| content |
HEADER HYDROLASE 21-NOV-02 1N8S
TITLE STRUCTURE OF THE PANCREATIC LIPASE-COLIPASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE, PANCREATIC;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PANCREATIC LIPASE, PL;
COMPND 5 EC: 3.1.1.3;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: COLIPASE II;
COMPND 8 CHAIN: C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 OTHER_DETAILS: PANCREATIC JUICE;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 7 ORGANISM_COMMON: PIG;
SOURCE 8 OTHER_DETAILS: EXTRACTED FROM PANCREAS
KEYWDS HYDROLASE, PANCREAS, SIGNAL
EXPDTA X-RAY DIFFRACTION
AUTHOR H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU
REVDAT 1 18-DEC-02 1N8S 0
JRNL AUTH H.VAN TILBEURGH,L.SARDA,R.VERGER,C.CAMBILLAU
JRNL TITL STRUCTURE OF THE PANCREATIC LIPASE-PROCOLIPASE
JRNL TITL 2 COMPLEX
JRNL REF NATURE V. 359 159 1992
JRNL REFN ASTM NATUAS UK ISSN 0028-0836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
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 : 17720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1114
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 : 4131
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : 0.003
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 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 1N8S COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-2002.
REMARK 100 THE RCSB ID CODE IS RCSB017661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-1991; 11-DEC-1991
REMARK 200 TEMPERATURE (KELVIN) : 277; 277
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : LURE ; LURE
REMARK 200 BEAMLINE : DW32; DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98; 0.98
REMARK 200 MONOCHROMATOR : MIRRORS; MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS
REMARK 200 DATA SCALING SOFTWARE : MARSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17720
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.040
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08500
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) : 3.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
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: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL-0.2-0.5M, PEG 8000 2%, MES
REMARK 280 0.1M, BETAOG BEYOND CMC, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,1/3-Z
REMARK 290 6555 -X,-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 167.33333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.66667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.66667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 167.33333
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, 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 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 VAL C 501
REMARK 465 PRO C 502
REMARK 465 ASP C 503
REMARK 465 PRO C 504
REMARK 465 ARG C 505
REMARK 465 GLY C 591
REMARK 465 ARG C 592
REMARK 465 SER C 593
REMARK 465 ASP C 594
REMARK 465 SER C 595
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 ARG A 337 CA - CB - CG ANGL. DEV. =-25.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ARG A 7 -52.74 82.20
REMARK 500 SER A 333 -105.51 53.06
REMARK 500 THR C 532 142.85 73.80
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LPA RELATED DB: PDB
REMARK 900 RELATED ID: 1LPB RELATED DB: PDB
DBREF 1N8S A 1 449 SWS P16233 LIPP_HUMAN 17 465
DBREF 1N8S C 501 595 PIR XLPG2 XLPG2 1 95
SEQRES 1 A 449 LYS GLU VAL CYS TYR GLU ARG LEU GLY CYS PHE SER ASP
SEQRES 2 A 449 ASP SER PRO TRP SER GLY ILE THR GLU ARG PRO LEU HIS
SEQRES 3 A 449 ILE LEU PRO TRP SER PRO LYS ASP VAL ASN THR ARG PHE
SEQRES 4 A 449 LEU LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN GLU
SEQRES 5 A 449 VAL ALA ALA ASP SER SER SER ILE SER GLY SER ASN PHE
SEQRES 6 A 449 LYS THR ASN ARG LYS THR ARG PHE ILE ILE HIS GLY PHE
SEQRES 7 A 449 ILE ASP LYS GLY GLU GLU ASN TRP LEU ALA ASN VAL CYS
SEQRES 8 A 449 LYS ASN LEU PHE LYS VAL GLU SER VAL ASN CYS ILE CYS
SEQRES 9 A 449 VAL ASP TRP LYS GLY GLY SER ARG THR GLY TYR THR GLN
SEQRES 10 A 449 ALA SER GLN ASN ILE ARG ILE VAL GLY ALA GLU VAL ALA
SEQRES 11 A 449 TYR PHE VAL GLU PHE LEU GLN SER ALA PHE GLY TYR SER
SEQRES 12 A 449 PRO SER ASN VAL HIS VAL ILE GLY HIS SER LEU GLY ALA
SEQRES 13 A 449 HIS ALA ALA GLY GLU ALA GLY ARG ARG THR ASN GLY THR
SEQRES 14 A 449 ILE GLY ARG ILE THR GLY LEU ASP PRO ALA GLU PRO CYS
SEQRES 15 A 449 PHE GLN GLY THR PRO GLU LEU VAL ARG LEU ASP PRO SER
SEQRES 16 A 449 ASP ALA LYS PHE VAL ASP VAL ILE HIS THR ASP GLY ALA
SEQRES 17 A 449 PRO ILE VAL PRO ASN LEU GLY PHE GLY MET SER GLN VAL
SEQRES 18 A 449 VAL GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY VAL GLU
SEQRES 19 A 449 MET PRO GLY CYS LYS LYS ASN ILE LEU SER GLN ILE VAL
SEQRES 20 A 449 ASP ILE ASP GLY ILE TRP GLU GLY THR ARG ASP PHE ALA
SEQRES 21 A 449 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR THR ASP
SEQRES 22 A 449 SER ILE VAL ASN PRO ASP GLY PHE ALA GLY PHE PRO CYS
SEQRES 23 A 449 ALA SER TYR ASN VAL PHE THR ALA ASN LYS CYS PHE PRO
SEQRES 24 A 449 CYS PRO SER GLY GLY CYS PRO GLN MET GLY HIS TYR ALA
SEQRES 25 A 449 ASP ARG TYR PRO GLY LYS THR ASN ASP VAL GLY GLN LYS
SEQRES 26 A 449 PHE TYR LEU ASP THR GLY ASP ALA SER ASN PHE ALA ARG
SEQRES 27 A 449 TRP ARG TYR LYS VAL SER VAL THR LEU SER GLY LYS LYS
SEQRES 28 A 449 VAL THR GLY HIS ILE LEU VAL SER LEU PHE GLY ASN LYS
SEQRES 29 A 449 GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY THR LEU
SEQRES 30 A 449 LYS PRO ASP SER THR HIS SER ASN GLU PHE ASP SER ASP
SEQRES 31 A 449 VAL ASP VAL GLY ASP LEU GLN MET VAL LYS PHE ILE TRP
SEQRES 32 A 449 TYR ASN ASN VAL ILE ASN PRO THR LEU PRO ARG VAL GLY
SEQRES 33 A 449 ALA SER LYS ILE ILE VAL GLU THR ASN VAL GLY LYS GLN
SEQRES 34 A 449 PHE ASN PHE CYS SER PRO GLU THR VAL ARG GLU GLU VAL
SEQRES 35 A 449 LEU LEU THR LEU THR PRO CYS
SEQRES 1 C 95 VAL PRO ASP PRO ARG GLY ILE ILE ILE ASN LEU ASP GLU
SEQRES 2 C 95 GLY GLU LEU CYS LEU ASN SER ALA GLN CYS LYS SER ASN
SEQRES 3 C 95 CYS CYS GLN HIS ASP THR ILE LEU SER LEU LEU ARG CYS
SEQRES 4 C 95 ALA LEU LYS ALA ARG GLU ASN SER GLU CYS SER ALA PHE
SEQRES 5 C 95 THR LEU TYR GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG
SEQRES 6 C 95 GLY LEU THR CYS GLU GLY ASP LYS SER LEU VAL GLY SER
SEQRES 7 C 95 ILE THR ASN THR ASN PHE GLY ILE CYS HIS ASN VAL GLY
SEQRES 8 C 95 ARG SER ASP SER
HELIX 1 1 SER A 30B ASN A 35 1 6
HELIX 2 2 ASP A 55 SER A 60 1 6
HELIX 3 3 GLY A 81 GLU A 83 5 3
HELIX 4 4 ASN A 84 GLU A 97 1 14
HELIX 5 5 TRP A 106 ARG A 111 1 6
HELIX 6 6 GLY A 113 GLY A 140 1 28
HELIX 7 7 SER A 142 SER A 144 5 3
HELIX 8 8 SER A 152 THR A 165 1 14
HELIX 9 9 ASP A 192 ALA A 196 5 5
HELIX 10 10 ASP A 247 GLU A 253 1 7
HELIX 11 11 ALA A 260 VAL A 275 1 16
HELIX 12 12 SER A 287 ALA A 293 1 7
HELIX 13 13 TYR A 310 TYR A 314 5 5
HELIX 14 14 ASN C 519 CYS C 523 5 5
SHEET 1 A 2 CYS A 4 TYR A 5 0
SHEET 2 A 2 GLY A 9 CYS A 10 -1 O GLY A 9 N TYR A 5
SHEET 1 B 9 ASN A 45 VAL A 52 0
SHEET 2 B 9 ARG A 37 THR A 42 -1 O PHE A 38 N VAL A 52
SHEET 3 B 9 VAL A 99 ASP A 105 -1 N CYS A 101 O TYR A 41
SHEET 4 B 9 LYS A 69 ILE A 74 1 O LYS A 69 N ASN A 100
SHEET 5 B 9 VAL A 146 HIS A 151 1 O HIS A 147 N PHE A 72
SHEET 6 B 9 ARG A 171 LEU A 175 1 O ARG A 171 N VAL A 148
SHEET 7 B 9 PHE A 198 ILE A 202 1 O PHE A 198 N ILE A 172
SHEET 8 B 9 LEU A 224 PRO A 228 1 O LEU A 224 N VAL A 201
SHEET 9 B 9 GLN A 323 LEU A 327 1 O GLN A 323 N ASP A 225
SHEET 1 C12 THR A 381 SER A 388 0
SHEET 2 C12 TRP A 338 GLY A 348 -1 N TRP A 338 O SER A 388
SHEET 3 C12 ARG A 414 GLU A 423 -1 N GLY A 416 O SER A 347
SHEET 4 C12 VAL A 438 ARG A 439 -1 N VAL A 438 O VAL A 415
SHEET 5 C12 ARG A 414 GLU A 423 -1 O VAL A 415 N VAL A 438
SHEET 6 C12 GLN A 429 CYS A 433 -1 N PHE A 430 O VAL A 422
SHEET 7 C12 LEU A 444 PRO A 448 -1 O THR A 447 N CYS A 433
SHEET 8 C12 LEU A 395 TYR A 403 -1 O VAL A 398 N LEU A 446
SHEET 9 C12 VAL A 351 GLY A 361 -1 N HIS A 354 O TYR A 403
SHEET 10 C12 GLY A 364 ASN A 365 -1 O GLY A 364 N GLY A 361
SHEET 11 C12 VAL A 351 GLY A 361 -1 N GLY A 361 O GLY A 364
SHEET 12 C12 TYR A 369 LEU A 376 -1 N TYR A 369 O VAL A 357
SHEET 1 D 2 CYS C 528 GLN C 529 0
SHEET 2 D 2 ARG C 538 CYS C 539 -1 N ARG C 538 O GLN C 529
SHEET 1 E 3 GLU C 548 SER C 550 0
SHEET 2 E 3 PHE C 584 ASN C 589 -1 O GLY C 585 N CYS C 549
SHEET 3 E 3 LEU C 567 GLY C 571 -1 N THR C 568 O HIS C 588
SSBOND 1 CYS A 4 CYS A 10
SSBOND 2 CYS A 90 CYS A 101
SSBOND 3 CYS A 237 CYS A 261
SSBOND 4 CYS A 285 CYS A 296
SSBOND 5 CYS A 299 CYS A 304
SSBOND 6 CYS A 433 CYS A 449
SSBOND 7 CYS C 517 CYS C 528
SSBOND 8 CYS C 523 CYS C 539
SSBOND 9 CYS C 527 CYS C 561
SSBOND 10 CYS C 549 CYS C 569
SSBOND 11 CYS C 563 CYS C 587
CISPEP 1 SER A 15 PRO A 16 0 16.55
CISPEP 2 VAL A 210 PRO A 211 0 16.18
CISPEP 3 PHE A 297 PRO A 298 0 -20.39
CRYST1 80.300 80.300 251.000 90.00 90.00 120.00 P 32 2 1 6
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 0.012453 0.007190 0.000000 0.00000
SCALE2 0.000000 0.014380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003984 0.00000
TER 3492 CYS A 449
TER 4133 VAL C 590
MASTER 259 0 0 14 28 0 0 6 4131 2 22 43
END |