SER HIS MET GLU LEU ALA GLN GLU
SEQRES 25 A 460 LEU MET GLU THR CYS TYR GLN MET ASN ARG GLN MET GLU
SEQRES 26 A 460 THR GLY LEU SER PRO GLU ILE VAL HIS PHE ASN LEU TYR
SEQRES 27 A 460 PRO GLN PRO GLY ARG ARG ASP VAL GLU VAL LYS PRO ALA
SEQRES 28 A 460 ASP ARG HIS ASN LEU LEU ARG PRO GLU THR VAL GLU SER
SEQRES 29 A 460 LEU PHE TYR LEU TYR ARG VAL THR GLY ASP ARG LYS TYR
SEQRES 30 A 460 GLN ASP TRP GLY TRP GLU ILE LEU GLN SER PHE SER ARG
SEQRES 31 A 460 PHE THR ARG VAL PRO SER GLY GLY TYR SER SER ILE ASN
SEQRES 32 A 460 ASN VAL GLN ASP PRO GLN LYS PRO GLU PRO ARG ASP LYS
SEQRES 33 A 460 MET GLU SER PHE PHE LEU GLY GLU THR LEU LYS TYR LEU
SEQRES 34 A 460 PHE LEU LEU PHE SER ASP ASP PRO ASN LEU LEU SER LEU
SEQRES 35 A 460 ASP ALA TYR VAL PHE ASN THR GLU ALA HIS PRO LEU PRO
SEQRES 36 A 460 ILE TRP THR PRO ALA
HET CA A 700 1
HET SO4 A 701 5
HET SO4 A 702 5
HET SO4 A 703 5
HET DMJ A 704 11
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM DMJ 1-DEOXYMANNOJIRIMYCIN
FORMUL 2 CA CA 2+
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 DMJ C6 H13 N O4
FORMUL 7 HOH *399(H2 O)
HELIX 1 1 ASN A 247 ALA A 268 1 22
HELIX 2 2 GLY A 288 ALA A 294 1 7
HELIX 3 3 ALA A 294 LEU A 301 1 8
HELIX 4 4 LEU A 303 LYS A 317 1 15
HELIX 5 5 LEU A 328 GLY A 347 1 20
HELIX 6 6 ASP A 348 MET A 363 1 16
HELIX 7 7 PRO A 364 ARG A 367 5 4
HELIX 8 8 VAL A 395 SER A 400 1 6
HELIX 9 9 ILE A 401 GLY A 413 1 13
HELIX 10 10 LYS A 415 LEU A 431 1 17
HELIX 11 11 ALA A 462 GLY A 476 1 15
HELIX 12 12 GLU A 480 LEU A 498 1 19
HELIX 13 13 LEU A 525 CYS A 527 5 3
HELIX 14 14 PHE A 528 HIS A 539 1 12
HELIX 15 15 PRO A 542 GLN A 562 1 21
HELIX 16 16 LYS A 588 ARG A 592 5 5
HELIX 17 17 PRO A 598 GLY A 612 1 15
HELIX 18 18 ARG A 614 THR A 631 1 18
HELIX 19 19 GLU A 657 GLU A 663 1 7
HELIX 20 20 GLU A 663 PHE A 672 1 10
SHEET 1 A 2 GLU A 273 LYS A 275 0
SHEET 2 A 2 SER A 280 SER A 282 -1 N SER A 280 O LYS A 275
SHEET 1 B 3 ASP A 325 ASN A 327 0
SHEET 2 B 3 ASP A 376 ASN A 378 -1 N VAL A 377 O VAL A 326
SHEET 3 B 3 ALA A 384 HIS A 385 -1 O HIS A 385 N ASP A 376
SHEET 1 C 3 SER A 393 THR A 394 0
SHEET 2 C 3 PHE A 442 ILE A 443 -1 N ILE A 443 O SER A 393
SHEET 3 C 3 PHE A 450 THR A 451 -1 N THR A 451 O PHE A 442
SHEET 1 D 3 VAL A 455 PHE A 456 0
SHEET 2 D 3 GLU A 512 ALA A 514 -1 O LEU A 513 N PHE A 456
SHEET 3 D 3 ARG A 517 SER A 519 -1 N ARG A 517 O ALA A 514
SHEET 1 E 2 LEU A 499 HIS A 501 0
SHEET 2 E 2 THR A 508 VAL A 510 -1 O PHE A 509 N ARG A 500
SHEET 1 F 3 LYS A 521 ASP A 523 0
SHEET 2 F 3 ILE A 571 PHE A 574 -1 N VAL A 572 O MET A 522
SHEET 3 F 3 VAL A 585 GLU A 586 -1 N GLU A 586 O HIS A 573
SHEET 1 G 2 TYR A 684 PHE A 686 0
SHEET 2 G 2 PRO A 692 PRO A 694 -1 O LEU A 693 N VAL A 685
SSBOND 1 CYS A 527 CYS A 556 1555 1555 2.03
LINK CA CA A 700 O THR A 688 1555 1555 2.58
LINK CA CA A 700 OG1 THR A 688 1555 1555 2.66
LINK CA CA A 700 O2 DMJ A 704 1555 1555 2.76
LINK CA CA A 700 O HOH A 705 1555 1555 2.69
LINK CA CA A 700 O HOH A 708 1555 1555 2.67
LINK CA CA A 700 O HOH A 710 1555 1555 2.56
LINK CA CA A 700 O HOH A 709 1555 1555 2.81
LINK CA CA A 700 O3 DMJ A 704 1555 1555 2.66
CISPEP 1 GLU A 503 PRO A 504 0 0.00
SITE 1 AC1 6 THR A 688 DMJ A 704 HOH A 705 HOH A 708
SITE 2 AC1 6 HOH A 709 HOH A 710
SITE 1 AC2 3 ARG A 500 HIS A 501 HOH A 926
SITE 1 AC3 4 TRP A 299 ARG A 304 LYS A 435 HOH A 870
SITE 1 AC4 5 TRP A 269 TRP A 313 LYS A 317 HOH A1039
SITE 2 AC4 5 HOH A1076
SITE 1 AC5 13 ARG A 334 ARG A 597 PRO A 598 GLU A 599
SITE 2 AC5 13 PHE A 659 GLU A 663 THR A 688 GLU A 689
SITE 3 AC5 13 CA A 700 HOH A 709 HOH A 710 HOH A 712
SITE 4 AC5 13 HOH A 713
CRYST1 96.174 96.174 137.118 90.00 90.00 120.00 P 31 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010398 0.006003 0.000000 0.00000
SCALE2 0.000000 0.012006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
