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HEADER HYDROLASE 17-MAY-02 1GZ7
TITLE CRYSTAL STRUCTURE OF THE CLOSED STATE OF LIPASE 2 FROM
TITLE 2 CANDIDA RUGOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA RUGOSA;
SOURCE 3 ORGANISM_COMMON: YEAST
KEYWDS HYDROLASE, CARBOXYLIC ESTERASE, GLYCOPROTEIN.
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MANCHENO,J.A.HERMOSO
REVDAT 1 12-JUN-03 1GZ7 0
JRNL AUTH J.M.MANCHENO,M.A.PERNAS,M.L.RUA,J.A.HERMOSO
JRNL TITL THE CLOSED STATE OF THE LIPASE 2 FROM CANDIDA
JRNL TITL 2 RUGOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.ALBERGHINA,M.LOTTI
REMARK 1 TITL CLONING, SEQUENCING, AND EXPRESSION OF CANDIDA
REMARK 1 TITL 2 RUGOSA LIPASES
REMARK 1 REF METHODS ENZYMOL. V. 284 246 1997
REMARK 1 REFN ASTM MENZAU US ISSN 0076-6879
REMARK 1 REFERENCE 2
REMARK 1 AUTH Y.KAWAGUCHI,H.HONDA,J.TANIGUCHI-MORIMURA,S.IWASAKI
REMARK 1 TITL THE CODON CUG IS READ AS SERINE IN AN ASPOROGENIC
REMARK 1 TITL 2 YEAST CANDIDA CYLINDRACEA
REMARK 1 REF NATURE V. 341 164 1989
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 935285.74
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 151824
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 : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 7672
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) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.5
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19977
REMARK 3 BIN R VALUE (WORKING SET) : 0.315
REMARK 3 BIN FREE R VALUE : 0.331
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1074
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 1471
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.91
REMARK 3 B22 (A**2) : -2.09
REMARK 3 B33 (A**2) : 0.18
REMARK 3 B12 (A**2) : 8.08
REMARK 3 B13 (A**2) : -8.09
REMARK 3 B23 (A**2) : 0.57
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
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 : 0.42525
REMARK 3 BSOL : 66.0866
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : CRY_XPLOR_PAR.TXT
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CRY_XPLOR_TOP.TXT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ELECTRON DENSITY CORRESPONDING
REMARK 3 TO RESIDUES 78 AND 79 IS NOT CONSISTENT WITH THE SEQUENCE
REMARK 3 DESCRIBED FOR LIPASE2 (ARG-HIS), BUT WITH LEU-ASP,
REMARK 3 PRECISELY THE SEQUENCE DESCRIBED FOR LIPASE 1 AND LIPASE 3.
REMARK 4
REMARK 4 1GZ7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-MAY-2002.
REMARK 100 THE EBI ID CODE IS EBI-9821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-2001
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE BM14
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.004
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152503
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.97
REMARK 200 RESOLUTION RANGE LOW (A) : 37.11
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 2.0
REMARK 200 R MERGE (I) : 0.095
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.6
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.1
REMARK 200 R MERGE FOR SHELL (I) : 0.299
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.2
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1TRH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (W/V) PEG 4000,
REMARK 280 SODIUM ACETATE 0.1M, PH 5.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE A 23 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 GLY A 57 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 LYS A 75 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP A 96 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LEU A 164 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASN A 192 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 294 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 LEU A 302 CA - CB - CG ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 303 N - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ILE A 315 N - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 THR A 316 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLN A 338 N - CA - C ANGL. DEV. = -11.1 DEGREES
REMARK 500 GLY A 342 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 VAL A 352 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 PRO A 390 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 THR A 400 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 PHE A 415 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 THR A 416 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 MET A 503 N - CA - C ANGL. DEV. = -10.7 DEGREES
REMARK 500 PHE A 526 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 PHE B 23 N - CA - C ANGL. DEV. = -10.4 DEGREES
REMARK 500 LYS B 39 N - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 ASP B 96 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 ASN B 192 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 VAL B 245 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG B 303 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ILE B 315 N - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 THR B 316 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ILE B 334 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLN B 338 N - CA - C ANGL. DEV. = -11.3 DEGREES
REMARK 500 GLY B 342 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 390 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 THR B 400 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 THR B 416 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 PHE B 448 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 MET B 503 N - CA - C ANGL. DEV. = -10.9 DEGREES
REMARK 500 PHE B 526 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 PHE C 23 N - CA - C ANGL. DEV. = -10.9 DEGREES
REMARK 500 LYS C 39 N - CA - C ANGL. DEV. = -19.9 DEGREES
REMARK 500 LYS C 39 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP C 96 N - CA - C ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU C 164 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASN C 192 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG C 303 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ILE C 334 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLN C 338 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLY C 342 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 PHE C 415 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 THR C 416 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 PHE C 448 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 MET C 503 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 PHE C 526 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 PHE D 23 N - CA - C ANGL. DEV. = -11.3 DEGREES
REMARK 500 LYS D 39 N - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 ASP D 96 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASN D 192 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG D 303 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 ILE D 315 N - CA - C ANGL. DEV. = -13.8 DEGREES
REMARK 500 THR D 316 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLN D 338 N - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 GLY D 342 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 VAL D 352 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 PRO D 390 C - N - CA ANGL. DEV. = 8.3 DEGREES
REMARK 500 PHE D 415 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 THR D 416 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 PHE D 448 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 MET D 503 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 PHE D 526 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 O ALA A 7 O HOH Z 4 2.13
REMARK 500 O ILE A 395 O HOH Z 361 2.15
REMARK 500 OG SER B 498 O HOH Y 319 1.63
REMARK 500 O GLY C 146 O HOH X 98 1.97
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
REMARK 500 O GLY B 280 CD PRO C 31 1645 2.07
REMARK 500 O HOH W 6 O HOH W 251 1455 2.03
REMARK 500 O HOH W 12 O HOH W 339 1455 2.09
REMARK 500 O HOH W 14 O HOH W 94 1455 2.12
REMARK 500 O HOH X 33 O HOH Y 179 1465 1.59
REMARK 500 O HOH X 80 O HOH W 231 1455 2.01
REMARK 500 O HOH Z 40 O HOH Z 150 1655 1.95
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 ILE A 18 -65.27 71.58
REMARK 500 SER A 209 -115.49 54.95
REMARK 500 VAL A 444 -53.22 70.37
REMARK 500 ILE B 18 -61.66 67.96
REMARK 500 SER B 209 -116.16 54.43
REMARK 500 VAL B 444 -45.28 71.59
REMARK 500 ILE C 18 -64.74 70.32
REMARK 500 VAL C 444 -43.02 72.16
REMARK 500 ILE D 18 -53.81 70.67
REMARK 500 VAL D 444 -45.77 73.75
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE C 38 LYS C 39 212.93
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 525 C X
REMARK 525 D W
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D
DBREF 1GZ7 A 1 534 SWS P32946 LIP2_CANRU 15 548
DBREF 1GZ7 B 1 534 SWS P32946 LIP2_CANRU 15 548
DBREF 1GZ7 C 1 534 SWS P32946 LIP2_CANRU 15 548
DBREF 1GZ7 D 1 534 SWS P32946 LIP2_CANRU 15 548
SEQADV 1GZ7 LEU A 78 SWS P32946 ARG 92 CONFLICT
SEQADV 1GZ7 ASP A 79 SWS P32946 HIS 93 CONFLICT
SEQADV 1GZ7 LEU B 78 SWS P32946 ARG 92 CONFLICT
SEQADV 1GZ7 ASP B 79 SWS P32946 HIS 93 CONFLICT
SEQADV 1GZ7 LEU C 78 SWS P32946 ARG 92 CONFLICT
SEQADV 1GZ7 ASP C 79 SWS P32946 HIS 93 CONFLICT
SEQADV 1GZ7 LEU D 78 SWS P32946 ARG 92 CONFLICT
SEQADV 1GZ7 ASP D 79 SWS P32946 HIS 93 CONFLICT
SEQRES 1 A 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 A 534 GLY LEU ASN ALA ILE VAL ASN GLU LYS PHE LEU GLY ILE
SEQRES 3 A 534 PRO PHE ALA GLU PRO PRO VAL GLY THR LEU ARG PHE LYS
SEQRES 4 A 534 PRO PRO VAL PRO TYR SER ALA SER LEU ASN GLY GLN GLN
SEQRES 5 A 534 PHE THR SER TYR GLY PRO SER CYS MET GLN MET ASN PRO
SEQRES 6 A 534 MET GLY SER PHE GLU ASP THR LEU PRO LYS ASN ALA LEU
SEQRES 7 A 534 ASP LEU VAL LEU GLN SER LYS ILE PHE GLN VAL VAL LEU
SEQRES 8 A 534 PRO ASN ASP GLU ASP CYS LEU THR ILE ASN VAL ILE ARG
SEQRES 9 A 534 PRO PRO GLY THR ARG ALA SER ALA GLY LEU PRO VAL MET
SEQRES 10 A 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU LEU GLY GLY SER
SEQRES 11 A 534 SER LEU PHE PRO GLY ASP GLN MET VAL ALA LYS SER VAL
SEQRES 12 A 534 LEU MET GLY LYS PRO VAL ILE HIS VAL SER MET ASN TYR
SEQRES 13 A 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY PRO ASP ILE
SEQRES 14 A 534 GLN ASN GLU GLY SER GLY ASN ALA GLY LEU HIS ASP GLN
SEQRES 15 A 534 ARG LEU ALA MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 A 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE TYR GLY GLU
SEQRES 17 A 534 SER ALA GLY SER MET SER THR PHE VAL HIS LEU VAL TRP
SEQRES 18 A 534 ASN ASP GLY ASP ASN THR TYR ASN GLY LYS PRO LEU PHE
SEQRES 19 A 534 ARG ALA ALA ILE MET GLN SER GLY CYS MET VAL PRO SER
SEQRES 20 A 534 ASP PRO VAL ASP GLY THR TYR GLY THR GLU ILE TYR ASN
SEQRES 21 A 534 GLN VAL VAL ALA SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 A 534 LYS LEU ALA CYS LEU ARG GLY LEU SER GLN ASP THR LEU
SEQRES 23 A 534 TYR GLN ALA THR SER ASP THR PRO GLY VAL LEU ALA TYR
SEQRES 24 A 534 PRO SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 A 534 THR PHE ILE THR ASP ASP MET TYR ALA LEU VAL ARG ASP
SEQRES 26 A 534 GLY LYS TYR ALA HIS VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 A 534 ASN ASP GLU GLY THR LEU PHE GLY LEU SER SER LEU ASN
SEQRES 28 A 534 VAL THR THR ASP ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 A 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 A 534 MET ALA ALA TYR THR SER ASP ILE THR GLN GLY SER PRO
SEQRES 31 A 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 A 534 LYS ARG ILE SER ALA LEU LEU GLY ASP LEU ALA PHE THR
SEQRES 33 A 534 LEU ALA ARG ARG TYR PHE LEU ASN TYR TYR GLN GLY GLY
SEQRES 34 A 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 A 534 PRO VAL LEU GLY THR PHE HIS GLY ASN ASP ILE ILE TRP
SEQRES 36 A 534 GLN ASP TYR LEU VAL GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 A 534 ASN ALA PHE ILE ALA PHE ALA ASN ASP LEU ASP PRO ASN
SEQRES 38 A 534 LYS ALA GLY LEU TRP THR ASN TRP PRO THR TYR THR SER
SEQRES 39 A 534 SER SER GLN SER GLY ASN ASN LEU MET GLN ILE ASN GLY
SEQRES 40 A 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG PRO ASP
SEQRES 41 A 534 ALA TYR SER ALA LEU PHE SER ASN PRO PRO SER PHE PHE
SEQRES 42 A 534 VAL
SEQRES 1 B 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 B 534 GLY LEU ASN ALA ILE VAL ASN GLU LYS PHE LEU GLY ILE
SEQRES 3 B 534 PRO PHE ALA GLU PRO PRO VAL GLY THR LEU ARG PHE LYS
SEQRES 4 B 534 PRO PRO VAL PRO TYR SER ALA SER LEU ASN GLY GLN GLN
SEQRES 5 B 534 PHE THR SER TYR GLY PRO SER CYS MET GLN MET ASN PRO
SEQRES 6 B 534 MET GLY SER PHE GLU ASP THR LEU PRO LYS ASN ALA LEU
SEQRES 7 B 534 ASP LEU VAL LEU GLN SER LYS ILE PHE GLN VAL VAL LEU
SEQRES 8 B 534 PRO ASN ASP GLU ASP CYS LEU THR ILE ASN VAL ILE ARG
SEQRES 9 B 534 PRO PRO GLY THR ARG ALA SER ALA GLY LEU PRO VAL MET
SEQRES 10 B 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU LEU GLY GLY SER
SEQRES 11 B 534 SER LEU PHE PRO GLY ASP GLN MET VAL ALA LYS SER VAL
SEQRES 12 B 534 LEU MET GLY LYS PRO VAL ILE HIS VAL SER MET ASN TYR
SEQRES 13 B 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY PRO ASP ILE
SEQRES 14 B 534 GLN ASN GLU GLY SER GLY ASN ALA GLY LEU HIS ASP GLN
SEQRES 15 B 534 ARG LEU ALA MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 B 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE TYR GLY GLU
SEQRES 17 B 534 SER ALA GLY SER MET SER THR PHE VAL HIS LEU VAL TRP
SEQRES 18 B 534 ASN ASP GLY ASP ASN THR TYR ASN GLY LYS PRO LEU PHE
SEQRES 19 B 534 ARG ALA ALA ILE MET GLN SER GLY CYS MET VAL PRO SER
SEQRES 20 B 534 ASP PRO VAL ASP GLY THR TYR GLY THR GLU ILE TYR ASN
SEQRES 21 B 534 GLN VAL VAL ALA SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 B 534 LYS LEU ALA CYS LEU ARG GLY LEU SER GLN ASP THR LEU
SEQRES 23 B 534 TYR GLN ALA THR SER ASP THR PRO GLY VAL LEU ALA TYR
SEQRES 24 B 534 PRO SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 B 534 THR PHE ILE THR ASP ASP MET TYR ALA LEU VAL ARG ASP
SEQRES 26 B 534 GLY LYS TYR ALA HIS VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 B 534 ASN ASP GLU GLY THR LEU PHE GLY LEU SER SER LEU ASN
SEQRES 28 B 534 VAL THR THR ASP ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 B 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 B 534 MET ALA ALA TYR THR SER ASP ILE THR GLN GLY SER PRO
SEQRES 31 B 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 B 534 LYS ARG ILE SER ALA LEU LEU GLY ASP LEU ALA PHE THR
SEQRES 33 B 534 LEU ALA ARG ARG TYR PHE LEU ASN TYR TYR GLN GLY GLY
SEQRES 34 B 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 B 534 PRO VAL LEU GLY THR PHE HIS GLY ASN ASP ILE ILE TRP
SEQRES 36 B 534 GLN ASP TYR LEU VAL GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 B 534 ASN ALA PHE ILE ALA PHE ALA ASN ASP LEU ASP PRO ASN
SEQRES 38 B 534 LYS ALA GLY LEU TRP THR ASN TRP PRO THR TYR THR SER
SEQRES 39 B 534 SER SER GLN SER GLY ASN ASN LEU MET GLN ILE ASN GLY
SEQRES 40 B 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG PRO ASP
SEQRES 41 B 534 ALA TYR SER ALA LEU PHE SER ASN PRO PRO SER PHE PHE
SEQRES 42 B 534 VAL
SEQRES 1 C 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 C 534 GLY LEU ASN ALA ILE VAL ASN GLU LYS PHE LEU GLY ILE
SEQRES 3 C 534 PRO PHE ALA GLU PRO PRO VAL GLY THR LEU ARG PHE LYS
SEQRES 4 C 534 PRO PRO VAL PRO TYR SER ALA SER LEU ASN GLY GLN GLN
SEQRES 5 C 534 PHE THR SER TYR GLY PRO SER CYS MET GLN MET ASN PRO
SEQRES 6 C 534 MET GLY SER PHE GLU ASP THR LEU PRO LYS ASN ALA LEU
SEQRES 7 C 534 ASP LEU VAL LEU GLN SER LYS ILE PHE GLN VAL VAL LEU
SEQRES 8 C 534 PRO ASN ASP GLU ASP CYS LEU THR ILE ASN VAL ILE ARG
SEQRES 9 C 534 PRO PRO GLY THR ARG ALA SER ALA GLY LEU PRO VAL MET
SEQRES 10 C 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU LEU GLY GLY SER
SEQRES 11 C 534 SER LEU PHE PRO GLY ASP GLN MET VAL ALA LYS SER VAL
SEQRES 12 C 534 LEU MET GLY LYS PRO VAL ILE HIS VAL SER MET ASN TYR
SEQRES 13 C 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY PRO ASP ILE
SEQRES 14 C 534 GLN ASN GLU GLY SER GLY ASN ALA GLY LEU HIS ASP GLN
SEQRES 15 C 534 ARG LEU ALA MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 C 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE TYR GLY GLU
SEQRES 17 C 534 SER ALA GLY SER MET SER THR PHE VAL HIS LEU VAL TRP
SEQRES 18 C 534 ASN ASP GLY ASP ASN THR TYR ASN GLY LYS PRO LEU PHE
SEQRES 19 C 534 ARG ALA ALA ILE MET GLN SER GLY CYS MET VAL PRO SER
SEQRES 20 C 534 ASP PRO VAL ASP GLY THR TYR GLY THR GLU ILE TYR ASN
SEQRES 21 C 534 GLN VAL VAL ALA SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 C 534 LYS LEU ALA CYS LEU ARG GLY LEU SER GLN ASP THR LEU
SEQRES 23 C 534 TYR GLN ALA THR SER ASP THR PRO GLY VAL LEU ALA TYR
SEQRES 24 C 534 PRO SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 C 534 THR PHE ILE THR ASP ASP MET TYR ALA LEU VAL ARG ASP
SEQRES 26 C 534 GLY LYS TYR ALA HIS VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 C 534 ASN ASP GLU GLY THR LEU PHE GLY LEU SER SER LEU ASN
SEQRES 28 C 534 VAL THR THR ASP ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 C 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 C 534 MET ALA ALA TYR THR SER ASP ILE THR GLN GLY SER PRO
SEQRES 31 C 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 C 534 LYS ARG ILE SER ALA LEU LEU GLY ASP LEU ALA PHE THR
SEQRES 33 C 534 LEU ALA ARG ARG TYR PHE LEU ASN TYR TYR GLN GLY GLY
SEQRES 34 C 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 C 534 PRO VAL LEU GLY THR PHE HIS GLY ASN ASP ILE ILE TRP
SEQRES 36 C 534 GLN ASP TYR LEU VAL GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 C 534 ASN ALA PHE ILE ALA PHE ALA ASN ASP LEU ASP PRO ASN
SEQRES 38 C 534 LYS ALA GLY LEU TRP THR ASN TRP PRO THR TYR THR SER
SEQRES 39 C 534 SER SER GLN SER GLY ASN ASN LEU MET GLN ILE ASN GLY
SEQRES 40 C 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG PRO ASP
SEQRES 41 C 534 ALA TYR SER ALA LEU PHE SER ASN PRO PRO SER PHE PHE
SEQRES 42 C 534 VAL
SEQRES 1 D 534 ALA PRO THR ALA THR LEU ALA ASN GLY ASP THR ILE THR
SEQRES 2 D 534 GLY LEU ASN ALA ILE VAL ASN GLU LYS PHE LEU GLY ILE
SEQRES 3 D 534 PRO PHE ALA GLU PRO PRO VAL GLY THR LEU ARG PHE LYS
SEQRES 4 D 534 PRO PRO VAL PRO TYR SER ALA SER LEU ASN GLY GLN GLN
SEQRES 5 D 534 PHE THR SER TYR GLY PRO SER CYS MET GLN MET ASN PRO
SEQRES 6 D 534 MET GLY SER PHE GLU ASP THR LEU PRO LYS ASN ALA LEU
SEQRES 7 D 534 ASP LEU VAL LEU GLN SER LYS ILE PHE GLN VAL VAL LEU
SEQRES 8 D 534 PRO ASN ASP GLU ASP CYS LEU THR ILE ASN VAL ILE ARG
SEQRES 9 D 534 PRO PRO GLY THR ARG ALA SER ALA GLY LEU PRO VAL MET
SEQRES 10 D 534 LEU TRP ILE PHE GLY GLY GLY PHE GLU LEU GLY GLY SER
SEQRES 11 D 534 SER LEU PHE PRO GLY ASP GLN MET VAL ALA LYS SER VAL
SEQRES 12 D 534 LEU MET GLY LYS PRO VAL ILE HIS VAL SER MET ASN TYR
SEQRES 13 D 534 ARG VAL ALA SER TRP GLY PHE LEU ALA GLY PRO ASP ILE
SEQRES 14 D 534 GLN ASN GLU GLY SER GLY ASN ALA GLY LEU HIS ASP GLN
SEQRES 15 D 534 ARG LEU ALA MET GLN TRP VAL ALA ASP ASN ILE ALA GLY
SEQRES 16 D 534 PHE GLY GLY ASP PRO SER LYS VAL THR ILE TYR GLY GLU
SEQRES 17 D 534 SER ALA GLY SER MET SER THR PHE VAL HIS LEU VAL TRP
SEQRES 18 D 534 ASN ASP GLY ASP ASN THR TYR ASN GLY LYS PRO LEU PHE
SEQRES 19 D 534 ARG ALA ALA ILE MET GLN SER GLY CYS MET VAL PRO SER
SEQRES 20 D 534 ASP PRO VAL ASP GLY THR TYR GLY THR GLU ILE TYR ASN
SEQRES 21 D 534 GLN VAL VAL ALA SER ALA GLY CYS GLY SER ALA SER ASP
SEQRES 22 D 534 LYS LEU ALA CYS LEU ARG GLY LEU SER GLN ASP THR LEU
SEQRES 23 D 534 TYR GLN ALA THR SER ASP THR PRO GLY VAL LEU ALA TYR
SEQRES 24 D 534 PRO SER LEU ARG LEU SER TYR LEU PRO ARG PRO ASP GLY
SEQRES 25 D 534 THR PHE ILE THR ASP ASP MET TYR ALA LEU VAL ARG ASP
SEQRES 26 D 534 GLY LYS TYR ALA HIS VAL PRO VAL ILE ILE GLY ASP GLN
SEQRES 27 D 534 ASN ASP GLU GLY THR LEU PHE GLY LEU SER SER LEU ASN
SEQRES 28 D 534 VAL THR THR ASP ALA GLN ALA ARG ALA TYR PHE LYS GLN
SEQRES 29 D 534 SER PHE ILE HIS ALA SER ASP ALA GLU ILE ASP THR LEU
SEQRES 30 D 534 MET ALA ALA TYR THR SER ASP ILE THR GLN GLY SER PRO
SEQRES 31 D 534 PHE ASP THR GLY ILE PHE ASN ALA ILE THR PRO GLN PHE
SEQRES 32 D 534 LYS ARG ILE SER ALA LEU LEU GLY ASP LEU ALA PHE THR
SEQRES 33 D 534 LEU ALA ARG ARG TYR PHE LEU ASN TYR TYR GLN GLY GLY
SEQRES 34 D 534 THR LYS TYR SER PHE LEU SER LYS GLN LEU SER GLY LEU
SEQRES 35 D 534 PRO VAL LEU GLY THR PHE HIS GLY ASN ASP ILE ILE TRP
SEQRES 36 D 534 GLN ASP TYR LEU VAL GLY SER GLY SER VAL ILE TYR ASN
SEQRES 37 D 534 ASN ALA PHE ILE ALA PHE ALA ASN ASP LEU ASP PRO ASN
SEQRES 38 D 534 LYS ALA GLY LEU TRP THR ASN TRP PRO THR TYR THR SER
SEQRES 39 D 534 SER SER GLN SER GLY ASN ASN LEU MET GLN ILE ASN GLY
SEQRES 40 D 534 LEU GLY LEU TYR THR GLY LYS ASP ASN PHE ARG PRO ASP
SEQRES 41 D 534 ALA TYR SER ALA LEU PHE SER ASN PRO PRO SER PHE PHE
SEQRES 42 D 534 VAL
HET NAG A1535 14
HET NAG A1536 14
HET GOL A1537 6
HET GOL A1538 6
HET NAG B1535 14
HET NAG B1536 14
HET GOL B1537 6
HET GOL B1538 6
HET NAG C1535 14
HET NAG C1536 14
HET GOL C1537 6
HET GOL C1538 6
HET NAG D1535 14
HET NAG D1536 14
HET GOL D1537 6
HET GOL D1538 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
HETNAM GOL GLYCEROL
HETSYN GOL GLYCEROL
FORMUL 5 NAG 8(C8 H15 N1 O6)
FORMUL 6 GOL 8(C3 H8 O3)
FORMUL 7 HOH *1471(H2 O1)
HELIX 1 1 VAL A 33 ARG A 37 5 5
HELIX 2 2 SER A 68 THR A 72 5 5
HELIX 3 3 PRO A 74 LYS A 85 1 12
HELIX 4 4 GLY A 135 MET A 145 1 11
HELIX 5 5 VAL A 158 LEU A 164 1 7
HELIX 6 6 GLY A 166 GLY A 173 1 8
HELIX 7 7 ASN A 176 ILE A 193 1 18
HELIX 8 8 ALA A 194 PHE A 196 5 3
HELIX 9 9 SER A 209 TRP A 221 1 13
HELIX 10 10 ASN A 222 ASP A 225 5 4
HELIX 11 11 GLY A 252 ALA A 266 1 15
HELIX 12 12 ASP A 273 GLY A 280 1 8
HELIX 13 13 SER A 282 SER A 291 1 10
HELIX 14 14 ASP A 318 ASP A 325 1 8
HELIX 15 15 GLY A 342 LEU A 347 1 6
HELIX 16 16 SER A 348 LEU A 350 5 3
HELIX 17 17 THR A 354 PHE A 366 1 13
HELIX 18 18 SER A 370 TYR A 381 1 12
HELIX 19 19 ASP A 384 GLY A 388 5 5
HELIX 20 20 GLN A 402 PHE A 415 1 14
HELIX 21 21 PHE A 415 TYR A 426 1 12
HELIX 22 22 GLY A 450 TYR A 458 1 9
HELIX 23 23 GLY A 463 ASN A 468 1 6
HELIX 24 24 ASN A 468 LEU A 478 1 11
HELIX 25 25 ASP A 479 GLY A 484 5 6
HELIX 26 26 ARG A 518 SER A 527 1 10
HELIX 27 27 ASN A 528 PHE A 533 5 6
HELIX 28 28 VAL B 33 ARG B 37 5 5
HELIX 29 29 SER B 68 THR B 72 5 5
HELIX 30 30 PRO B 74 LYS B 85 1 12
HELIX 31 31 GLY B 135 MET B 145 1 11
HELIX 32 32 VAL B 158 LEU B 164 1 7
HELIX 33 33 GLY B 166 GLY B 173 1 8
HELIX 34 34 ASN B 176 ILE B 193 1 18
HELIX 35 35 ALA B 194 PHE B 196 5 3
HELIX 36 36 SER B 209 TRP B 221 1 13
HELIX 37 37 ASN B 222 ASP B 225 5 4
HELIX 38 38 GLY B 252 GLY B 267 1 16
HELIX 39 39 ASP B 273 GLY B 280 1 8
HELIX 40 40 SER B 282 ASP B 292 1 11
HELIX 41 41 ASP B 318 ASP B 325 1 8
HELIX 42 42 GLY B 342 LEU B 347 1 6
HELIX 43 43 THR B 354 PHE B 366 1 13
HELIX 44 44 SER B 370 TYR B 381 1 12
HELIX 45 45 ASP B 384 GLY B 388 5 5
HELIX 46 46 GLN B 402 PHE B 415 1 14
HELIX 47 47 PHE B 415 TYR B 426 1 12
HELIX 48 48 ASN B 451 TYR B 458 1 8
HELIX 49 49 GLY B 463 ASN B 468 1 6
HELIX 50 50 ASN B 468 LEU B 478 1 11
HELIX 51 51 ASP B 479 GLY B 484 5 6
HELIX 52 52 ARG B 518 SER B 527 1 10
HELIX 53 53 ASN B 528 PHE B 533 5 6
HELIX 54 54 VAL C 33 ARG C 37 5 5
HELIX 55 55 PRO C 74 SER C 84 1 11
HELIX 56 56 GLY C 135 MET C 145 1 11
HELIX 57 57 VAL C 158 LEU C 164 1 7
HELIX 58 58 GLY C 166 GLY C 173 1 8
HELIX 59 59 ASN C 176 ILE C 193 1 18
HELIX 60 60 ALA C 194 PHE C 196 5 3
HELIX 61 61 SER C 209 TRP C 221 1 13
HELIX 62 62 ASN C 222 ASP C 225 5 4
HELIX 63 63 GLY C 252 GLY C 267 1 16
HELIX 64 64 ASP C 273 GLY C 280 1 8
HELIX 65 65 SER C 282 SER C 291 1 10
HELIX 66 66 ASP C 318 ASP C 325 1 8
HELIX 67 67 GLY C 342 LEU C 347 1 6
HELIX 68 68 SER C 348 LEU C 350 5 3
HELIX 69 69 THR C 354 PHE C 366 1 13
HELIX 70 70 SER C 370 TYR C 381 1 12
HELIX 71 71 GLN C 402 PHE C 415 1 14
HELIX 72 72 PHE C 415 TYR C 426 1 12
HELIX 73 73 ASN C 451 TYR C 458 1 8
HELIX 74 74 GLY C 463 ASN C 468 1 6
HELIX 75 75 ASN C 468 LEU C 478 1 11
HELIX 76 76 ASP C 479 GLY C 484 5 6
HELIX 77 77 ARG C 518 SER C 527 1 10
HELIX 78 78 ASN C 528 PHE C 533 5 6
HELIX 79 79 VAL D 33 ARG D 37 5 5
HELIX 80 80 PRO D 74 LYS D 85 1 12
HELIX 81 81 GLY D 135 MET D 145 1 11
HELIX 82 82 VAL D 158 LEU D 164 1 7
HELIX 83 83 GLY D 166 GLY D 173 1 8
HELIX 84 84 ASN D 176 ILE D 193 1 18
HELIX 85 85 ALA D 194 PHE D 196 5 3
HELIX 86 86 SER D 209 TRP D 221 1 13
HELIX 87 87 ASN D 222 ASP D 225 5 4
HELIX 88 88 GLY D 252 GLY D 267 1 16
HELIX 89 89 ASP D 273 GLY D 280 1 8
HELIX 90 90 SER D 282 ASP D 292 1 11
HELIX 91 91 ASP D 318 ASP D 325 1 8
HELIX 92 92 GLY D 342 LEU D 347 1 6
HELIX 93 93 SER D 348 LEU D 350 5 3
HELIX 94 94 THR D 354 PHE D 366 1 13
HELIX 95 95 SER D 370 TYR D 381 1 12
HELIX 96 96 GLN D 402 PHE D 415 1 14
HELIX 97 97 PHE D 415 TYR D 426 1 12
HELIX 98 98 ASN D 451 TYR D 458 1 8
HELIX 99 99 GLY D 463 ASN D 468 1 6
HELIX 100 100 ASN D 468 LEU D 478 1 11
HELIX 101 101 ASP D 479 GLY D 484 5 6
HELIX 102 102 ARG D 518 SER D 527 1 10
HELIX 103 103 ASN D 528 PHE D 533 5 6
SHEET 1 AA 2 THR A 3 THR A 5 0
SHEET 2 AA 2 THR A 11 THR A 13 -1 O ILE A 12 N ALA A 4
SHEET 1 AB11 LEU A 15 ASN A 16 0
SHEET 2 AB11 GLU A 21 PRO A 27 -1 O LYS A 22 N LEU A 15
SHEET 3 AB11 THR A 99 ARG A 104 -1 O ILE A 100 N ILE A 26
SHEET 4 AB11 ILE A 150 MET A 154 -1 O HIS A 151 N ILE A 103
SHEET 5 AB11 LEU A 114 ILE A 120 1 O PRO A 115 N ILE A 150
SHEET 6 AB11 GLY A 198 GLU A 208 1 N ASP A 199 O LEU A 114
SHEET 7 AB11 ALA A 236 GLN A 240 1 O ALA A 236 N ILE A 205
SHEET 8 AB11 VAL A 333 GLN A 338 1 O ILE A 334 N MET A 239
SHEET 9 AB11 LYS A 431 SER A 436 1 O TYR A 432 N ILE A 335
SHEET 10 AB11 LEU A 502 ILE A 505 1 O MET A 503 N LEU A 435
SHEET 11 AB11 LEU A 510 GLY A 513 -1 O TYR A 511 N GLN A 504
SHEET 1 AC 2 THR A 227 TYR A 228 0
SHEET 2 AC 2 LYS A 231 PRO A 232 -1 O LYS A 231 N TYR A 228
SHEET 1 BA 2 THR B 3 THR B 5 0
SHEET 2 BA 2 THR B 11 THR B 13 -1 O ILE B 12 N ALA B 4
SHEET 1 BB11 LEU B 15 ASN B 16 0
SHEET 2 BB11 GLU B 21 PRO B 27 -1 O LYS B 22 N LEU B 15
SHEET 3 BB11 THR B 99 ARG B 104 -1 O ILE B 100 N ILE B 26
SHEET 4 BB11 ILE B 150 MET B 154 -1 O HIS B 151 N ILE B 103
SHEET 5 BB11 LEU B 114 ILE B 120 1 O PRO B 115 N ILE B 150
SHEET 6 BB11 GLY B 198 GLU B 208 1 N ASP B 199 O LEU B 114
SHEET 7 BB11 ALA B 236 GLN B 240 1 O ALA B 236 N ILE B 205
SHEET 8 BB11 VAL B 333 GLN B 338 1 O ILE B 334 N MET B 239
SHEET 9 BB11 LYS B 431 SER B 436 1 O TYR B 432 N ILE B 335
SHEET 10 BB11 LEU B 502 ILE B 505 1 O MET B 503 N LEU B 435
SHEET 11 BB11 LEU B 510 GLY B 513 -1 O TYR B 511 N GLN B 504
SHEET 1 BC 2 THR B 227 TYR B 228 0
SHEET 2 BC 2 LYS B 231 PRO B 232 -1 O LYS B 231 N TYR B 228
SHEET 1 CA 2 THR C 3 THR C 5 0
SHEET 2 CA 2 THR C 11 THR C 13 -1 O ILE C 12 N ALA C 4
SHEET 1 CB11 LEU C 15 ASN C 16 0
SHEET 2 CB11 GLU C 21 PRO C 27 -1 O LYS C 22 N LEU C 15
SHEET 3 CB11 THR C 99 ARG C 104 -1 O ILE C 100 N ILE C 26
SHEET 4 CB11 ILE C 150 MET C 154 -1 O HIS C 151 N ILE C 103
SHEET 5 CB11 LEU C 114 ILE C 120 1 O PRO C 115 N ILE C 150
SHEET 6 CB11 GLY C 198 GLU C 208 1 N ASP C 199 O LEU C 114
SHEET 7 CB11 ALA C 236 GLN C 240 1 O ALA C 236 N ILE C 205
SHEET 8 CB11 VAL C 333 GLN C 338 1 O ILE C 334 N MET C 239
SHEET 9 CB11 LYS C 431 SER C 436 1 O TYR C 432 N ILE C 335
SHEET 10 CB11 LEU C 502 ILE C 505 1 O MET C 503 N LEU C 435
SHEET 11 CB11 LEU C 510 GLY C 513 -1 O TYR C 511 N GLN C 504
SHEET 1 CC 2 THR C 227 TYR C 228 0
SHEET 2 CC 2 LYS C 231 PRO C 232 -1 O LYS C 231 N TYR C 228
SHEET 1 DA 2 THR D 3 THR D 5 0
SHEET 2 DA 2 THR D 11 THR D 13 -1 O ILE D 12 N ALA D 4
SHEET 1 DB11 LEU D 15 ASN D 16 0
SHEET 2 DB11 GLU D 21 PRO D 27 -1 O LYS D 22 N LEU D 15
SHEET 3 DB11 THR D 99 ARG D 104 -1 O ILE D 100 N ILE D 26
SHEET 4 DB11 ILE D 150 MET D 154 -1 O HIS D 151 N ILE D 103
SHEET 5 DB11 LEU D 114 ILE D 120 1 O PRO D 115 N ILE D 150
SHEET 6 DB11 GLY D 198 GLU D 208 1 N ASP D 199 O LEU D 114
SHEET 7 DB11 ALA D 236 GLN D 240 1 O ALA D 236 N ILE D 205
SHEET 8 DB11 VAL D 333 GLN D 338 1 O ILE D 334 N MET D 239
SHEET 9 DB11 LYS D 431 SER D 436 1 O TYR D 432 N ILE D 335
SHEET 10 DB11 LEU D 502 ILE D 505 1 O MET D 503 N LEU D 435
SHEET 11 DB11 LEU D 510 GLY D 513 -1 O TYR D 511 N GLN D 504
SHEET 1 DC 2 THR D 227 TYR D 228 0
SHEET 2 DC 2 LYS D 231 PRO D 232 -1 O LYS D 231 N TYR D 228
SSBOND 1 CYS A 60 CYS A 97 1555 1555
SSBOND 2 CYS A 268 CYS A 277 1555 1555
SSBOND 3 CYS B 60 CYS B 97 1555 1555
SSBOND 4 CYS B 268 CYS B 277 1555 1555
SSBOND 5 CYS C 60 CYS C 97 1555 1555
SSBOND 6 CYS C 268 CYS C 277 1555 1555
SSBOND 7 CYS D 60 CYS D 97 1555 1555
SSBOND 8 CYS D 268 CYS D 277 1555 1555
LINK ND2 ASN A 351 C1 NAG A1535 1555 1555
LINK O4 NAG A1535 C1 NAG A1536 1555 1555
LINK ND2 ASN B 351 C1 NAG B1535 1555 1555
LINK O4 NAG B1535 C1 NAG B1536 1555 1555
LINK ND2 ASN C 351 C1 NAG C1535 1555 1555
LINK O4 NAG C1535 C1 NAG C1536 1555 1555
LINK OG SER D 272 O7 NAG A1535 1455 1555
LINK ND2 ASN D 351 C1 NAG D1535 1555 1555
LINK O4 NAG D1535 C1 NAG D1536 1555 1555
CISPEP 1 LEU A 91 PRO A 92 0 0.05
CISPEP 2 SER A 389 PRO A 390 0 0.28
CISPEP 3 LEU B 91 PRO B 92 0 -0.03
CISPEP 4 SER B 389 PRO B 390 0 0.25
CISPEP 5 LEU C 91 PRO C 92 0 0.08
CISPEP 6 SER C 389 PRO C 390 0 0.10
CISPEP 7 LEU D 91 PRO D 92 0 -0.02
CISPEP 8 SER D 389 PRO D 390 0 0.13
SITE 1 AC1 4 TYR A 299 ASN A 351 SER D 272 HOH Z 458
SITE 1 AC2 4 TYR A 299 HOH Z 458 HOH Z 459 HOH Z 460
SITE 1 AC3 5 SER A 111 ALA A 112 TYR B 299 ASN B 351
SITE 2 AC3 5 HOH Y 352
SITE 1 AC5 3 TYR C 299 ASN C 351 HOH X 225
SITE 1 AC6 1 TYR C 299
SITE 1 AC7 4 TYR D 299 ASN D 351 GLN D 357 HOH W 344
SITE 1 AC8 2 TYR D 299 HOH W 344
SITE 1 AC9 7 ASN A 226 PRO A 232 PHE A 234 ALA A 329
SITE 2 AC9 7 HIS A 330 HOH Z 461 HOH Z 462
SITE 1 BC1 5 ASN B 226 PRO B 232 PHE B 234 ALA B 329
SITE 2 BC1 5 HIS B 330
SITE 1 BC2 6 ASN C 226 PRO C 232 PHE C 234 HIS C 330
SITE 2 BC2 6 HOH X 311 HOH X 312
SITE 1 BC3 6 ASN D 226 PRO D 232 PHE D 234 HIS D 330
SITE 2 BC3 6 HOH W 150 HOH W 345
SITE 1 BC4 5 PRO A 41 HIS A 180 ARG A 183 LEU A 184
SITE 2 BC4 5 GLN A 187
SITE 1 BC5 4 HIS B 180 ARG B 183 GLN B 187 TRP B 221
SITE 1 BC6 5 HIS C 180 ARG C 183 GLN C 187 TRP C 221
SITE 2 BC6 5 HOH X 117
SITE 1 BC7 5 HIS D 180 ARG D 183 GLN D 187 TRP D 221
SITE 2 BC7 5 PHE D 314
CRYST1 61.150 91.140 108.460 90.78 106.31 86.91 P 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 0.016353 -0.000883 0.004786 0.00000
SCALE2 0.000000 0.010988 -0.000017 0.00000
SCALE3 0.000000 0.000000 0.009607 0.00000
TER 4054 VAL A 534
TER 8108 VAL B 534
TER 12162 VAL C 534
TER 16216 VAL D 534
MASTER 441 0 16 103 60 0 23 617843 4 181 168
END |