HEADER HYDROLASE 06-SEP-12 3VX1
TITLE CRYSTAL STRUCTURE OF ALPHA-AMYLASE FROM ASPERGILLUS ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE A TYPE-1/2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE, TAKA-AMYLASE A, TAA;
COMPND 5 EC: 3.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_COMMON: YELLOW KOJI MOLD;
SOURCE 4 ORGANISM_TAXID: 510516;
SOURCE 5 STRAIN: ATCC 42149 / RIB 40
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUGAHARA
REVDAT 3 08-NOV-23 3VX1 1 HETSYN
REVDAT 2 29-JUL-20 3VX1 1 COMPND REMARK HETNAM LINK
REVDAT 2 2 1 SITE
REVDAT 1 11-SEP-13 3VX1 0
JRNL AUTH M.SUGAHARA
JRNL TITL CRYSTAL STRUCTURE OF ALPHA-AMYLASE FROM ASPERGILLUS ORYZAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
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) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 22852
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) : 0.208
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1147
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.3910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 107
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 299
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 3VX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000095606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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) : 1.54
REMARK 200 MONOCHROMATOR : MULTI-LAYER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23047
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 151288.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2TAA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CACL2, PH 5.8, OIL
REMARK 280 -MICROBATCH METHOD, TEMPERATURE 293K
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 25.18400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.77550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.33900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.77550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.18400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.33900
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 478
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 TRP A 216 NE1 TRP A 216 CE2 0.111
REMARK 500 TRP A 385 NE1 TRP A 385 CE2 0.110
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 ALA A 78 46.13 -86.67
REMARK 500 GLN A 85 -38.69 -137.81
REMARK 500 CYS A 150 146.41 -176.27
REMARK 500 THR A 207 51.04 38.15
REMARK 500 ALA A 329 124.85 -39.94
REMARK 500 ASP A 340 133.40 -36.33
REMARK 500 LYS A 389 146.48 -172.89
REMARK 500 SER A 472 173.18 -58.09
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 A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 121 OD1
REMARK 620 2 GLU A 162 O 152.7
REMARK 620 3 ASP A 175 OD2 121.5 84.0
REMARK 620 4 ASP A 175 OD1 80.5 115.3 49.2
REMARK 620 5 HIS A 210 O 77.5 76.0 159.2 136.7
REMARK 620 6 HOH A1315 O 109.6 68.6 104.5 149.7 73.4
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VX0 RELATED DB: PDB
DBREF 3VX1 A 1 478 UNP P0C1B3 AMYA1_ASPOR 22 499
SEQRES 1 A 478 ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES 2 A 478 LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES 3 A 478 THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES 4 A 478 GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES 5 A 478 GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES 6 A 478 THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES 7 A 478 TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES 8 A 478 GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES 9 A 478 SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES 10 A 478 VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES 11 A 478 SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES 12 A 478 ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES 13 A 478 ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES 14 A 478 THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES 15 A 478 VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES 16 A 478 SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES 17 A 478 LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES 18 A 478 ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES 19 A 478 ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES 20 A 478 GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES 21 A 478 ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES 22 A 478 ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES 23 A 478 THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES 24 A 478 ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES 25 A 478 ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES 26 A 478 ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES 27 A 478 ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES 28 A 478 TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES 29 A 478 ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES 30 A 478 GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES 31 A 478 ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES 32 A 478 GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES 33 A 478 ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES 34 A 478 ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES 35 A 478 VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES 36 A 478 ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES 37 A 478 LEU ALA GLY SER LYS ILE CYS SER SER SER
MODRES 3VX1 ASN A 197 ASN GLYCOSYLATION SITE
HET NAG A1001 14
HET CA A1002 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 CA CA 2+
FORMUL 4 HOH *299(H2 O)
HELIX 1 1 THR A 2 SER A 8 1 7
HELIX 2 2 LEU A 15 ALA A 20 1 6
HELIX 3 3 ASN A 31 GLN A 35 5 5
HELIX 4 4 THR A 41 ASP A 47 1 7
HELIX 5 5 LYS A 48 GLY A 54 1 7
HELIX 6 6 THR A 96 ARG A 110 1 15
HELIX 7 7 ASP A 133 PHE A 137 5 5
HELIX 8 8 SER A 142 PHE A 146 5 5
HELIX 9 9 ASP A 157 CYS A 164 1 8
HELIX 10 10 LYS A 180 SER A 199 1 20
HELIX 11 11 THR A 207 VAL A 211 5 5
HELIX 12 12 GLN A 212 ASP A 214 5 3
HELIX 13 13 PHE A 215 GLY A 224 1 10
HELIX 14 14 ASP A 235 CYS A 240 1 6
HELIX 15 15 PRO A 241 VAL A 245 5 5
HELIX 16 16 ASN A 251 LYS A 263 1 13
HELIX 17 17 SER A 268 CYS A 283 1 16
HELIX 18 18 ASP A 285 LEU A 288 5 4
HELIX 19 19 ARG A 300 THR A 305 1 6
HELIX 20 20 ASP A 307 ASN A 321 1 15
HELIX 21 21 GLY A 330 HIS A 334 5 5
HELIX 22 22 ALA A 346 GLY A 351 5 6
HELIX 23 23 SER A 356 ASP A 376 1 21
HELIX 24 24 GLU A 467 ALA A 470 5 4
SHEET 1 A 8 GLY A 248 VAL A 249 0
SHEET 2 A 8 TYR A 226 GLY A 229 1 N GLY A 229 O GLY A 248
SHEET 3 A 8 GLY A 202 ILE A 205 1 N LEU A 203 O ILE A 228
SHEET 4 A 8 TYR A 113 VAL A 118 1 N VAL A 118 O ARG A 204
SHEET 5 A 8 ALA A 59 ILE A 62 1 N ILE A 60 O MET A 115
SHEET 6 A 8 ILE A 11 LEU A 14 1 N LEU A 14 O TRP A 61
SHEET 7 A 8 ILE A 324 TYR A 328 1 O ILE A 327 N PHE A 13
SHEET 8 A 8 GLY A 290 THR A 291 1 N THR A 291 O ILE A 324
SHEET 1 B 2 THR A 66 GLN A 68 0
SHEET 2 B 2 GLN A 84 LEU A 90 -1 O GLN A 85 N ALA A 67
SHEET 1 C 3 TYR A 125 ASP A 126 0
SHEET 2 C 3 VAL A 171 LEU A 173 -1 O SER A 172 N TYR A 125
SHEET 3 C 3 LEU A 166 GLY A 167 -1 N LEU A 166 O LEU A 173
SHEET 1 D 6 TRP A 385 ASP A 390 0
SHEET 2 D 6 THR A 393 LYS A 398 -1 O ALA A 395 N TYR A 388
SHEET 3 D 6 ILE A 405 SER A 410 -1 O LEU A 409 N ILE A 394
SHEET 4 D 6 ARG A 461 PRO A 465 -1 O ARG A 461 N ILE A 408
SHEET 5 D 6 GLN A 433 GLU A 436 -1 N THR A 435 O TYR A 464
SHEET 6 D 6 THR A 441 THR A 444 -1 O THR A 441 N GLU A 436
SHEET 1 E 2 TYR A 419 LEU A 423 0
SHEET 2 E 2 VAL A 451 MET A 455 -1 O MET A 455 N TYR A 419
SSBOND 1 CYS A 30 CYS A 38 1555 1555 2.02
SSBOND 2 CYS A 150 CYS A 164 1555 1555 2.04
SSBOND 3 CYS A 240 CYS A 283 1555 1555 2.04
SSBOND 4 CYS A 440 CYS A 475 1555 1555 2.02
LINK ND2 ASN A 197 C1 NAG A1001 1555 1555 1.41
LINK OD1 ASN A 121 CA CA A1002 1555 1555 2.51
LINK O GLU A 162 CA CA A1002 1555 1555 2.67
LINK OD2 ASP A 175 CA CA A1002 1555 1555 2.63
LINK OD1 ASP A 175 CA CA A1002 1555 1555 2.69
LINK O HIS A 210 CA CA A1002 1555 1555 2.68
LINK CA CA A1002 O HOH A1315 1555 1555 2.90
CISPEP 1 LYS A 138 PRO A 139 0 0.25
CISPEP 2 ASP A 340 PRO A 341 0 -0.52
CRYST1 50.368 66.678 131.551 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 0.019854 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014997 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
