HEADER HYDROLASE 18-AUG-00 1FMX
TITLE STRUCTURE OF NATIVE PROTEINASE A IN THE SPACE GROUP P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACCHAROPEPSIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEINASE A;
COMPND 5 EC: 3.4.23.25
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS PROTEINASE A, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GUSTCHINA,M.LI,L.H.PHYLIP,W.E.LEES,J.KAY,A.WLODAWER
REVDAT 5 29-JUL-20 1FMX 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 04-OCT-17 1FMX 1 REMARK
REVDAT 3 13-JUL-11 1FMX 1 VERSN
REVDAT 2 24-FEB-09 1FMX 1 VERSN
REVDAT 1 31-JUL-02 1FMX 0
JRNL AUTH A.GUSTCHINA,M.LI,L.H.PHYLIP,W.E.LEES,J.KAY,A.WLODAWER
JRNL TITL AN UNUSUAL ORIENTATION FOR TYR75 IN THE ACTIVE SITE OF THE
JRNL TITL 2 ASPARTIC PROTEINASE FROM SACCHAROMYCES CEREVISIAE.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 295 1020 2002
JRNL REFN ISSN 0006-291X
JRNL PMID 12127998
JRNL DOI 10.1016/S0006-291X(02)00742-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.LI,L.PHYLIP,W.LEES,J.WINTHER,B.DUNN,A.WLODAWER,J.KAY,
REMARK 1 AUTH 2 A.GUSTCHINA
REMARK 1 TITL THE ASPARTIC PROTEINASE FROM A. CEREVISIAE FOLDS ITS OWN
REMARK 1 TITL 2 INHIBITOR INTO A HELIX
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 113 2000
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/72378
REMARK 2
REMARK 2 RESOLUTION. 2.61 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) : 2.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2089705.790
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 21354
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) : 0.205
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1038
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2518
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 129
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.033
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4996
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 95
REMARK 3 SOLVENT ATOMS : 197
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.66000
REMARK 3 B22 (A**2) : 6.86000
REMARK 3 B33 (A**2) : -2.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 10.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.36
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.54
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.330
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) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 60.63
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 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FMX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CCD
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22963
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.56200
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 (%): 54.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500, AMMONIUM SULFATE, PH 5.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 24.53700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A 77
REMARK 465 THR A 78
REMARK 465 GLY A 79
REMARK 465 SER A 80
REMARK 465 GLY B 77
REMARK 465 THR B 78
REMARK 465 GLY B 79
REMARK 465 SER B 80
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 TRP A 244 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 244 CZ3 CH2
REMARK 470 TRP B 244 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 244 CZ3 CH2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASP B 162
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 106 N CG2
REMARK 480 SER A 107 CB OG
REMARK 480 PHE A 113 CG CD1 CE1 CZ
REMARK 480 ALA A 114 CB
REMARK 480 PHE A 115 CG CD2 CE2 CZ
REMARK 480 LYS A 133 CE NZ
REMARK 480 GLU A 164 N CA CB CG CD OE1 OE2
REMARK 480 LYS A 178 NZ
REMARK 480 LYS A 180 CE NZ
REMARK 480 GLU A 209 CG CD OE1 OE2
REMARK 480 GLU A 211 CG CD OE1 OE2
REMARK 480 SER A 212 OG
REMARK 480 GLU A 237 CG
REMARK 480 LYS A 241 CD CE NZ
REMARK 480 THR A 245 N C O OG1 CG2
REMARK 480 GLY A 246 C O
REMARK 480 ASN A 253 ND2
REMARK 480 ILE A 262 CD1
REMARK 480 GLU A 296 CD OE1 OE2
REMARK 480 LYS A 327 CD
REMARK 480 GLU B 71 CD OE1 OE2
REMARK 480 LEU B 111 CD1 CD2
REMARK 480 THR B 112 OG1
REMARK 480 LYS B 133 CE NZ
REMARK 480 LYS B 161 C CE NZ
REMARK 480 THR B 163 OG1 CG2
REMARK 480 GLU B 164 CB CG CD OE1 OE2
REMARK 480 ASN B 165 ND2
REMARK 480 LYS B 178 NZ
REMARK 480 LYS B 180 CE NZ
REMARK 480 GLU B 209 CG CD OE1 OE2
REMARK 480 GLU B 211 CG CD OE1 OE2
REMARK 480 SER B 212 OG
REMARK 480 GLU B 237 CG
REMARK 480 LYS B 241 CD CE NZ
REMARK 480 THR B 245 OG1 CG2
REMARK 480 GLN B 247 CG CD OE1 NE2
REMARK 480 ASP B 251 CB CG OD1 OD2
REMARK 480 ASN B 253 ND2
REMARK 480 ILE B 262 CD1
REMARK 480 GLU B 296 CD OE1 OE2
REMARK 480 LYS B 327 CD
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 PRO B 109 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP B 162 CA - C - N ANGL. DEV. = -23.0 DEGREES
REMARK 500 CYS B 252 CA - CB - SG ANGL. DEV. = 7.0 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 ASN A 44 -3.10 -57.29
REMARK 500 TYR A 65 157.43 -44.80
REMARK 500 ASN A 68 -47.52 -144.91
REMARK 500 ASP A 88 175.24 173.80
REMARK 500 PRO A 109 -102.36 -6.30
REMARK 500 LEU A 111 -97.92 -33.64
REMARK 500 GLU A 164 -66.91 -20.51
REMARK 500 ALA A 192 -57.04 -169.53
REMARK 500 LEU A 223 -165.16 -120.84
REMARK 500 THR A 245 -41.25 -139.76
REMARK 500 ASP A 251 109.71 -56.99
REMARK 500 ASN A 257 27.41 -77.68
REMARK 500 ASN B 12 8.20 50.52
REMARK 500 ASN B 68 -39.87 -148.52
REMARK 500 PRO B 109 -38.82 -35.79
REMARK 500 LEU B 111 -85.63 0.43
REMARK 500 THR B 112 -47.02 -25.68
REMARK 500 LYS B 133 38.24 35.41
REMARK 500 GLN B 144 43.21 -68.75
REMARK 500 ASP B 145 44.01 27.45
REMARK 500 ARG B 151 148.67 -178.71
REMARK 500 SER B 160 30.34 -66.92
REMARK 500 ASP B 162 83.14 -23.32
REMARK 500 THR B 163 124.79 19.16
REMARK 500 ASN B 165 -6.47 129.71
REMARK 500 GLU B 176 -22.94 -33.54
REMARK 500 PHE B 179 141.81 -175.89
REMARK 500 ALA B 192 -77.54 -162.48
REMARK 500 ASN B 257 34.09 -86.02
REMARK 500 VAL B 281 63.24 -115.35
REMARK 500 SER B 282 99.92 69.27
REMARK 500 TYR B 316 78.13 -115.86
REMARK 500 ASN B 321 49.68 26.15
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 193 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAG C 2
REMARK 615 BMA C 3
REMARK 615 NAG A 333
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FMU RELATED DB: PDB
REMARK 900 1FMU CONTAINS THE SAME PROTEIN IN ANOTHER SPACE GROUP.
DBREF 1FMX A 1 329 UNP P07267 CARP_YEAST 77 405
DBREF 1FMX B 1 329 UNP P07267 CARP_YEAST 77 405
SEQRES 1 A 329 GLY GLY HIS ASP VAL PRO LEU THR ASN TYR LEU ASN ALA
SEQRES 2 A 329 GLN TYR TYR THR ASP ILE THR LEU GLY THR PRO PRO GLN
SEQRES 3 A 329 ASN PHE LYS VAL ILE LEU ASP THR GLY SER SER ASN LEU
SEQRES 4 A 329 TRP VAL PRO SER ASN GLU CYS GLY SER LEU ALA CYS PHE
SEQRES 5 A 329 LEU HIS SER LYS TYR ASP HIS GLU ALA SER SER SER TYR
SEQRES 6 A 329 LYS ALA ASN GLY THR GLU PHE ALA ILE GLN TYR GLY THR
SEQRES 7 A 329 GLY SER LEU GLU GLY TYR ILE SER GLN ASP THR LEU SER
SEQRES 8 A 329 ILE GLY ASP LEU THR ILE PRO LYS GLN ASP PHE ALA GLU
SEQRES 9 A 329 ALA THR SER GLU PRO GLY LEU THR PHE ALA PHE GLY LYS
SEQRES 10 A 329 PHE ASP GLY ILE LEU GLY LEU GLY TYR ASP THR ILE SER
SEQRES 11 A 329 VAL ASP LYS VAL VAL PRO PRO PHE TYR ASN ALA ILE GLN
SEQRES 12 A 329 GLN ASP LEU LEU ASP GLU LYS ARG PHE ALA PHE TYR LEU
SEQRES 13 A 329 GLY ASP THR SER LYS ASP THR GLU ASN GLY GLY GLU ALA
SEQRES 14 A 329 THR PHE GLY GLY ILE ASP GLU SER LYS PHE LYS GLY ASP
SEQRES 15 A 329 ILE THR TRP LEU PRO VAL ARG ARG LYS ALA TYR TRP GLU
SEQRES 16 A 329 VAL LYS PHE GLU GLY ILE GLY LEU GLY ASP GLU TYR ALA
SEQRES 17 A 329 GLU LEU GLU SER HIS GLY ALA ALA ILE ASP THR GLY THR
SEQRES 18 A 329 SER LEU ILE THR LEU PRO SER GLY LEU ALA GLU MET ILE
SEQRES 19 A 329 ASN ALA GLU ILE GLY ALA LYS LYS GLY TRP THR GLY GLN
SEQRES 20 A 329 TYR THR LEU ASP CYS ASN THR ARG ASP ASN LEU PRO ASP
SEQRES 21 A 329 LEU ILE PHE ASN PHE ASN GLY TYR ASN PHE THR ILE GLY
SEQRES 22 A 329 PRO TYR ASP TYR THR LEU GLU VAL SER GLY SER CYS ILE
SEQRES 23 A 329 SER ALA ILE THR PRO MET ASP PHE PRO GLU PRO VAL GLY
SEQRES 24 A 329 PRO LEU ALA ILE VAL GLY ASP ALA PHE LEU ARG LYS TYR
SEQRES 25 A 329 TYR SER ILE TYR ASP LEU GLY ASN ASN ALA VAL GLY LEU
SEQRES 26 A 329 ALA LYS ALA ILE
SEQRES 1 B 329 GLY GLY HIS ASP VAL PRO LEU THR ASN TYR LEU ASN ALA
SEQRES 2 B 329 GLN TYR TYR THR ASP ILE THR LEU GLY THR PRO PRO GLN
SEQRES 3 B 329 ASN PHE LYS VAL ILE LEU ASP THR GLY SER SER ASN LEU
SEQRES 4 B 329 TRP VAL PRO SER ASN GLU CYS GLY SER LEU ALA CYS PHE
SEQRES 5 B 329 LEU HIS SER LYS TYR ASP HIS GLU ALA SER SER SER TYR
SEQRES 6 B 329 LYS ALA ASN GLY THR GLU PHE ALA ILE GLN TYR GLY THR
SEQRES 7 B 329 GLY SER LEU GLU GLY TYR ILE SER GLN ASP THR LEU SER
SEQRES 8 B 329 ILE GLY ASP LEU THR ILE PRO LYS GLN ASP PHE ALA GLU
SEQRES 9 B 329 ALA THR SER GLU PRO GLY LEU THR PHE ALA PHE GLY LYS
SEQRES 10 B 329 PHE ASP GLY ILE LEU GLY LEU GLY TYR ASP THR ILE SER
SEQRES 11 B 329 VAL ASP LYS VAL VAL PRO PRO PHE TYR ASN ALA ILE GLN
SEQRES 12 B 329 GLN ASP LEU LEU ASP GLU LYS ARG PHE ALA PHE TYR LEU
SEQRES 13 B 329 GLY ASP THR SER LYS ASP THR GLU ASN GLY GLY GLU ALA
SEQRES 14 B 329 THR PHE GLY GLY ILE ASP GLU SER LYS PHE LYS GLY ASP
SEQRES 15 B 329 ILE THR TRP LEU PRO VAL ARG ARG LYS ALA TYR TRP GLU
SEQRES 16 B 329 VAL LYS PHE GLU GLY ILE GLY LEU GLY ASP GLU TYR ALA
SEQRES 17 B 329 GLU LEU GLU SER HIS GLY ALA ALA ILE ASP THR GLY THR
SEQRES 18 B 329 SER LEU ILE THR LEU PRO SER GLY LEU ALA GLU MET ILE
SEQRES 19 B 329 ASN ALA GLU ILE GLY ALA LYS LYS GLY TRP THR GLY GLN
SEQRES 20 B 329 TYR THR LEU ASP CYS ASN THR ARG ASP ASN LEU PRO ASP
SEQRES 21 B 329 LEU ILE PHE ASN PHE ASN GLY TYR ASN PHE THR ILE GLY
SEQRES 22 B 329 PRO TYR ASP TYR THR LEU GLU VAL SER GLY SER CYS ILE
SEQRES 23 B 329 SER ALA ILE THR PRO MET ASP PHE PRO GLU PRO VAL GLY
SEQRES 24 B 329 PRO LEU ALA ILE VAL GLY ASP ALA PHE LEU ARG LYS TYR
SEQRES 25 B 329 TYR SER ILE TYR ASP LEU GLY ASN ASN ALA VAL GLY LEU
SEQRES 26 B 329 ALA LYS ALA ILE
MODRES 1FMX ASN B 269 ASN GLYCOSYLATION SITE
MODRES 1FMX ASN B 68 ASN GLYCOSYLATION SITE
MODRES 1FMX ASN A 269 ASN GLYCOSYLATION SITE
MODRES 1FMX ASN A 68 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET NAG D 1 14
HET NAG D 2 14
HET NAG A 333 14
HET NAG B 332 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 7 HOH *197(H2 O)
HELIX 1 1 SER A 48 LEU A 53 1 6
HELIX 2 2 ASP A 58 SER A 62 5 5
HELIX 3 3 GLY A 110 GLY A 116 1 7
HELIX 4 4 TYR A 126 SER A 130 5 5
HELIX 5 5 SER A 130 VAL A 134 5 5
HELIX 6 6 PRO A 136 GLN A 144 1 9
HELIX 7 7 ASP A 175 SER A 177 5 3
HELIX 8 8 PRO A 227 GLY A 239 1 13
HELIX 9 9 ASP A 251 LEU A 258 5 8
HELIX 10 10 GLY A 273 TYR A 277 1 5
HELIX 11 11 GLY A 305 ARG A 310 1 6
HELIX 12 12 SER B 48 HIS B 54 1 7
HELIX 13 13 ASP B 58 SER B 62 5 5
HELIX 14 14 GLY B 110 PHE B 115 1 6
HELIX 15 15 TYR B 126 SER B 130 5 5
HELIX 16 16 SER B 130 VAL B 134 5 5
HELIX 17 17 PRO B 136 GLN B 144 1 9
HELIX 18 18 ASP B 175 LYS B 178 5 4
HELIX 19 19 PRO B 227 ILE B 238 1 12
HELIX 20 20 ASP B 251 LEU B 258 5 8
HELIX 21 21 GLY B 273 TYR B 277 1 5
HELIX 22 22 GLY B 305 ARG B 310 1 6
SHEET 1 A 6 HIS A 3 PRO A 6 0
SHEET 2 A 6 GLY A 167 PHE A 171 -1 N ALA A 169 O VAL A 5
SHEET 3 A 6 ARG A 151 LEU A 156 -1 O ALA A 153 N THR A 170
SHEET 4 A 6 TYR A 312 ASP A 317 -1 O SER A 314 N PHE A 154
SHEET 5 A 6 ALA A 322 ALA A 328 -1 O ALA A 322 N ASP A 317
SHEET 6 A 6 PHE A 179 PRO A 187 -1 N LYS A 180 O LYS A 327
SHEET 1 B10 THR A 8 TYR A 10 0
SHEET 2 B10 GLN A 14 LEU A 21 -1 O GLN A 14 N TYR A 10
SHEET 3 B10 GLN A 26 ASP A 33 -1 N GLN A 26 O LEU A 21
SHEET 4 B10 GLY A 120 GLY A 123 1 O GLY A 120 N ILE A 31
SHEET 5 B10 LEU A 39 PRO A 42 -1 N TRP A 40 O ILE A 121
SHEET 6 B10 LEU A 95 SER A 107 1 O ALA A 103 N VAL A 41
SHEET 7 B10 GLU A 82 ILE A 92 -1 O GLU A 82 N SER A 107
SHEET 8 B10 LYS A 66 ALA A 73 -1 O LYS A 66 N GLN A 87
SHEET 9 B10 GLU A 82 ILE A 92 -1 N GLY A 83 O PHE A 72
SHEET 10 B10 GLN A 14 LEU A 21 -1 N THR A 20 O SER A 91
SHEET 1 C 7 TYR A 268 ILE A 272 0
SHEET 2 C 7 LEU A 261 PHE A 265 -1 N LEU A 261 O ILE A 272
SHEET 3 C 7 GLU A 195 LEU A 203 -1 N GLU A 199 O ASN A 264
SHEET 4 C 7 ALA A 208 ILE A 217 -1 O ALA A 208 N ILE A 201
SHEET 5 C 7 LEU A 301 VAL A 304 1 O ALA A 302 N ALA A 216
SHEET 6 C 7 ILE A 224 LEU A 226 -1 N THR A 225 O ILE A 303
SHEET 7 C 7 ILE A 289 PRO A 291 1 O THR A 290 N LEU A 226
SHEET 1 D 4 LYS A 241 LYS A 242 0
SHEET 2 D 4 TYR A 248 LEU A 250 -1 O THR A 249 N LYS A 241
SHEET 3 D 4 SER A 284 SER A 287 -1 O CYS A 285 N LEU A 250
SHEET 4 D 4 THR A 278 VAL A 281 -1 O LEU A 279 N ILE A 286
SHEET 1 E15 THR B 184 PRO B 187 0
SHEET 2 E15 ALA B 322 LYS B 327 -1 N VAL B 323 O LEU B 186
SHEET 3 E15 TYR B 312 ASP B 317 -1 N TYR B 313 O ALA B 326
SHEET 4 E15 ARG B 151 LEU B 156 -1 O PHE B 152 N TYR B 316
SHEET 5 E15 GLY B 167 PHE B 171 -1 N GLU B 168 O TYR B 155
SHEET 6 E15 HIS B 3 TYR B 10 -1 N HIS B 3 O PHE B 171
SHEET 7 E15 GLN B 14 LEU B 21 -1 O GLN B 14 N TYR B 10
SHEET 8 E15 GLU B 82 ILE B 92 -1 N SER B 91 O THR B 20
SHEET 9 E15 LYS B 66 ALA B 73 -1 O LYS B 66 N GLN B 87
SHEET 10 E15 GLU B 82 ILE B 92 -1 O GLY B 83 N PHE B 72
SHEET 11 E15 LEU B 95 SER B 107 -1 O LEU B 95 N ILE B 92
SHEET 12 E15 LEU B 39 PRO B 42 1 O LEU B 39 N ALA B 103
SHEET 13 E15 GLY B 120 GLY B 123 -1 N ILE B 121 O TRP B 40
SHEET 14 E15 GLN B 26 ASP B 33 1 O LYS B 29 N GLY B 120
SHEET 15 E15 GLN B 14 LEU B 21 -1 N THR B 17 O VAL B 30
SHEET 1 F 9 ILE B 289 PRO B 291 0
SHEET 2 F 9 ILE B 224 LEU B 226 1 O ILE B 224 N THR B 290
SHEET 3 F 9 LEU B 301 VAL B 304 -1 N ILE B 303 O THR B 225
SHEET 4 F 9 GLY B 214 ILE B 217 1 O GLY B 214 N ALA B 302
SHEET 5 F 9 GLU B 195 LEU B 203 -1 N VAL B 196 O ALA B 215
SHEET 6 F 9 GLU B 206 GLU B 209 -1 O GLU B 206 N LEU B 203
SHEET 7 F 9 GLU B 195 LEU B 203 -1 N ILE B 201 O ALA B 208
SHEET 8 F 9 LEU B 261 PHE B 265 -1 N ILE B 262 O GLY B 202
SHEET 9 F 9 TYR B 268 ILE B 272 -1 O TYR B 268 N PHE B 265
SHEET 1 G 2 LYS B 241 LYS B 242 0
SHEET 2 G 2 TYR B 248 THR B 249 -1 O THR B 249 N LYS B 241
SHEET 1 H 2 THR B 278 GLU B 280 0
SHEET 2 H 2 CYS B 285 SER B 287 -1 N ILE B 286 O LEU B 279
SSBOND 1 CYS A 46 CYS A 51 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 285 1555 1555 2.03
SSBOND 3 CYS B 46 CYS B 51 1555 1555 2.02
SSBOND 4 CYS B 252 CYS B 285 1555 1555 2.01
LINK ND2 ASN A 68 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 269 C1 NAG A 333 1555 1555 1.46
LINK ND2 ASN B 68 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN B 269 C1 NAG B 332 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.38
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.40
CISPEP 1 THR A 23 PRO A 24 0 -1.74
CISPEP 2 GLU A 296 PRO A 297 0 0.67
CISPEP 3 GLY A 299 PRO A 300 0 -1.23
CISPEP 4 THR B 23 PRO B 24 0 -0.04
CISPEP 5 GLU B 296 PRO B 297 0 -2.94
CISPEP 6 GLY B 299 PRO B 300 0 0.08
CRYST1 82.964 49.074 94.685 90.00 96.50 90.00 P 1 21 1 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 0.012053 0.000000 0.001372 0.00000
SCALE2 0.000000 0.020377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
