HEADER HYDROLASE 14-NOV-05 2F1A
TITLE GOLGI ALPHA-MANNOSIDASE II COMPLEX WITH (2R,3R,4S)-2-({[(1S)-2-
TITLE 2 HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL
CAVEAT 2F1A MPD A 1801 HAS WRONG CHIRALITY AT ATOM C4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-MANNOSIDASE II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
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, GMII;
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 CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMTBIP_NHIS
KEYWDS GLYCOSYL HYDROLASE FAMILY 38, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.KUNTZ,D.R.ROSE
REVDAT 6 23-AUG-23 2F1A 1 HETSYN
REVDAT 5 29-JUL-20 2F1A 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE
REVDAT 4 13-JUL-11 2F1A 1 VERSN
REVDAT 3 24-FEB-09 2F1A 1 VERSN
REVDAT 2 23-OCT-07 2F1A 1 JRNL
REVDAT 1 05-DEC-06 2F1A 0
JRNL AUTH P.ENGLEBIENNE,H.FIAUX,D.A.KUNTZ,C.R.CORBEIL,
JRNL AUTH 2 S.GERBER-LEMAIRE,D.R.ROSE,N.MOITESSIER
JRNL TITL EVALUATION OF DOCKING PROGRAMS FOR PREDICTING BINDING OF
JRNL TITL 2 GOLGI ALPHA-MANNOSIDASE II INHIBITORS: A COMPARISON WITH
JRNL TITL 3 CRYSTALLOGRAPHY.
JRNL REF PROTEINS V. 69 160 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 17557336
JRNL DOI 10.1002/PROT.21479
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 96240.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 174398
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) : 0.168
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.300
REMARK 3 FREE R VALUE TEST SET COUNT : 3983
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 24945
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 524
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 1099
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.42000
REMARK 3 B22 (A**2) : 0.75000
REMARK 3 B33 (A**2) : 0.67000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 30.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.180
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) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.050 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.460 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.730 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 43.97
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : GB2.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 PARAMETER FILE 7 : NULL
REMARK 3 PARAMETER FILE 8 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : CIS_PEPTIDE.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : PO4.TOP
REMARK 3 TOPOLOGY FILE 7 : GB2.TOP
REMARK 3 TOPOLOGY FILE 8 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035327.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793376
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 180243
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
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 (%) : 96.3
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 0.57000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.720
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: PDB ENTRY 1HWW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG 6K, MPD, NACL, 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 34.45200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.29250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.68000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.29250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.45200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.68000
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 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 GLN A 97 CG GLN A 97 CD 0.171
REMARK 500 SER A 411 CA SER A 411 CB 0.182
REMARK 500 ARG A 770 CB ARG A 770 CG -0.202
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 ASP A 204 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 818 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 963 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 963 NE - CZ - NH2 ANGL. DEV. = -3.2 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 78.55 -103.63
REMARK 500 TRP A 95 -86.15 -172.00
REMARK 500 ASP A 106 -58.11 -131.62
REMARK 500 THR A 162 -64.05 68.54
REMARK 500 GLN A 227 -45.99 -137.57
REMARK 500 ASP A 340 -170.61 -170.66
REMARK 500 LYS A 345 -71.52 -92.62
REMARK 500 SER A 411 -122.07 40.53
REMARK 500 TRP A 415 58.07 -90.32
REMARK 500 HIS A 471 4.53 -69.76
REMARK 500 ILE A 549 -47.26 -148.69
REMARK 500 LEU A 550 116.03 -165.95
REMARK 500 PRO A 562 38.61 -80.62
REMARK 500 SER A 703 158.17 -42.70
REMARK 500 ASN A 732 56.63 -97.04
REMARK 500 SER A 762 -3.25 71.36
REMARK 500 ILE A 831 77.59 -118.10
REMARK 500 SER A 833 -13.45 -153.13
REMARK 500 ASP A 839 -162.11 -128.08
REMARK 500 PRO A 990 -79.51 -39.17
REMARK 500 GLU A 991 94.17 55.41
REMARK 500 GLU A 992 -139.38 -134.40
REMARK 500 HIS A 993 72.50 33.34
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 TYR A 75 12.77
REMARK 500 HIS A 709 10.62
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 A1805 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 90 NE2
REMARK 620 2 ASP A 92 OD1 93.2
REMARK 620 3 ASP A 204 OD2 96.8 168.1
REMARK 620 4 HIS A 471 NE2 104.7 91.7 92.1
REMARK 620 5 GB2 A1804 O3 162.5 86.5 82.1 92.8
REMARK 620 6 GB2 A1804 O4 90.3 89.8 83.7 164.8 72.2
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: 1PS2 RELATED DB: PDB
REMARK 900 RELATED ID: 1QWN RELATED DB: PDB
REMARK 900 RELATED ID: 1QX1 RELATED DB: PDB
REMARK 900 RELATED ID: 1R33 RELATED DB: PDB
REMARK 900 RELATED ID: 1R34 RELATED DB: PDB
REMARK 900 RELATED ID: 1TQS RELATED DB: PDB
REMARK 900 RELATED ID: 1TQT RELATED DB: PDB
REMARK 900 RELATED ID: 1TQU RELATED DB: PDB
REMARK 900 RELATED ID: 1TQW RELATED DB: PDB
REMARK 900 RELATED ID: 2ALW RELATED DB: PDB
REMARK 900 RELATED ID: 2F18 RELATED DB: PDB
REMARK 900 RELATED ID: 2F1B RELATED DB: PDB
DBREF 2F1A A 13 1045 GB 517481 CAA54732 76 1108
SEQADV 2F1A ARG A 1 GB 517481 EXPRESSION TAG
SEQADV 2F1A SER A 2 GB 517481 EXPRESSION TAG
SEQADV 2F1A SER A 3 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 4 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 5 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 6 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 7 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 8 GB 517481 EXPRESSION TAG
SEQADV 2F1A HIS A 9 GB 517481 EXPRESSION TAG
SEQADV 2F1A GLY A 10 GB 517481 EXPRESSION TAG
SEQADV 2F1A GLU A 11 GB 517481 EXPRESSION TAG
SEQADV 2F1A PHE A 12 GB 517481 EXPRESSION TAG
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 2F1A ASN A 194 ASN GLYCOSYLATION SITE
HET NAG A1802 14
HET PO4 A1803 5
HET ZN A1805 1
HET GB2 A1804 18
HET MPD A1801 8
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETNAM ZN ZINC ION
HETNAM GB2 (2R,3R,4S)-2-({[(1S)-2-HYDROXY-1-
HETNAM 2 GB2 PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-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
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 PO4 O4 P 3-
FORMUL 4 ZN ZN 2+
FORMUL 5 GB2 C13 H20 N2 O3
FORMUL 6 MPD C6 H14 O2
FORMUL 7 HOH *1099(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 HIS A 139 1 10
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 SER A 200 O ASN A 223
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 2 ALA A 408 ARG A 410 0
SHEET 2 D 2 ASN A 413 TYR A 414 -1 O ASN A 413 N ARG A 410
SHEET 1 E 6 PHE A 524 ASP A 527 0
SHEET 2 E 6 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 E 6 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 E 6 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 E 6 VAL A 578 ASP A 582 -1 N THR A 581 O VAL A 633
SHEET 6 E 6 PRO A 587 VAL A 588 -1 O VAL A 588 N VAL A 580
SHEET 1 F 5 PHE A 524 ASP A 527 0
SHEET 2 F 5 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 F 5 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 F 5 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 F 5 GLN A 945 PHE A 946 -1 O PHE A 946 N LEU A 629
SHEET 1 G 5 THR A 542 ILE A 543 0
SHEET 2 G 5 ARG A 565 VAL A 573 1 O TYR A 572 N ILE A 543
SHEET 3 G 5 THR A 606 VAL A 624 -1 O ILE A 618 N PHE A 571
SHEET 4 G 5 ALA A 590 ASP A 601 -1 N SER A 593 O ARG A 617
SHEET 5 G 5 THR A 644 TYR A 646 1 O SER A 645 N VAL A 592
SHEET 1 H12 LYS A 669 GLY A 671 0
SHEET 2 H12 SER A 648 LEU A 652 1 N LEU A 651 O LYS A 669
SHEET 3 H12 VAL A 745 LYS A 749 -1 O VAL A 745 N LEU A 652
SHEET 4 H12 SER A 754 LEU A 760 -1 O SER A 757 N LEU A 746
SHEET 5 H12 VAL A 763 MET A 769 -1 O MET A 769 N SER A 754
SHEET 6 H12 GLU A 775 VAL A 780 -1 O GLU A 775 N ILE A 768
SHEET 7 H12 VAL A 888 LYS A 898 -1 O VAL A 888 N VAL A 780
SHEET 8 H12 THR A 842 THR A 848 -1 N THR A 845 O VAL A 895
SHEET 9 H12 GLY A 834 GLU A 838 -1 N MET A 835 O LEU A 846
SHEET 10 H12 ILE A 803 LEU A 808 -1 N TYR A 805 O PHE A 836
SHEET 11 H12 GLN A 812 ARG A 817 -1 O ARG A 816 N PHE A 804
SHEET 12 H12 ALA A 911 GLY A 912 -1 O GLY A 912 N PHE A 813
SHEET 1 I 5 ILE A 676 ARG A 679 0
SHEET 2 I 5 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 I 5 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 I 5 VAL A 706 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 I 5 SER A 736 PRO A 737 -1 O SER A 736 N LYS A 714
SHEET 1 J 8 ILE A 676 ARG A 679 0
SHEET 2 J 8 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 J 8 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 J 8 VAL A 706 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 J 8 THR A 788 THR A 796 -1 O ARG A 793 N LYS A 711
SHEET 6 J 8 GLU A 861 ARG A 869 -1 O GLN A 866 N ILE A 790
SHEET 7 J 8 LEU A 852 SER A 855 -1 N GLY A 853 O MET A 865
SHEET 8 J 8 TYR A 829 ILE A 831 -1 N TYR A 829 O GLY A 854
SHEET 1 K 5 LEU A 957 ARG A 964 0
SHEET 2 K 5 GLN A 973 ARG A 981 -1 O GLY A 976 N ARG A 963
SHEET 3 K 5 THR A1036 HIS A1043 -1 O ALA A1037 N LEU A 979
SHEET 4 K 5 VAL A1006 THR A1012 -1 N ALA A1007 O SER A1042
SHEET 5 K 5 ASN A1019 HIS A1022 -1 O LEU A1020 N ARG A1011
SSBOND 1 CYS A 31 CYS A 1032 1555 1555 2.05
SSBOND 2 CYS A 275 CYS A 282 1555 1555 2.04
SSBOND 3 CYS A 283 CYS A 297 1555 1555 2.09
SSBOND 4 CYS A 902 CYS A 987 1555 1555 2.07
SSBOND 5 CYS A 1000 CYS A 1009 1555 1555 2.01
LINK ND2 ASN A 194 C1 NAG A1802 1555 1555 1.45
LINK NE2 HIS A 90 ZN ZN A1805 1555 1555 2.11
LINK OD1 ASP A 92 ZN ZN A1805 1555 1555 2.16
LINK OD2 ASP A 204 ZN ZN A1805 1555 1555 2.08
LINK NE2 HIS A 471 ZN ZN A1805 1555 1555 2.09
LINK O3 GB2 A1804 ZN ZN A1805 1555 1555 2.20
LINK O4 GB2 A1804 ZN ZN A1805 1555 1555 2.35
CISPEP 1 PHE A 405 THR A 406 0 -1.27
CISPEP 2 TRP A 531 PRO A 532 0 0.21
CRYST1 68.904 109.360 138.585 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 0.014513 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009144 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
