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HEADER HYDROLASE 12-MAR-99 1HLG
TITLE CRYSTAL STRUCTURE OF HUMAN GASTRIC LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE, GASTRIC;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGAN: STOMAC;
SOURCE 5 CELL: CHIEF CELL;
SOURCE 6 EXPRESSION_SYSTEM: INSECT CELL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROUSSEL,S.CANAAN,R.VERGER,C.CAMBILLAU
REVDAT 1 15-MAR-00 1HLG 0
JRNL AUTH A.ROUSSEL,S.CANAAN,M.P.EGLOFF,M.RIVIERE,L.DUPUIS,
JRNL AUTH 2 R.VERGER,C.CAMBILLAU
JRNL TITL CRYSTAL STRUCTURE OF HUMAN GASTRIC LIPASE AND
JRNL TITL 2 MODEL OF LYSOSOMAL ACID LIPASE, TWO LIPOLYTIC
JRNL TITL 3 ENZYMES OF MEDICAL INTEREST
JRNL REF J.BIOL.CHEM. V. 274 16995 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
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) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 47643
REMARK 3
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) : 0.210
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2381
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7293
REMARK 3 BIN R VALUE (WORKING SET) : 0.3190
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 389
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5960
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 140
REMARK 3 SOLVENT ATOMS : 92
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.510
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
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
REMARK 3 NCS MODEL : RESTRAINTS
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 3 : PARAM3.CHO
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 3 : TOPH3.CHO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HLG COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000645.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : W32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.963
REMARK 200 MONOCHROMATOR : LURE
REMARK 200 OPTICS : LURE
REMARK 200
REMARK 200 DETECTOR TYPE : MAR 345
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45522
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: CCP4 PACKAGE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 1/2+Z,1/2-X,-Y
REMARK 290 7555 1/2-Z,-X,1/2+Y
REMARK 290 8555 -Z,1/2+X,1/2-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,1/2+Z,1/2-X
REMARK 290 11555 1/2+Y,1/2-Z,-X
REMARK 290 12555 1/2-Y,-Z,1/2+X
REMARK 290 13555 1/2+X,1/2+Y,1/2+Z
REMARK 290 14555 -X,1/2-Y,Z
REMARK 290 15555 1/2-X,Y,-Z
REMARK 290 16555 X,-Y,1/2-Z
REMARK 290 17555 1/2+Z,1/2+X,1/2+Y
REMARK 290 18555 Z,-X,1/2-Y
REMARK 290 19555 -Z,1/2-X,Y
REMARK 290 20555 1/2-Z,X,-Y
REMARK 290 21555 1/2+Y,1/2+Z,1/2+X
REMARK 290 22555 1/2-Y,Z,-X
REMARK 290 23555 Y,-Z,1/2-X
REMARK 290 24555 -Y,1/2-Z,X
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 122.16500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 122.16500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 122.16500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 122.16500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 122.16500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 122.16500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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, B, C, 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 ASN A 54
REMARK 465 THR A 55
REMARK 465 GLY A 56
REMARK 465 ASN B 54
REMARK 465 THR B 55
REMARK 465 GLY B 56
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
REMARK 500 O HOH 46 O HOH 146 2.17
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN A 51 OD1 ASN A 51 CG 0.128
REMARK 500 ASN A 51 ND2 ASN A 51 CG 0.107
REMARK 500 SER A 52 OG SER A 52 CB 0.112
REMARK 500 ARG A 229 NH1 ARG A 229 CZ 0.113
REMARK 500 MET A 297 CE MET A 297 SD 0.128
REMARK 500 MET A 360 CE MET A 360 SD 0.146
REMARK 500 LYS B 50 CG LYS B 50 CB 0.188
REMARK 500 LYS B 50 CD LYS B 50 CG 0.228
REMARK 500 LYS B 50 CE LYS B 50 CD 0.180
REMARK 500 LYS B 50 NZ LYS B 50 CE 0.180
REMARK 500 LYS B 50 O LYS B 50 C 0.147
REMARK 500 ASN B 51 CG ASN B 51 CB 0.176
REMARK 500 ASN B 51 OD1 ASN B 51 CG 0.128
REMARK 500 MET B 231 SD MET B 231 CG 0.158
REMARK 500 MET B 231 CE MET B 231 SD 0.154
REMARK 500 ASP B 377 OD1 ASP B 377 CG 0.165
REMARK 500 ASP B 377 OD2 ASP B 377 CG 0.161
REMARK 500 LYS B 378 CG LYS B 378 CB 0.118
REMARK 500 LYS B 378 CD LYS B 378 CG 0.141
REMARK 500 LYS B 378 O LYS B 378 C 0.140
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 GLY A 37 N - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 LYS A 50 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 SER A 76 N - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 TYR A 110 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 209 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 ASN A 252 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 GLN A 301 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 GLY B 37 N - CA - C ANGL. DEV. = 12.5 DEGREES
REMARK 500 LYS B 49 CD - CE - NZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 LYS B 50 CD - CE - NZ ANGL. DEV. = 11.2 DEGREES
REMARK 500 LYS B 50 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 SER B 76 N - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP B 209 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ASN B 252 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 GLN B 301 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: SA
REMARK 800 SITE_DESCRIPTION:
REMARK 800 ACTIVE SITE CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: SB
REMARK 800 SITE_DESCRIPTION:
REMARK 800 ACTIVE SITE CHAIN B
REMARK 800
DBREF 1HLG A 9 379 SWS P07098 LIPG_HUMAN 28 398
DBREF 1HLG B 9 379 SWS P07098 LIPG_HUMAN 28 398
SEQRES 1 A 371 SER PRO GLU VAL THR MET ASN ILE SER GLN MET ILE THR
SEQRES 2 A 371 TYR TRP GLY TYR PRO ASN GLU GLU TYR GLU VAL VAL THR
SEQRES 3 A 371 GLU ASP GLY TYR ILE LEU GLU VAL ASN ARG ILE PRO TYR
SEQRES 4 A 371 GLY LYS LYS ASN SER GLY ASN THR GLY GLN ARG PRO VAL
SEQRES 5 A 371 VAL PHE LEU GLN HIS GLY LEU LEU ALA SER ALA THR ASN
SEQRES 6 A 371 TRP ILE SER ASN LEU PRO ASN ASN SER LEU ALA PHE ILE
SEQRES 7 A 371 LEU ALA ASP ALA GLY TYR ASP VAL TRP LEU GLY ASN SER
SEQRES 8 A 371 ARG GLY ASN THR TRP ALA ARG ARG ASN LEU TYR TYR SER
SEQRES 9 A 371 PRO ASP SER VAL GLU PHE TRP ALA PHE SER PHE ASP GLU
SEQRES 10 A 371 MET ALA LYS TYR ASP LEU PRO ALA THR ILE ASP PHE ILE
SEQRES 11 A 371 VAL LYS LYS THR GLY GLN LYS GLN LEU HIS TYR VAL GLY
SEQRES 12 A 371 HIS SER GLN GLY THR THR ILE GLY PHE ILE ALA PHE SER
SEQRES 13 A 371 THR ASN PRO SER LEU ALA LYS ARG ILE LYS THR PHE TYR
SEQRES 14 A 371 ALA LEU ALA PRO VAL ALA THR VAL LYS TYR THR LYS SER
SEQRES 15 A 371 LEU ILE ASN LYS LEU ARG PHE VAL PRO GLN SER LEU PHE
SEQRES 16 A 371 LYS PHE ILE PHE GLY ASP LYS ILE PHE TYR PRO HIS ASN
SEQRES 17 A 371 PHE PHE ASP GLN PHE LEU ALA THR GLU VAL CYS SER ARG
SEQRES 18 A 371 GLU MET LEU ASN LEU LEU CYS SER ASN ALA LEU PHE ILE
SEQRES 19 A 371 ILE CYS GLY PHE ASP SER LYS ASN PHE ASN THR SER ARG
SEQRES 20 A 371 LEU ASP VAL TYR LEU SER HIS ASN PRO ALA GLY THR SER
SEQRES 21 A 371 VAL GLN ASN MET PHE HIS TRP THR GLN ALA VAL LYS SER
SEQRES 22 A 371 GLY LYS PHE GLN ALA TYR ASP TRP GLY SER PRO VAL GLN
SEQRES 23 A 371 ASN ARG MET HIS TYR ASP GLN SER GLN PRO PRO TYR TYR
SEQRES 24 A 371 ASN VAL THR ALA MET ASN VAL PRO ILE ALA VAL TRP ASN
SEQRES 25 A 371 GLY GLY LYS ASP LEU LEU ALA ASP PRO GLN ASP VAL GLY
SEQRES 26 A 371 LEU LEU LEU PRO LYS LEU PRO ASN LEU ILE TYR HIS LYS
SEQRES 27 A 371 GLU ILE PRO PHE TYR ASN HIS LEU ASP PHE ILE TRP ALA
SEQRES 28 A 371 MET ASP ALA PRO GLN GLU VAL TYR ASN ASP ILE VAL SER
SEQRES 29 A 371 MET ILE SER GLU ASP LYS LYS
SEQRES 1 B 371 SER PRO GLU VAL THR MET ASN ILE SER GLN MET ILE THR
SEQRES 2 B 371 TYR TRP GLY TYR PRO ASN GLU GLU TYR GLU VAL VAL THR
SEQRES 3 B 371 GLU ASP GLY TYR ILE LEU GLU VAL ASN ARG ILE PRO TYR
SEQRES 4 B 371 GLY LYS LYS ASN SER GLY ASN THR GLY GLN ARG PRO VAL
SEQRES 5 B 371 VAL PHE LEU GLN HIS GLY LEU LEU ALA SER ALA THR ASN
SEQRES 6 B 371 TRP ILE SER ASN LEU PRO ASN ASN SER LEU ALA PHE ILE
SEQRES 7 B 371 LEU ALA ASP ALA GLY TYR ASP VAL TRP LEU GLY ASN SER
SEQRES 8 B 371 ARG GLY ASN THR TRP ALA ARG ARG ASN LEU TYR TYR SER
SEQRES 9 B 371 PRO ASP SER VAL GLU PHE TRP ALA PHE SER PHE ASP GLU
SEQRES 10 B 371 MET ALA LYS TYR ASP LEU PRO ALA THR ILE ASP PHE ILE
SEQRES 11 B 371 VAL LYS LYS THR GLY GLN LYS GLN LEU HIS TYR VAL GLY
SEQRES 12 B 371 HIS SER GLN GLY THR THR ILE GLY PHE ILE ALA PHE SER
SEQRES 13 B 371 THR ASN PRO SER LEU ALA LYS ARG ILE LYS THR PHE TYR
SEQRES 14 B 371 ALA LEU ALA PRO VAL ALA THR VAL LYS TYR THR LYS SER
SEQRES 15 B 371 LEU ILE ASN LYS LEU ARG PHE VAL PRO GLN SER LEU PHE
SEQRES 16 B 371 LYS PHE ILE PHE GLY ASP LYS ILE PHE TYR PRO HIS ASN
SEQRES 17 B 371 PHE PHE ASP GLN PHE LEU ALA THR GLU VAL CYS SER ARG
SEQRES 18 B 371 GLU MET LEU ASN LEU LEU CYS SER ASN ALA LEU PHE ILE
SEQRES 19 B 371 ILE CYS GLY PHE ASP SER LYS ASN PHE ASN THR SER ARG
SEQRES 20 B 371 LEU ASP VAL TYR LEU SER HIS ASN PRO ALA GLY THR SER
SEQRES 21 B 371 VAL GLN ASN MET PHE HIS TRP THR GLN ALA VAL LYS SER
SEQRES 22 B 371 GLY LYS PHE GLN ALA TYR ASP TRP GLY SER PRO VAL GLN
SEQRES 23 B 371 ASN ARG MET HIS TYR ASP GLN SER GLN PRO PRO TYR TYR
SEQRES 24 B 371 ASN VAL THR ALA MET ASN VAL PRO ILE ALA VAL TRP ASN
SEQRES 25 B 371 GLY GLY LYS ASP LEU LEU ALA ASP PRO GLN ASP VAL GLY
SEQRES 26 B 371 LEU LEU LEU PRO LYS LEU PRO ASN LEU ILE TYR HIS LYS
SEQRES 27 B 371 GLU ILE PRO PHE TYR ASN HIS LEU ASP PHE ILE TRP ALA
SEQRES 28 B 371 MET ASP ALA PRO GLN GLU VAL TYR ASN ASP ILE VAL SER
SEQRES 29 B 371 MET ILE SER GLU ASP LYS LYS
MODRES 1HLG ASN A 15 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN A 80 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN A 252 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN A 308 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN B 15 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN B 80 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN B 252 ASN GLYCOSYLATION SITE
MODRES 1HLG ASN B 308 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG C 3 14
HET NAG C 4 14
HET NAG C 5 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG D 3 14
HET NAG D 4 14
HET NAG D 5 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 10(C8 H15 N1 O6)
FORMUL 11 HOH *92(H2 O1)
HELIX 1 1 SER A 9 MET A 14 5 6
HELIX 2 2 ASN A 15 TRP A 23 1 9
HELIX 3 3 SER A 70 SER A 76 5 7
HELIX 4 4 SER A 82 ALA A 90 1 9
HELIX 5 5 VAL A 116 ALA A 120 5 5
HELIX 6 6 SER A 122 TYR A 129 1 8
HELIX 7 7 TYR A 129 GLY A 143 1 15
HELIX 8 8 SER A 153 ASN A 166 1 14
HELIX 9 9 ASN A 166 LYS A 171 1 6
HELIX 10 10 SER A 190 VAL A 198 5 9
HELIX 11 11 PRO A 199 GLY A 208 1 10
HELIX 12 12 PHE A 221 MET A 231 1 11
HELIX 13 13 LEU A 232 SER A 237 1 6
HELIX 14 14 ASN A 238 GLY A 245 1 8
HELIX 15 15 ASN A 252 SER A 254 5 3
HELIX 16 16 ARG A 255 SER A 261 1 7
HELIX 17 17 SER A 268 GLY A 282 1 15
HELIX 18 18 SER A 291 ASP A 300 1 10
HELIX 19 19 ASN A 308 MET A 312 5 5
HELIX 20 20 ASP A 328 LEU A 339 1 12
HELIX 21 21 LEU A 354 ALA A 359 1 6
HELIX 22 22 ASP A 361 VAL A 366 1 6
HELIX 23 23 VAL A 366 SER A 375 1 10
HELIX 24 24 SER B 9 MET B 14 5 6
HELIX 25 25 ASN B 15 TRP B 23 1 9
HELIX 26 26 SER B 70 SER B 76 5 7
HELIX 27 27 SER B 82 ALA B 90 1 9
HELIX 28 28 VAL B 116 ALA B 120 5 5
HELIX 29 29 SER B 122 TYR B 129 1 8
HELIX 30 30 TYR B 129 GLY B 143 1 15
HELIX 31 31 SER B 153 SER B 164 1 12
HELIX 32 32 ASN B 166 LYS B 171 1 6
HELIX 33 33 SER B 190 VAL B 198 5 9
HELIX 34 34 PRO B 199 GLY B 208 1 10
HELIX 35 35 PHE B 221 MET B 231 1 11
HELIX 36 36 LEU B 232 SER B 237 1 6
HELIX 37 37 ASN B 238 GLY B 245 1 8
HELIX 38 38 ASN B 252 SER B 254 5 3
HELIX 39 39 ARG B 255 SER B 261 1 7
HELIX 40 40 SER B 268 GLY B 282 1 15
HELIX 41 41 SER B 291 ASP B 300 1 10
HELIX 42 42 ASN B 308 MET B 312 5 5
HELIX 43 43 ASP B 328 LEU B 339 1 12
HELIX 44 44 LEU B 354 ALA B 359 1 6
HELIX 45 45 ASP B 361 VAL B 366 1 6
HELIX 46 46 VAL B 366 SER B 375 1 10
SHEET 1 A 8 GLU A 28 VAL A 33 0
SHEET 2 A 8 ILE A 39 ILE A 45 -1 N LEU A 40 O VAL A 32
SHEET 3 A 8 ASP A 93 LEU A 96 -1 O VAL A 94 N ILE A 45
SHEET 4 A 8 VAL A 60 GLN A 64 1 O VAL A 61 N TRP A 95
SHEET 5 A 8 LEU A 147 HIS A 152 1 N HIS A 148 O VAL A 60
SHEET 6 A 8 ILE A 173 LEU A 179 1 N LYS A 174 O LEU A 147
SHEET 7 A 8 ILE A 316 GLY A 321 1 O ALA A 317 N ALA A 178
SHEET 8 A 8 LEU A 342 ILE A 348 1 N ILE A 343 O ILE A 316
SHEET 1 B 8 GLU B 28 VAL B 33 0
SHEET 2 B 8 TYR B 38 ILE B 45 -1 N LEU B 40 O VAL B 32
SHEET 3 B 8 ASP B 93 LEU B 96 -1 O VAL B 94 N ILE B 45
SHEET 4 B 8 VAL B 60 GLN B 64 1 N VAL B 61 O ASP B 93
SHEET 5 B 8 LEU B 147 HIS B 152 1 N HIS B 148 O VAL B 60
SHEET 6 B 8 ILE B 173 LEU B 179 1 N LYS B 174 O LEU B 147
SHEET 7 B 8 ILE B 316 GLY B 321 1 O ALA B 317 N ALA B 178
SHEET 8 B 8 LEU B 342 ILE B 348 1 N ILE B 343 O ILE B 316
SHEET 1 C 3 GLU B 28 VAL B 33 0
SHEET 2 C 3 TYR B 38 ILE B 45 -1 N LEU B 40 O VAL B 32
SHEET 3 C 3 ARG B 107 ASN B 108 -1 O ARG B 107 N ILE B 39
SSBOND 1 CYS A 227 CYS A 236
SSBOND 2 CYS B 227 CYS B 236
LINK O4 NAG C 3 C1 NAG C 4
LINK O4 NAG D 3 C1 NAG D 4
LINK ND2 ASN A 15 C1 NAG C 1
LINK ND2 ASN A 80 C1 NAG C 2
LINK ND2 ASN A 252 C1 NAG C 3
LINK ND2 ASN A 308 C1 NAG C 5
LINK ND2 ASN B 15 C1 NAG D 1
LINK ND2 ASN B 80 C1 NAG D 2
LINK ND2 ASN B 252 C1 NAG D 3
LINK ND2 ASN B 308 C1 NAG D 5
CISPEP 1 ASN A 263 PRO A 264 0 -0.34
CISPEP 2 ASN B 263 PRO B 264 0 -0.36
SITE 1 SA 3 SER A 153 ASP A 324 HIS A 353
SITE 2 SB 3 SER B 153 ASP B 324 HIS B 353
CRYST1 244.330 244.330 244.330 90.00 90.00 90.00 I 21 3 48
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 0.004093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004093 0.00000
END |