HEADER HYDROLASE 28-AUG-98 1BSI
TITLE HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: PANCREAS;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS AMYLASE, PICHIA PASTORIS, GLYCOSYLATED PROTEIN, MUTAGENESIS,
KEYWDS 2 DIABETES, CATALYSIS, PANCREATIC, ENZYME, HUMAN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.H.RYDBERG,G.SIDHU,H.C.VO,J.HEWITT,H.C.F.COTE,Y.WANG,S.NUMAO,
AUTHOR 2 R.T.A.MACGILLIVRAY,C.M.OVERALL,G.D.BRAYER,S.G.WITHERS
REVDAT 6 29-JUL-20 1BSI 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 25-DEC-19 1BSI 1 SEQRES LINK
REVDAT 4 13-JUL-11 1BSI 1 VERSN
REVDAT 3 24-FEB-09 1BSI 1 VERSN
REVDAT 2 01-APR-03 1BSI 1 JRNL
REVDAT 1 18-MAY-99 1BSI 0
JRNL AUTH E.H.RYDBERG,G.SIDHU,H.C.VO,J.HEWITT,H.C.COTE,Y.WANG,S.NUMAO,
JRNL AUTH 2 R.T.MACGILLIVRAY,C.M.OVERALL,G.D.BRAYER,S.G.WITHERS
JRNL TITL CLONING, MUTAGENESIS, AND STRUCTURAL ANALYSIS OF HUMAN
JRNL TITL 2 PANCREATIC ALPHA-AMYLASE EXPRESSED IN PICHIA PASTORIS.
JRNL REF PROTEIN SCI. V. 8 635 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10091666
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 31856
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 3946
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 222
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.450
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 1BSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172054.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 26.45500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.88500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.88500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.45500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 239 N - CA - C ANGL. DEV. = 16.1 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 TYR A 31 -51.76 -139.32
REMARK 500 MET A 102 -144.95 -111.53
REMARK 500 THR A 163 51.98 39.41
REMARK 500 ASP A 317 49.89 -102.75
REMARK 500 THR A 376 -4.32 77.36
REMARK 500 SER A 414 -109.40 -131.84
REMARK 500 ASP A 433 33.95 -92.34
REMARK 500 PRO A 486 41.66 -74.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 498 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100 OD1
REMARK 620 2 ARG A 158 O 158.1
REMARK 620 3 ASP A 167 OD1 80.8 117.9
REMARK 620 4 ASP A 167 OD2 124.9 77.0 50.1
REMARK 620 5 HIS A 201 O 75.6 82.5 142.8 159.3
REMARK 620 6 HOH A 501 O 74.0 119.7 76.0 71.4 122.8
REMARK 620 7 HOH A 543 O 103.0 73.2 133.5 96.4 80.4 61.4
REMARK 620 8 HOH A 721 O 97.1 80.5 69.8 88.7 84.9 145.7 151.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF 1BSI A 2 496 UNP P04746 AMYP_HUMAN 17 511
SEQRES 1 A 496 PCA TYR SER PRO ASN THR GLN GLN GLY ARG THR SER ILE
SEQRES 2 A 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 A 496 GLU CYS GLU ARG TYR LEU ALA PRO LYS GLY PHE GLY GLY
SEQRES 4 A 496 VAL GLN VAL SER PRO PRO ASN GLU ASN VAL ALA ILE TYR
SEQRES 5 A 496 ASN PRO PHE ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 A 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASP GLU
SEQRES 7 A 496 PHE ARG ASN MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 A 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 A 496 ASN ALA VAL SER ALA GLY THR SER SER THR CYS GLY SER
SEQRES 10 A 496 TYR PHE ASN PRO GLY SER ARG ASP PHE PRO ALA VAL PRO
SEQRES 11 A 496 TYR SER GLY TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 A 496 GLY SER GLY ASP ILE GLU ASN TYR ASN ASP ALA THR GLN
SEQRES 13 A 496 VAL ARG ASP CYS ARG LEU THR GLY LEU LEU ASP LEU ALA
SEQRES 14 A 496 LEU GLU LYS ASP TYR VAL ARG SER LYS ILE ALA GLU TYR
SEQRES 15 A 496 MET ASN HIS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 A 496 LEU ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 A 496 ALA ILE LEU ASP LYS LEU HIS ASN LEU ASN SER ASN TRP
SEQRES 18 A 496 PHE PRO ALA GLY SER LYS PRO PHE ILE TYR GLN GLU VAL
SEQRES 19 A 496 ILE ASP LEU GLY GLY GLU PRO ILE LYS SER SER ASP TYR
SEQRES 20 A 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 A 496 LYS LEU GLY THR VAL ILE ARG LYS TRP ASN GLY GLU LYS
SEQRES 22 A 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 A 496 VAL PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 A 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY ALA SER ILE
SEQRES 25 A 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS MET ALA VAL
SEQRES 26 A 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 A 496 MET SER SER TYR ARG TRP PRO ARG GLN PHE GLN ASN GLY
SEQRES 28 A 496 ASN ASP VAL ASN ASP TRP VAL GLY PRO PRO ASN ASN ASN
SEQRES 29 A 496 GLY VAL ILE LYS GLU VAL THR ILE ASN PRO ASP THR THR
SEQRES 30 A 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLN
SEQRES 31 A 496 ILE ARG ASN MET VAL ILE PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 A 496 GLN PRO PHE THR ASN TRP TYR ASP ASN GLY SER ASN GLN
SEQRES 33 A 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 A 496 ASN ASN ASP ASP TRP SER PHE SER LEU THR LEU GLN THR
SEQRES 35 A 496 GLY LEU PRO ALA GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 A 496 ASP LYS ILE ASN GLY ASN CYS THR GLY ILE LYS ILE TYR
SEQRES 37 A 496 VAL SER ASP ASP GLY LYS ALA HIS PHE SER ILE SER ASN
SEQRES 38 A 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 A 496 LYS LEU
MODRES 1BSI ASN A 461 ASN GLYCOSYLATION SITE
MODRES 1BSI PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 8
HET NAG A 497 14
HET CA A 498 1
HET CL A 499 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 PCA C5 H7 N O3
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 CA CA 2+
FORMUL 4 CL CL 1-
FORMUL 5 HOH *222(H2 O)
HELIX 1 1 TRP A 21 ARG A 30 1 10
HELIX 2 2 TRP A 58 TYR A 62 5 5
HELIX 3 3 GLU A 76 VAL A 89 1 14
HELIX 4 4 GLY A 133 ASP A 135 5 3
HELIX 5 5 ALA A 154 ASP A 159 1 6
HELIX 6 6 LEU A 162 GLY A 164 5 3
HELIX 7 7 ASP A 173 ILE A 189 1 17
HELIX 8 8 SER A 199 HIS A 201 5 3
HELIX 9 9 PRO A 204 LYS A 213 1 10
HELIX 10 10 SER A 244 TYR A 247 5 4
HELIX 11 11 PHE A 256 ILE A 266 1 11
HELIX 12 12 TRP A 269 GLY A 271 5 3
HELIX 13 13 MET A 274 ASN A 279 5 6
HELIX 14 14 GLU A 282 TRP A 284 5 3
HELIX 15 15 SER A 289 ARG A 291 5 3
HELIX 16 16 ASN A 301 ARG A 303 5 3
HELIX 17 17 GLY A 309 SER A 311 5 3
HELIX 18 18 PHE A 315 ALA A 330 5 16
HELIX 19 19 GLU A 385 ARG A 387 5 3
HELIX 20 20 ARG A 389 VAL A 400 1 12
HELIX 21 21 ALA A 492 SER A 494 5 3
SHEET 1 A 6 THR A 336 SER A 340 0
SHEET 2 A 6 SER A 12 LEU A 16 1 N ILE A 13 O THR A 336
SHEET 3 A 6 GLY A 39 VAL A 42 1 N GLY A 39 O VAL A 14
SHEET 4 A 6 ARG A 92 ALA A 97 1 N ARG A 92 O VAL A 40
SHEET 5 A 6 GLY A 193 LEU A 196 1 N GLY A 193 O VAL A 95
SHEET 6 A 6 PHE A 229 GLN A 232 1 N PHE A 229 O PHE A 194
SHEET 1 B 3 GLN A 416 ARG A 421 0
SHEET 2 B 3 GLY A 425 ASN A 430 -1 N PHE A 429 O VAL A 417
SHEET 3 B 3 PHE A 487 HIS A 491 -1 N ILE A 490 O PHE A 426
SHEET 1 C 2 PHE A 436 GLN A 441 0
SHEET 2 C 2 LYS A 474 ILE A 479 -1 N ILE A 479 O PHE A 436
SHEET 1 D 2 GLY A 447 CYS A 450 0
SHEET 2 D 2 LYS A 466 VAL A 469 -1 N VAL A 469 O GLY A 447
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.03
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.03
SSBOND 3 CYS A 141 CYS A 160 1555 1555 2.03
SSBOND 4 CYS A 378 CYS A 384 1555 1555 2.02
SSBOND 5 CYS A 450 CYS A 462 1555 1555 2.02
LINK C PCA A 1 N TYR A 2 1555 1555 1.34
LINK ND2 ASN A 461 C1 NAG A 497 1555 1555 1.45
LINK OD1 ASN A 100 CA CA A 498 1555 1555 2.44
LINK O ARG A 158 CA CA A 498 1555 1555 2.44
LINK OD1 ASP A 167 CA CA A 498 1555 1555 2.61
LINK OD2 ASP A 167 CA CA A 498 1555 1555 2.55
LINK O HIS A 201 CA CA A 498 1555 1555 2.46
LINK CA CA A 498 O HOH A 501 1555 1555 2.44
LINK CA CA A 498 O HOH A 543 1555 1555 2.62
LINK CA CA A 498 O HOH A 721 1555 1555 2.62
CISPEP 1 ASN A 53 PRO A 54 0 0.16
CISPEP 2 VAL A 129 PRO A 130 0 -1.07
CRYST1 52.910 68.900 131.770 90.00 90.00 90.00 P 21 21 21 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 0.018900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007589 0.00000
HETATM 1 N PCA A 1 6.058 19.849 66.335 1.00 17.37 N
HETATM 2 CA PCA A 1 6.330 19.889 64.898 1.00 16.46 C
HETATM 3 CB PCA A 1 5.919 18.549 64.376 1.00 17.14 C
HETATM 4 CG PCA A 1 5.310 17.864 65.496 1.00 19.81 C
HETATM 5 CD PCA A 1 5.439 18.638 66.732 1.00 18.83 C
HETATM 6 OE PCA A 1 5.053 18.365 67.910 1.00 22.91 O
HETATM 7 C PCA A 1 5.547 20.961 64.157 1.00 13.85 C
HETATM 8 O PCA A 1 5.724 21.089 62.931 1.00 13.51 O
(ATOM LINES ARE NOT SHOWN.)
END
