HEADER HYDROLASE 14-NOV-05 2F12
TITLE CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2 IN COMPLEX
TITLE 2 WITH 3- HYDROXYPROPYL ETHER MIMETIC INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA-
COMPND 5 NEURAMINIDASE 2;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: 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: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS SIALIDASE, NEURAMINIDASE, INFLUENZA VIRUS, DRUG DESIGN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.G.CHAVAS,R.KATO,M.C.MANN,R.J.THOMSON,J.C.DYASON,M.VON
AUTHOR 2 ITZSTEIN,P.FUSI,C.TRINGALI,B.VENERANDO,G.TETTAMANTI,E.MONTI,
AUTHOR 3 S.WAKATSUKI
REVDAT 2 24-FEB-09 2F12 1 VERSN
REVDAT 1 21-NOV-06 2F12 0
JRNL AUTH L.M.G.CHAVAS,R.KATO,M.C.MANN,R.J.THOMSON,
JRNL AUTH 2 J.C.DYASON,M.VON ITZSTEIN,P.FUSI,C.TRINGALI,
JRNL AUTH 3 B.VENERANDO,G.TETTAMANTI,E.MONTI,S.WAKATSUKI
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2 IN
JRNL TITL 2 COMPLEX WITH 3- HYDROXYPROPYL ETHER MIMETIC
JRNL TITL 3 INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.27 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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.02
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) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15960
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) : 0.200
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 848
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 : 2831
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.43300
REMARK 3 B22 (A**2) : -6.85000
REMARK 3 B33 (A**2) : 10.28300
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) : 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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.41
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : 51.64
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 : HEM_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
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 2F12 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUAMTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16808
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 62.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1SNT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM/POTASSIUM PHOSPHATE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.16500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.16500
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 1.000000 0.000000 0.000000 43.79500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.98500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.79500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.98500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.16500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.79500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.98500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.16500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.79500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.98500
REMARK 290 SMTRY3 8 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 300 REMARK: THE MONOMER IN THE ASYMMETRIC UNIT FORMS THE BIOLOGICAL
REMARK 300 MOLECULE
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 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 A1104 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 43
REMARK 465 LYS A 44
REMARK 465 LYS A 45
REMARK 465 ASP A 46
REMARK 465 GLU A 47
REMARK 465 HIS A 48
REMARK 465 PRO A 186
REMARK 465 THR A 226
REMARK 465 GLY A 227
REMARK 465 GLU A 228
REMARK 465 SER A 284
REMARK 465 GLY A 285
REMARK 465 PRO A 286
REMARK 465 GLY A 287
REMARK 465 SER A 288
REMARK 465 PRO A 289
REMARK 465 LEU A 378
REMARK 465 PRO A 379
REMARK 465 GLN A 380
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 CD1 ILE A 187 CD1 LEU A 260 3555 2.12
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 GLN A 188 C ARG A 189 N -0.383
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 GLN A 188 CA - C - N ANGL. DEV. = -15.2 DEGREES
REMARK 500 GLN A 188 O - C - N ANGL. DEV. = 13.6 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 ILE A 22 70.86 58.37
REMARK 500 ASN A 86 63.94 60.29
REMARK 500 GLN A 108 25.45 -67.21
REMARK 500 THR A 110 -159.06 -114.80
REMARK 500 THR A 117 -10.57 -163.73
REMARK 500 THR A 156 -176.44 -174.04
REMARK 500 LEU A 217 -138.14 -112.88
REMARK 500 PHE A 255 77.72 -115.45
REMARK 500 GLN A 256 -76.56 -53.86
REMARK 500 PRO A 268 -65.00 -26.01
REMARK 500 PRO A 269 -110.13 -37.91
REMARK 500 ASP A 306 81.85 53.81
REMARK 500 ALA A 317 113.89 -37.73
REMARK 500 ALA A 333 -125.18 -128.89
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 A1066 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A1116 DISTANCE = 6.33 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1002
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTM A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SNT RELATED DB: PDB
REMARK 900 HUMAN NEU2 APO-FORM
REMARK 900 RELATED ID: 1SO7 RELATED DB: PDB
REMARK 900 HUMAN NEU2 SUGAR-INDUCED FORM
REMARK 900 RELATED ID: 1VCU RELATED DB: PDB
REMARK 900 HUMAN NEU2-DANA COMPLEX
REMARK 900 RELATED ID: 2F0Z RELATED DB: PDB
REMARK 900 RELATED ID: 2F10 RELATED DB: PDB
REMARK 900 RELATED ID: 2F11 RELATED DB: PDB
REMARK 900 RELATED ID: 2F13 RELATED DB: PDB
REMARK 900 RELATED ID: 2F24 RELATED DB: PDB
REMARK 900 RELATED ID: 2F25 RELATED DB: PDB
REMARK 900 RELATED ID: 2F26 RELATED DB: PDB
REMARK 900 RELATED ID: 2F27 RELATED DB: PDB
REMARK 900 RELATED ID: 2F28 RELATED DB: PDB
REMARK 900 RELATED ID: 2F29 RELATED DB: PDB
DBREF 2F12 A 1 380 UNP Q9Y3R4 NEUR2_HUMAN 1 380
SEQADV 2F12 GLY A -1 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 2F12 SER A 0 UNP Q9Y3R4 CLONING ARTIFACT
SEQRES 1 A 382 GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES 2 A 382 VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES 3 A 382 LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES 4 A 382 ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU
SEQRES 5 A 382 LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES 6 A 382 HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES 7 A 382 ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES 8 A 382 LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES 9 A 382 ILE ALA ILE PRO GLY GLN VAL THR GLU GLN GLN GLN LEU
SEQRES 10 A 382 GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES 11 A 382 SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES 12 A 382 LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES 13 A 382 SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES 14 A 382 ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES 15 A 382 TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES 16 A 382 ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES 17 A 382 ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES 18 A 382 GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES 19 A 382 THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES 20 A 382 ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES 21 A 382 GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES 22 A 382 CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES 23 A 382 GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES 24 A 382 PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES 25 A 382 LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES 26 A 382 PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES 27 A 382 LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES 28 A 382 PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES 29 A 382 VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES 30 A 382 GLU TYR LEU PRO GLN
HET PO4 A1002 5
HET HTM A1001 19
HETNAM PO4 PHOSPHATE ION
HETNAM HTM 6-(3-HYDROXYPROPOXY)-5-ACETAMIDO-5,6-DIHYDRO-4-
HETNAM 2 HTM HYDROXY-4H-PYRAN-2-CARBOXYLIC ACID
HETSYN HTM 3-HYDROXYPROPYL ETHER MIMETIC
FORMUL 2 PO4 O4 P 3-
FORMUL 3 HTM C11 H17 N O7
FORMUL 4 HOH *155(H2 O)
HELIX 1 1 PRO A 29 GLN A 31 5 3
HELIX 2 2 ALA A 61 HIS A 64 5 4
HELIX 3 3 GLU A 111 GLN A 116 1 6
HELIX 4 4 LEU A 142 GLY A 148 1 7
HELIX 5 5 PRO A 149 ARG A 152 5 4
HELIX 6 6 ALA A 317 TRP A 321 5 5
HELIX 7 7 LEU A 369 PHE A 373 1 5
SHEET 1 A 7 GLN A 8 GLN A 14 0
SHEET 2 A 7 GLU A 361 THR A 368 -1 O PHE A 364 N GLU A 10
SHEET 3 A 7 PRO A 348 ALA A 356 -1 N CYS A 352 O LEU A 365
SHEET 4 A 7 VAL A 325 THR A 342 -1 N GLY A 341 O LEU A 349
SHEET 5 A 7 ALA A 305 ASN A 312 -1 N ASP A 306 O GLY A 330
SHEET 6 A 7 GLN A 291 PRO A 298 -1 N TYR A 295 O TYR A 310
SHEET 7 A 7 SER A 275 PRO A 280 -1 N PHE A 279 O TRP A 292
SHEET 1 B 4 ALA A 19 LEU A 28 0
SHEET 2 B 4 SER A 33 ARG A 41 -1 O ARG A 41 N ALA A 19
SHEET 3 B 4 LEU A 51 ASP A 60 -1 O LEU A 51 N GLN A 40
SHEET 4 B 4 GLN A 65 TRP A 68 -1 O GLN A 65 N ASP A 60
SHEET 1 C 4 ALA A 19 LEU A 28 0
SHEET 2 C 4 SER A 33 ARG A 41 -1 O ARG A 41 N ALA A 19
SHEET 3 C 4 LEU A 51 ASP A 60 -1 O LEU A 51 N GLN A 40
SHEET 4 C 4 GLU A 72 VAL A 73 -1 O GLU A 72 N LEU A 54
SHEET 1 D 4 HIS A 82 ASP A 92 0
SHEET 2 D 4 THR A 97 PRO A 106 -1 O PHE A 99 N LEU A 90
SHEET 3 D 4 ARG A 123 SER A 129 -1 O SER A 129 N LEU A 98
SHEET 4 D 4 ARG A 140 ASP A 141 -1 O ARG A 140 N GLN A 126
SHEET 1 E 3 TRP A 154 VAL A 159 0
SHEET 2 E 3 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 E 3 LEU A 165 GLN A 166 -1 N LEU A 165 O VAL A 175
SHEET 1 F 4 TRP A 154 VAL A 159 0
SHEET 2 F 4 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 F 4 ILE A 191 SER A 199 -1 O SER A 199 N LEU A 174
SHEET 4 F 4 ALA A 207 ARG A 208 -1 O ALA A 207 N LEU A 198
SHEET 1 G 4 THR A 216 VAL A 224 0
SHEET 2 G 4 VAL A 231 SER A 238 -1 O ARG A 237 N LEU A 217
SHEET 3 G 4 ALA A 242 SER A 248 -1 O VAL A 244 N ALA A 236
SHEET 4 G 4 SER A 258 VAL A 265 -1 O VAL A 261 N ARG A 243
CISPEP 1 GLY A 160 PRO A 161 0 0.28
CISPEP 2 PRO A 315 PRO A 316 0 0.15
SITE 1 AC1 8 GLN A 14 GLY A 16 ALA A 17 HIS A 18
SITE 2 AC1 8 TYR A 20 PRO A 316 ALA A 317 HOH A1071
SITE 1 AC2 11 ARG A 21 ILE A 22 GLU A 111 LEU A 115
SITE 2 AC2 11 TYR A 181 LEU A 217 GLU A 218 ARG A 237
SITE 3 AC2 11 ARG A 304 TYR A 334 HOH A1017
CRYST1 87.590 87.970 92.330 90.00 90.00 90.00 C 2 2 21 8
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 0.011417 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010831 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
