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HEADER HYDROLASE 12-JUN-10 3NGM
TITLE CRYSTAL STRUCTURE OF LIPASE FROM GIBBERELLA ZEAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXTRACELLULAR LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 1-319;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GIBBERELLA ZEAE;
SOURCE 3 ORGANISM_TAXID: 5518;
SOURCE 4 GENE: FGL1;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KM71;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLIZG7
KEYWDS SECRET LIPASE, GIBBERELLA ZEAE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.Y.LOU,M.LI,Y.N.SUN,Y.LIU,Z.LIU,Z.H.RAO
REVDAT 1 25-MAY-11 3NGM 0
JRNL AUTH Z.Y.LOU,M.LI,Y.N.SUN,Y.LIU,Z.LIU,W.P.WU,Z.H.RAO
JRNL TITL CRYSTAL STRUCTURE OF A SECRETED LIPASE FROM GIBBERELLA ZEAE
JRNL TITL 2 REVEALS A NOVEL "DOUBLE-LOCK" MECHANISM
JRNL REF PROTEIN CELL V. 1 760 2010
JRNL REFN ISSN 1674-800X
JRNL PMID 21203917
JRNL DOI 10.1007/S13238-010-0094-Y
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 29217
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) : 0.238
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2906
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 : 8792
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 218
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 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) : 1.097
REMARK 3 BOND ANGLES (DEGREES) : 0.01
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 : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NGM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB059803.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1EIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 39.20850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.90100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.50050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.90100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.20850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.50050
REMARK 290 SMTRY3 4 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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 ALA A 269
REMARK 465 GLY A 270
REMARK 465 GLY A 271
REMARK 465 ILE A 272
REMARK 465 SER A 273
REMARK 465 TRP A 274
REMARK 465 ARG A 275
REMARK 465 ARG A 276
REMARK 465 TYR A 277
REMARK 465 ARG A 278
REMARK 465 SER A 279
REMARK 465 ALA A 280
REMARK 465 LYS A 281
REMARK 465 ARG A 282
REMARK 465 GLU A 283
REMARK 465 SER A 284
REMARK 465 ILE A 285
REMARK 465 SER A 286
REMARK 465 GLU A 287
REMARK 465 ARG A 288
REMARK 465 ALA A 289
REMARK 465 SER A 319
REMARK 465 ALA B 269
REMARK 465 GLY B 270
REMARK 465 GLY B 271
REMARK 465 ILE B 272
REMARK 465 SER B 273
REMARK 465 TRP B 274
REMARK 465 ARG B 275
REMARK 465 ARG B 276
REMARK 465 TYR B 277
REMARK 465 ARG B 278
REMARK 465 SER B 279
REMARK 465 ALA B 280
REMARK 465 LYS B 281
REMARK 465 ARG B 282
REMARK 465 GLU B 283
REMARK 465 SER B 284
REMARK 465 ILE B 285
REMARK 465 SER B 286
REMARK 465 GLU B 287
REMARK 465 ARG B 288
REMARK 465 ALA B 289
REMARK 465 SER B 319
REMARK 465 ALA C 269
REMARK 465 GLY C 270
REMARK 465 GLY C 271
REMARK 465 ILE C 272
REMARK 465 SER C 273
REMARK 465 TRP C 274
REMARK 465 ARG C 275
REMARK 465 ARG C 276
REMARK 465 TYR C 277
REMARK 465 ARG C 278
REMARK 465 SER C 279
REMARK 465 ALA C 280
REMARK 465 LYS C 281
REMARK 465 ARG C 282
REMARK 465 GLU C 283
REMARK 465 SER C 284
REMARK 465 ILE C 285
REMARK 465 SER C 286
REMARK 465 GLU C 287
REMARK 465 ARG C 288
REMARK 465 ALA C 289
REMARK 465 SER C 319
REMARK 465 ALA D 269
REMARK 465 GLY D 270
REMARK 465 GLY D 271
REMARK 465 ILE D 272
REMARK 465 SER D 273
REMARK 465 TRP D 274
REMARK 465 ARG D 275
REMARK 465 ARG D 276
REMARK 465 TYR D 277
REMARK 465 ARG D 278
REMARK 465 SER D 279
REMARK 465 ALA D 280
REMARK 465 LYS D 281
REMARK 465 ARG D 282
REMARK 465 GLU D 283
REMARK 465 SER D 284
REMARK 465 ILE D 285
REMARK 465 SER D 286
REMARK 465 GLU D 287
REMARK 465 ARG D 288
REMARK 465 ALA D 289
REMARK 465 SER D 319
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 NH2 ARG B 202 O HOH B 350 2.00
REMARK 500 N THR A 292 O HOH A 327 2.02
REMARK 500 O LYS C 59 O HOH C 356 2.03
REMARK 500 CB CYS B 237 O HOH B 321 2.06
REMARK 500 N ILE B 83 O HOH B 358 2.06
REMARK 500 N ASN B 242 O HOH B 332 2.06
REMARK 500 OG SER B 119 O HOH B 345 2.07
REMARK 500 CB SER B 26 O HOH B 320 2.07
REMARK 500 N ARG C 86 O HOH C 352 2.08
REMARK 500 O CYS B 36 O HOH B 334 2.09
REMARK 500 OD1 ASN A 133 O HOH A 344 2.11
REMARK 500 OE1 GLU C 74 O HOH C 340 2.12
REMARK 500 O GLN C 244 O HOH C 328 2.12
REMARK 500 N VAL D 174 O HOH D 335 2.14
REMARK 500 O GLY D 223 O HOH D 323 2.14
REMARK 500 O HOH C 322 O HOH C 358 2.14
REMARK 500 OG1 THR B 162 O HOH B 357 2.15
REMARK 500 OD2 ASP C 98 O HOH C 323 2.16
REMARK 500 NE2 GLN D 45 O HOH D 344 2.16
REMARK 500 N CYS B 41 O HOH B 344 2.17
REMARK 500 CB ASN B 242 O HOH B 332 2.17
REMARK 500 CA THR C 102 O HOH C 332 2.17
REMARK 500 OG SER B 316 O HOH B 333 2.18
REMARK 500 O HOH B 354 O HOH C 334 2.18
REMARK 500 SG CYS D 245 O HOH D 354 2.18
REMARK 500 O ALA C 22 OG SER C 26 2.18
REMARK 500 CB CYS C 237 O HOH C 336 2.18
REMARK 500 N ALA A 263 O HOH A 352 2.18
REMARK 500 O VAL C 193 O HOH C 360 2.19
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 GLY B 223 C GLY B 223 O -0.097
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 GLY A 224 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 CYS A 267 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 CYS A 267 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 SER A 268 C - N - CA ANGL. DEV. = 15.7 DEGREES
REMARK 500 GLY B 223 CA - C - O ANGL. DEV. = -28.1 DEGREES
REMARK 500 SER B 268 CA - CB - OG ANGL. DEV. = -22.6 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 CYS A 24 -4.33 -169.32
REMARK 500 GLU A 27 -17.17 -140.80
REMARK 500 ALA A 30 160.16 -49.21
REMARK 500 CYS A 41 48.65 -156.02
REMARK 500 ALA A 53 152.15 179.14
REMARK 500 SER A 109 -76.62 -38.80
REMARK 500 ASN A 133 63.25 -151.13
REMARK 500 PRO A 134 -7.32 -52.03
REMARK 500 SER A 144 -149.45 67.24
REMARK 500 LEU A 164 -155.38 -127.55
REMARK 500 ASP A 165 104.24 175.12
REMARK 500 ALA A 196 -116.67 37.69
REMARK 500 ILE A 207 -9.94 -57.52
REMARK 500 ASP A 228 44.59 -85.69
REMARK 500 ALA A 241 69.36 -107.27
REMARK 500 CYS A 245 -118.40 -136.48
REMARK 500 ASP A 253 48.54 -73.93
REMARK 500 PHE A 261 -13.19 72.53
REMARK 500 GLN A 262 -174.90 -172.19
REMARK 500 THR A 292 -172.91 -61.25
REMARK 500 ARG A 317 -165.15 -100.19
REMARK 500 GLU B 27 7.35 -158.67
REMARK 500 ALA B 30 137.07 -36.82
REMARK 500 ALA B 32 177.31 -53.60
REMARK 500 ASN B 39 19.59 55.69
REMARK 500 ALA B 49 75.09 -69.25
REMARK 500 ALA B 53 146.23 -178.20
REMARK 500 ASN B 84 84.92 97.63
REMARK 500 ASP B 97 -162.72 -108.38
REMARK 500 SER B 100 45.53 -142.58
REMARK 500 ASN B 133 55.49 -161.12
REMARK 500 PRO B 134 29.83 -56.78
REMARK 500 SER B 135 -31.83 -139.86
REMARK 500 SER B 144 -141.09 37.46
REMARK 500 ALA B 187 136.99 -39.08
REMARK 500 ALA B 196 -116.83 40.16
REMARK 500 ILE B 227 -135.54 -129.98
REMARK 500 ASP B 228 18.25 33.03
REMARK 500 ILE B 231 -39.42 -26.80
REMARK 500 CYS B 245 -104.48 -123.83
REMARK 500 ASN B 246 -81.46 -69.76
REMARK 500 LEU B 258 31.85 -77.27
REMARK 500 PHE B 261 -47.88 69.95
REMARK 500 ASP B 265 33.72 -82.36
REMARK 500 LYS B 312 -18.83 -45.50
REMARK 500 ARG B 317 -118.70 -110.00
REMARK 500 CYS C 41 67.88 -168.33
REMARK 500 ALA C 49 104.16 -34.46
REMARK 500 SER C 100 46.78 -150.62
REMARK 500 SER C 144 -155.39 52.10
REMARK 500
REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 267 SER A 268 96.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY B 223 30.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 CYS A 267 20.7 L L OUTSIDE RANGE
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 C 344 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH C 365 DISTANCE = 6.58 ANGSTROMS
DBREF 3NGM A 1 319 UNP Q6WER3 Q6WER3_GIBZE 31 349
DBREF 3NGM B 1 319 UNP Q6WER3 Q6WER3_GIBZE 31 349
DBREF 3NGM C 1 319 UNP Q6WER3 Q6WER3_GIBZE 31 349
DBREF 3NGM D 1 319 UNP Q6WER3 Q6WER3_GIBZE 31 349
SEQADV 3NGM ILE A 159 UNP Q6WER3 VAL 189 CONFLICT
SEQADV 3NGM SER A 316 UNP Q6WER3 ARG 346 CONFLICT
SEQADV 3NGM ARG A 317 UNP Q6WER3 PRO 347 CONFLICT
SEQADV 3NGM SER A 318 UNP Q6WER3 LEU 348 CONFLICT
SEQADV 3NGM SER A 319 UNP Q6WER3 ILE 349 CONFLICT
SEQADV 3NGM ILE B 159 UNP Q6WER3 VAL 189 CONFLICT
SEQADV 3NGM SER B 316 UNP Q6WER3 ARG 346 CONFLICT
SEQADV 3NGM ARG B 317 UNP Q6WER3 PRO 347 CONFLICT
SEQADV 3NGM SER B 318 UNP Q6WER3 LEU 348 CONFLICT
SEQADV 3NGM SER B 319 UNP Q6WER3 ILE 349 CONFLICT
SEQADV 3NGM ILE C 159 UNP Q6WER3 VAL 189 CONFLICT
SEQADV 3NGM SER C 316 UNP Q6WER3 ARG 346 CONFLICT
SEQADV 3NGM ARG C 317 UNP Q6WER3 PRO 347 CONFLICT
SEQADV 3NGM SER C 318 UNP Q6WER3 LEU 348 CONFLICT
SEQADV 3NGM SER C 319 UNP Q6WER3 ILE 349 CONFLICT
SEQADV 3NGM ILE D 159 UNP Q6WER3 VAL 189 CONFLICT
SEQADV 3NGM SER D 316 UNP Q6WER3 ARG 346 CONFLICT
SEQADV 3NGM ARG D 317 UNP Q6WER3 PRO 347 CONFLICT
SEQADV 3NGM SER D 318 UNP Q6WER3 LEU 348 CONFLICT
SEQADV 3NGM SER D 319 UNP Q6WER3 ILE 349 CONFLICT
SEQRES 1 A 319 ALA VAL SER VAL SER THR THR ASP PHE GLY ASN PHE LYS
SEQRES 2 A 319 PHE TYR ILE GLN HIS GLY ALA ALA ALA TYR CYS ASN SER
SEQRES 3 A 319 GLU ALA PRO ALA GLY ALA LYS VAL THR CYS SER GLY ASN
SEQRES 4 A 319 GLY CYS PRO THR VAL GLN SER ASN GLY ALA THR ILE VAL
SEQRES 5 A 319 ALA SER PHE THR GLY SER LYS THR GLY ILE GLY GLY TYR
SEQRES 6 A 319 VAL ALA THR ASP PRO THR ARG LYS GLU ILE VAL VAL SER
SEQRES 7 A 319 PHE ARG GLY SER ILE ASN ILE ARG ASN TRP LEU THR ASN
SEQRES 8 A 319 LEU ASP PHE ASP GLN ASP ASP CYS SER LEU THR SER GLY
SEQRES 9 A 319 CYS GLY VAL HIS SER GLY PHE GLN ASN ALA TRP ASN GLU
SEQRES 10 A 319 ILE SER ALA ALA ALA THR ALA ALA VAL ALA LYS ALA ARG
SEQRES 11 A 319 LYS ALA ASN PRO SER PHE LYS VAL VAL SER VAL GLY HIS
SEQRES 12 A 319 SER LEU GLY GLY ALA VAL ALA THR LEU ALA GLY ALA ASN
SEQRES 13 A 319 LEU ARG ILE GLY GLY THR PRO LEU ASP ILE TYR THR TYR
SEQRES 14 A 319 GLY SER PRO ARG VAL GLY ASN THR GLN LEU ALA ALA PHE
SEQRES 15 A 319 VAL SER ASN GLN ALA GLY GLY GLU PHE ARG VAL THR ASN
SEQRES 16 A 319 ALA LYS ASP PRO VAL PRO ARG LEU PRO PRO LEU ILE PHE
SEQRES 17 A 319 GLY TYR ARG HIS THR SER PRO GLU TYR TRP LEU SER GLY
SEQRES 18 A 319 SER GLY GLY ASP LYS ILE ASP TYR THR ILE ASN ASP VAL
SEQRES 19 A 319 LYS VAL CYS GLU GLY ALA ALA ASN LEU GLN CYS ASN GLY
SEQRES 20 A 319 GLY THR LEU GLY LEU ASP ILE ASP ALA HIS LEU HIS TYR
SEQRES 21 A 319 PHE GLN ALA THR ASP ALA CYS SER ALA GLY GLY ILE SER
SEQRES 22 A 319 TRP ARG ARG TYR ARG SER ALA LYS ARG GLU SER ILE SER
SEQRES 23 A 319 GLU ARG ALA THR MET THR ASP ALA GLU LEU GLU LYS LYS
SEQRES 24 A 319 LEU ASN SER TYR VAL GLU MET ASP LYS GLU TYR ILE LYS
SEQRES 25 A 319 THR HIS ALA SER ARG SER SER
SEQRES 1 B 319 ALA VAL SER VAL SER THR THR ASP PHE GLY ASN PHE LYS
SEQRES 2 B 319 PHE TYR ILE GLN HIS GLY ALA ALA ALA TYR CYS ASN SER
SEQRES 3 B 319 GLU ALA PRO ALA GLY ALA LYS VAL THR CYS SER GLY ASN
SEQRES 4 B 319 GLY CYS PRO THR VAL GLN SER ASN GLY ALA THR ILE VAL
SEQRES 5 B 319 ALA SER PHE THR GLY SER LYS THR GLY ILE GLY GLY TYR
SEQRES 6 B 319 VAL ALA THR ASP PRO THR ARG LYS GLU ILE VAL VAL SER
SEQRES 7 B 319 PHE ARG GLY SER ILE ASN ILE ARG ASN TRP LEU THR ASN
SEQRES 8 B 319 LEU ASP PHE ASP GLN ASP ASP CYS SER LEU THR SER GLY
SEQRES 9 B 319 CYS GLY VAL HIS SER GLY PHE GLN ASN ALA TRP ASN GLU
SEQRES 10 B 319 ILE SER ALA ALA ALA THR ALA ALA VAL ALA LYS ALA ARG
SEQRES 11 B 319 LYS ALA ASN PRO SER PHE LYS VAL VAL SER VAL GLY HIS
SEQRES 12 B 319 SER LEU GLY GLY ALA VAL ALA THR LEU ALA GLY ALA ASN
SEQRES 13 B 319 LEU ARG ILE GLY GLY THR PRO LEU ASP ILE TYR THR TYR
SEQRES 14 B 319 GLY SER PRO ARG VAL GLY ASN THR GLN LEU ALA ALA PHE
SEQRES 15 B 319 VAL SER ASN GLN ALA GLY GLY GLU PHE ARG VAL THR ASN
SEQRES 16 B 319 ALA LYS ASP PRO VAL PRO ARG LEU PRO PRO LEU ILE PHE
SEQRES 17 B 319 GLY TYR ARG HIS THR SER PRO GLU TYR TRP LEU SER GLY
SEQRES 18 B 319 SER GLY GLY ASP LYS ILE ASP TYR THR ILE ASN ASP VAL
SEQRES 19 B 319 LYS VAL CYS GLU GLY ALA ALA ASN LEU GLN CYS ASN GLY
SEQRES 20 B 319 GLY THR LEU GLY LEU ASP ILE ASP ALA HIS LEU HIS TYR
SEQRES 21 B 319 PHE GLN ALA THR ASP ALA CYS SER ALA GLY GLY ILE SER
SEQRES 22 B 319 TRP ARG ARG TYR ARG SER ALA LYS ARG GLU SER ILE SER
SEQRES 23 B 319 GLU ARG ALA THR MET THR ASP ALA GLU LEU GLU LYS LYS
SEQRES 24 B 319 LEU ASN SER TYR VAL GLU MET ASP LYS GLU TYR ILE LYS
SEQRES 25 B 319 THR HIS ALA SER ARG SER SER
SEQRES 1 C 319 ALA VAL SER VAL SER THR THR ASP PHE GLY ASN PHE LYS
SEQRES 2 C 319 PHE TYR ILE GLN HIS GLY ALA ALA ALA TYR CYS ASN SER
SEQRES 3 C 319 GLU ALA PRO ALA GLY ALA LYS VAL THR CYS SER GLY ASN
SEQRES 4 C 319 GLY CYS PRO THR VAL GLN SER ASN GLY ALA THR ILE VAL
SEQRES 5 C 319 ALA SER PHE THR GLY SER LYS THR GLY ILE GLY GLY TYR
SEQRES 6 C 319 VAL ALA THR ASP PRO THR ARG LYS GLU ILE VAL VAL SER
SEQRES 7 C 319 PHE ARG GLY SER ILE ASN ILE ARG ASN TRP LEU THR ASN
SEQRES 8 C 319 LEU ASP PHE ASP GLN ASP ASP CYS SER LEU THR SER GLY
SEQRES 9 C 319 CYS GLY VAL HIS SER GLY PHE GLN ASN ALA TRP ASN GLU
SEQRES 10 C 319 ILE SER ALA ALA ALA THR ALA ALA VAL ALA LYS ALA ARG
SEQRES 11 C 319 LYS ALA ASN PRO SER PHE LYS VAL VAL SER VAL GLY HIS
SEQRES 12 C 319 SER LEU GLY GLY ALA VAL ALA THR LEU ALA GLY ALA ASN
SEQRES 13 C 319 LEU ARG ILE GLY GLY THR PRO LEU ASP ILE TYR THR TYR
SEQRES 14 C 319 GLY SER PRO ARG VAL GLY ASN THR GLN LEU ALA ALA PHE
SEQRES 15 C 319 VAL SER ASN GLN ALA GLY GLY GLU PHE ARG VAL THR ASN
SEQRES 16 C 319 ALA LYS ASP PRO VAL PRO ARG LEU PRO PRO LEU ILE PHE
SEQRES 17 C 319 GLY TYR ARG HIS THR SER PRO GLU TYR TRP LEU SER GLY
SEQRES 18 C 319 SER GLY GLY ASP LYS ILE ASP TYR THR ILE ASN ASP VAL
SEQRES 19 C 319 LYS VAL CYS GLU GLY ALA ALA ASN LEU GLN CYS ASN GLY
SEQRES 20 C 319 GLY THR LEU GLY LEU ASP ILE ASP ALA HIS LEU HIS TYR
SEQRES 21 C 319 PHE GLN ALA THR ASP ALA CYS SER ALA GLY GLY ILE SER
SEQRES 22 C 319 TRP ARG ARG TYR ARG SER ALA LYS ARG GLU SER ILE SER
SEQRES 23 C 319 GLU ARG ALA THR MET THR ASP ALA GLU LEU GLU LYS LYS
SEQRES 24 C 319 LEU ASN SER TYR VAL GLU MET ASP LYS GLU TYR ILE LYS
SEQRES 25 C 319 THR HIS ALA SER ARG SER SER
SEQRES 1 D 319 ALA VAL SER VAL SER THR THR ASP PHE GLY ASN PHE LYS
SEQRES 2 D 319 PHE TYR ILE GLN HIS GLY ALA ALA ALA TYR CYS ASN SER
SEQRES 3 D 319 GLU ALA PRO ALA GLY ALA LYS VAL THR CYS SER GLY ASN
SEQRES 4 D 319 GLY CYS PRO THR VAL GLN SER ASN GLY ALA THR ILE VAL
SEQRES 5 D 319 ALA SER PHE THR GLY SER LYS THR GLY ILE GLY GLY TYR
SEQRES 6 D 319 VAL ALA THR ASP PRO THR ARG LYS GLU ILE VAL VAL SER
SEQRES 7 D 319 PHE ARG GLY SER ILE ASN ILE ARG ASN TRP LEU THR ASN
SEQRES 8 D 319 LEU ASP PHE ASP GLN ASP ASP CYS SER LEU THR SER GLY
SEQRES 9 D 319 CYS GLY VAL HIS SER GLY PHE GLN ASN ALA TRP ASN GLU
SEQRES 10 D 319 ILE SER ALA ALA ALA THR ALA ALA VAL ALA LYS ALA ARG
SEQRES 11 D 319 LYS ALA ASN PRO SER PHE LYS VAL VAL SER VAL GLY HIS
SEQRES 12 D 319 SER LEU GLY GLY ALA VAL ALA THR LEU ALA GLY ALA ASN
SEQRES 13 D 319 LEU ARG ILE GLY GLY THR PRO LEU ASP ILE TYR THR TYR
SEQRES 14 D 319 GLY SER PRO ARG VAL GLY ASN THR GLN LEU ALA ALA PHE
SEQRES 15 D 319 VAL SER ASN GLN ALA GLY GLY GLU PHE ARG VAL THR ASN
SEQRES 16 D 319 ALA LYS ASP PRO VAL PRO ARG LEU PRO PRO LEU ILE PHE
SEQRES 17 D 319 GLY TYR ARG HIS THR SER PRO GLU TYR TRP LEU SER GLY
SEQRES 18 D 319 SER GLY GLY ASP LYS ILE ASP TYR THR ILE ASN ASP VAL
SEQRES 19 D 319 LYS VAL CYS GLU GLY ALA ALA ASN LEU GLN CYS ASN GLY
SEQRES 20 D 319 GLY THR LEU GLY LEU ASP ILE ASP ALA HIS LEU HIS TYR
SEQRES 21 D 319 PHE GLN ALA THR ASP ALA CYS SER ALA GLY GLY ILE SER
SEQRES 22 D 319 TRP ARG ARG TYR ARG SER ALA LYS ARG GLU SER ILE SER
SEQRES 23 D 319 GLU ARG ALA THR MET THR ASP ALA GLU LEU GLU LYS LYS
SEQRES 24 D 319 LEU ASN SER TYR VAL GLU MET ASP LYS GLU TYR ILE LYS
SEQRES 25 D 319 THR HIS ALA SER ARG SER SER
FORMUL 5 HOH *218(H2 O)
HELIX 1 1 SER A 5 SER A 26 1 22
HELIX 2 2 CYS A 41 ASN A 47 1 7
HELIX 3 3 ASN A 84 LEU A 92 1 9
HELIX 4 4 SER A 109 ALA A 132 1 24
HELIX 5 5 SER A 144 GLY A 160 1 17
HELIX 6 6 THR A 177 GLN A 186 1 10
HELIX 7 7 PRO A 199 LEU A 203 5 5
HELIX 8 8 PRO A 205 PHE A 208 5 4
HELIX 9 9 THR A 230 ASN A 232 5 3
HELIX 10 10 ASP A 253 LEU A 258 1 6
HELIX 11 11 ALA A 263 CYS A 267 5 5
HELIX 12 12 THR A 292 THR A 313 1 22
HELIX 13 13 SER B 5 ALA B 21 1 17
HELIX 14 14 ALA B 22 CYS B 24 5 3
HELIX 15 15 CYS B 41 ASN B 47 1 7
HELIX 16 16 ASN B 84 LEU B 92 1 9
HELIX 17 17 SER B 109 ALA B 132 1 24
HELIX 18 18 SER B 144 GLY B 161 1 18
HELIX 19 19 THR B 177 GLN B 186 1 10
HELIX 20 20 PRO B 205 PHE B 208 5 4
HELIX 21 21 THR B 230 ASN B 232 5 3
HELIX 22 22 ASP B 253 LEU B 258 1 6
HELIX 23 23 THR B 264 SER B 268 5 5
HELIX 24 24 THR B 292 ALA B 315 1 24
HELIX 25 25 SER C 5 ASN C 25 1 21
HELIX 26 26 CYS C 36 GLY C 40 5 5
HELIX 27 27 CYS C 41 ASN C 47 1 7
HELIX 28 28 ASN C 84 LEU C 92 1 9
HELIX 29 29 SER C 109 LYS C 131 1 23
HELIX 30 30 SER C 144 GLY C 161 1 18
HELIX 31 31 ASN C 176 GLN C 186 1 11
HELIX 32 32 PRO C 199 LEU C 203 5 5
HELIX 33 33 PRO C 205 GLY C 209 5 5
HELIX 34 34 CYS C 245 THR C 249 5 5
HELIX 35 35 ASP C 253 LEU C 258 1 6
HELIX 36 36 THR C 292 THR C 313 1 22
HELIX 37 37 SER D 5 ALA D 22 1 18
HELIX 38 38 TYR D 23 ALA D 28 5 6
HELIX 39 39 CYS D 41 SER D 46 1 6
HELIX 40 40 ASN D 84 LEU D 92 1 9
HELIX 41 41 SER D 109 ASN D 133 1 25
HELIX 42 42 SER D 144 THR D 162 1 19
HELIX 43 43 THR D 177 GLN D 186 1 10
HELIX 44 44 PRO D 205 PHE D 208 5 4
HELIX 45 45 THR D 230 VAL D 234 5 5
HELIX 46 46 ASP D 253 LEU D 258 1 6
HELIX 47 47 THR D 292 HIS D 314 1 23
SHEET 1 A 8 THR A 50 THR A 56 0
SHEET 2 A 8 GLY A 63 ASP A 69 -1 O VAL A 66 N VAL A 52
SHEET 3 A 8 GLU A 74 PHE A 79 -1 O SER A 78 N TYR A 65
SHEET 4 A 8 LYS A 137 HIS A 143 1 O LYS A 137 N ILE A 75
SHEET 5 A 8 ILE A 166 TYR A 169 1 O TYR A 167 N SER A 140
SHEET 6 A 8 GLU A 190 ASN A 195 1 O VAL A 193 N THR A 168
SHEET 7 A 8 GLU A 216 LEU A 219 1 O LEU A 219 N THR A 194
SHEET 8 A 8 VAL A 234 CYS A 237 -1 O LYS A 235 N TRP A 218
SHEET 1 B 2 GLN A 96 ASP A 98 0
SHEET 2 B 2 GLY A 106 HIS A 108 -1 O VAL A 107 N ASP A 97
SHEET 1 C 2 GLY A 175 ASN A 176 0
SHEET 2 C 2 TYR A 210 ARG A 211 -1 O ARG A 211 N GLY A 175
SHEET 1 D 8 THR B 50 THR B 56 0
SHEET 2 D 8 GLY B 63 ASP B 69 -1 O VAL B 66 N VAL B 52
SHEET 3 D 8 GLU B 74 PHE B 79 -1 O VAL B 76 N ALA B 67
SHEET 4 D 8 LYS B 137 HIS B 143 1 O LYS B 137 N ILE B 75
SHEET 5 D 8 LEU B 164 TYR B 169 1 O ASP B 165 N SER B 140
SHEET 6 D 8 GLU B 190 ASN B 195 1 O VAL B 193 N THR B 168
SHEET 7 D 8 GLU B 216 LEU B 219 1 O LEU B 219 N THR B 194
SHEET 8 D 8 VAL B 234 CYS B 237 -1 O LYS B 235 N TRP B 218
SHEET 1 E 2 GLN B 96 ASP B 98 0
SHEET 2 E 2 GLY B 106 HIS B 108 -1 O VAL B 107 N ASP B 97
SHEET 1 F 2 GLY B 175 ASN B 176 0
SHEET 2 F 2 TYR B 210 ARG B 211 -1 O ARG B 211 N GLY B 175
SHEET 1 G 8 THR C 50 THR C 56 0
SHEET 2 G 8 GLY C 63 ASP C 69 -1 O VAL C 66 N VAL C 52
SHEET 3 G 8 GLU C 74 PHE C 79 -1 O VAL C 76 N ALA C 67
SHEET 4 G 8 LYS C 137 HIS C 143 1 O VAL C 139 N ILE C 75
SHEET 5 G 8 ASP C 165 TYR C 169 1 O TYR C 167 N SER C 140
SHEET 6 G 8 GLU C 190 ASN C 195 1 O VAL C 193 N THR C 168
SHEET 7 G 8 GLU C 216 LEU C 219 1 O LEU C 219 N THR C 194
SHEET 8 G 8 VAL C 234 VAL C 236 -1 O LYS C 235 N TRP C 218
SHEET 1 H 2 GLN C 96 ASP C 97 0
SHEET 2 H 2 VAL C 107 HIS C 108 -1 O VAL C 107 N ASP C 97
SHEET 1 I 8 THR D 50 SER D 54 0
SHEET 2 I 8 GLY D 64 ASP D 69 -1 O THR D 68 N THR D 50
SHEET 3 I 8 GLU D 74 PHE D 79 -1 O VAL D 76 N ALA D 67
SHEET 4 I 8 LYS D 137 HIS D 143 1 O LYS D 137 N ILE D 75
SHEET 5 I 8 LEU D 164 TYR D 169 1 O TYR D 169 N GLY D 142
SHEET 6 I 8 GLU D 190 ASN D 195 1 O PHE D 191 N ILE D 166
SHEET 7 I 8 GLU D 216 LEU D 219 1 O TYR D 217 N THR D 194
SHEET 8 I 8 VAL D 236 CYS D 237 -1 O CYS D 237 N GLU D 216
SHEET 1 J 2 GLN D 96 ASP D 97 0
SHEET 2 J 2 VAL D 107 HIS D 108 -1 O VAL D 107 N ASP D 97
SHEET 1 K 2 GLY D 175 ASN D 176 0
SHEET 2 K 2 TYR D 210 ARG D 211 -1 O ARG D 211 N GLY D 175
SSBOND 1 CYS A 24 CYS A 267 1555 1555 1.50
SSBOND 2 CYS A 36 CYS A 41 1555 1555 2.04
SSBOND 3 CYS A 99 CYS A 105 1555 1555 2.05
SSBOND 4 CYS A 237 CYS A 245 1555 1555 2.02
SSBOND 5 CYS B 24 CYS B 267 1555 1555 2.04
SSBOND 6 CYS B 36 CYS B 41 1555 1555 2.04
SSBOND 7 CYS B 99 CYS B 105 1555 1555 2.04
SSBOND 8 CYS B 237 CYS B 245 1555 1555 2.02
SSBOND 9 CYS C 24 CYS C 267 1555 1555 2.03
SSBOND 10 CYS C 36 CYS C 41 1555 1555 2.04
SSBOND 11 CYS C 99 CYS C 105 1555 1555 2.04
SSBOND 12 CYS C 237 CYS C 245 1555 1555 2.02
SSBOND 13 CYS D 24 CYS D 267 1555 1555 2.03
SSBOND 14 CYS D 36 CYS D 41 1555 1555 2.03
SSBOND 15 CYS D 99 CYS D 105 1555 1555 2.04
SSBOND 16 CYS D 237 CYS D 245 1555 1555 2.02
CISPEP 1 LEU A 203 PRO A 204 0 -0.35
CISPEP 2 SER A 214 PRO A 215 0 -0.14
CISPEP 3 LEU B 203 PRO B 204 0 0.13
CISPEP 4 SER B 214 PRO B 215 0 0.68
CISPEP 5 LEU C 203 PRO C 204 0 -0.32
CISPEP 6 SER C 214 PRO C 215 0 0.39
CISPEP 7 LEU D 203 PRO D 204 0 -0.12
CISPEP 8 SER D 214 PRO D 215 0 0.13
CRYST1 78.417 91.001 195.802 90.00 90.00 90.00 P 21 21 21 16
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 0.012752 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005107 0.00000
TER 2199 SER A 318
TER 4398 SER B 318
TER 6597 SER C 318
TER 8796 SER D 318
MASTER 532 0 0 47 46 0 0 6 9010 4 32 100
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