HEADER HYDROLASE 12-FEB-02 1L0P
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE COMPLEX BETWEEN PSYCHROPHILIC ALPHA
TITLE 2 AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS AND NITRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE 3 ORGANISM_TAXID: 228
KEYWDS BETA-ALPHA-8-BARREL, 3 DOMAIN STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.AGHAJARI,R.HASER
REVDAT 3 16-AUG-23 1L0P 1 REMARK LINK
REVDAT 2 24-FEB-09 1L0P 1 VERSN
REVDAT 1 19-JUN-02 1L0P 0
JRNL AUTH N.AGHAJARI,G.FELLER,C.GERDAY,R.HASER
JRNL TITL STRUCTURAL BASIS OF ALPHA-AMYLASE ACTIVATION BY CHLORIDE.
JRNL REF PROTEIN SCI. V. 11 1435 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 12021442
JRNL DOI 10.1110/PS.0202602
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.56
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 : 29614
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) : 0.146
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2956
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 : 3448
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.70
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.270
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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: FINAL CYCLE OF REFINEMENT WAS CARRIED
REMARK 3 OUT USING CNS.
REMARK 4
REMARK 4 1L0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015537.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-DEC-98
REMARK 200 TEMPERATURE (KELVIN) : 288.0
REMARK 200 PH : 7.00
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 : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29641
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 42.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.15000
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1AQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, HEPES, PH 7.00, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 35.65000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.20000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.65000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.20000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.45000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.65000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.20000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.45000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.65000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.20000
REMARK 290 SMTRY3 8 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: 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 23 -57.86 -130.31
REMARK 500 ASN A 129 15.33 -143.96
REMARK 500 ASP A 130 87.10 -150.36
REMARK 500 PRO A 295 48.80 -77.39
REMARK 500 PHE A 329 -8.82 71.24
REMARK 500 ALA A 330 -131.50 -106.01
REMARK 500 ASN A 332 -112.90 -112.23
REMARK 500 THR A 365 -5.13 73.67
REMARK 500 ASN A 366 -107.08 -132.83
REMARK 500 ASN A 432 69.88 -154.55
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 800 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 88 OD1
REMARK 620 2 GLN A 135 O 149.8
REMARK 620 3 ASP A 144 OD1 76.5 119.4
REMARK 620 4 ASP A 144 OD2 125.5 79.9 51.4
REMARK 620 5 HIS A 178 O 73.0 78.1 133.1 154.6
REMARK 620 6 HOH A1091 O 77.4 127.5 82.2 80.4 123.6
REMARK 620 7 HOH A1107 O 91.5 74.8 65.7 81.9 80.2 147.7
REMARK 620 8 HOH A1108 O 116.7 66.8 144.3 100.7 82.1 70.0 140.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQH RELATED DB: PDB
REMARK 900 NATIVE PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS
REMARK 900 HALOPLANCTIS
REMARK 900 RELATED ID: 1AQM RELATED DB: PDB
REMARK 900 PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN
REMARK 900 COMPLEX WITH NITRATE
REMARK 900 RELATED ID: 1G94 RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS
REMARK 900 HALOPLANCTIS AND ACARBOSE
REMARK 900 RELATED ID: 1G9H RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS
REMARK 900 HALOPLANCTIS AND COMPONENT II
REMARK 900 RELATED ID: 1JD7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300R OF PSYCHROPHILIC
REMARK 900 ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS
REMARK 900 RELATED ID: 1JD9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300Q OF PSYCHROPHILIC
REMARK 900 ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS
DBREF 1L0P A 1 448 UNP P29957 AMY_ALTHA 25 472
SEQRES 1 A 448 THR PRO THR THR PHE VAL HIS LEU PHE GLU TRP ASN TRP
SEQRES 2 A 448 GLN ASP VAL ALA GLN GLU CYS GLU GLN TYR LEU GLY PRO
SEQRES 3 A 448 LYS GLY TYR ALA ALA VAL GLN VAL SER PRO PRO ASN GLU
SEQRES 4 A 448 HIS ILE THR GLY SER GLN TRP TRP THR ARG TYR GLN PRO
SEQRES 5 A 448 VAL SER TYR GLU LEU GLN SER ARG GLY GLY ASN ARG ALA
SEQRES 6 A 448 GLN PHE ILE ASP MET VAL ASN ARG CYS SER ALA ALA GLY
SEQRES 7 A 448 VAL ASP ILE TYR VAL ASP THR LEU ILE ASN HIS MET ALA
SEQRES 8 A 448 ALA GLY SER GLY THR GLY THR ALA GLY ASN SER PHE GLY
SEQRES 9 A 448 ASN LYS SER PHE PRO ILE TYR SER PRO GLN ASP PHE HIS
SEQRES 10 A 448 GLU SER CYS THR ILE ASN ASN SER ASP TYR GLY ASN ASP
SEQRES 11 A 448 ARG TYR ARG VAL GLN ASN CYS GLU LEU VAL GLY LEU ALA
SEQRES 12 A 448 ASP LEU ASP THR ALA SER ASN TYR VAL GLN ASN THR ILE
SEQRES 13 A 448 ALA ALA TYR ILE ASN ASP LEU GLN ALA ILE GLY VAL LYS
SEQRES 14 A 448 GLY PHE ARG PHE ASP ALA SER LYS HIS VAL ALA ALA SER
SEQRES 15 A 448 ASP ILE GLN SER LEU MET ALA LYS VAL ASN GLY SER PRO
SEQRES 16 A 448 VAL VAL PHE GLN GLU VAL ILE ASP GLN GLY GLY GLU ALA
SEQRES 17 A 448 VAL GLY ALA SER GLU TYR LEU SER THR GLY LEU VAL THR
SEQRES 18 A 448 GLU PHE LYS TYR SER THR GLU LEU GLY ASN THR PHE ARG
SEQRES 19 A 448 ASN GLY SER LEU ALA TRP LEU SER ASN PHE GLY GLU GLY
SEQRES 20 A 448 TRP GLY PHE MET PRO SER SER SER ALA VAL VAL PHE VAL
SEQRES 21 A 448 ASP ASN HIS ASP ASN GLN ARG GLY HIS GLY GLY ALA GLY
SEQRES 22 A 448 ASN VAL ILE THR PHE GLU ASP GLY ARG LEU TYR ASP LEU
SEQRES 23 A 448 ALA ASN VAL PHE MET LEU ALA TYR PRO TYR GLY TYR PRO
SEQRES 24 A 448 LYS VAL MET SER SER TYR ASP PHE HIS GLY ASP THR ASP
SEQRES 25 A 448 ALA GLY GLY PRO ASN VAL PRO VAL HIS ASN ASN GLY ASN
SEQRES 26 A 448 LEU GLU CYS PHE ALA SER ASN TRP LYS CYS GLU HIS ARG
SEQRES 27 A 448 TRP SER TYR ILE ALA GLY GLY VAL ASP PHE ARG ASN ASN
SEQRES 28 A 448 THR ALA ASP ASN TRP ALA VAL THR ASN TRP TRP ASP ASN
SEQRES 29 A 448 THR ASN ASN GLN ILE SER PHE GLY ARG GLY SER SER GLY
SEQRES 30 A 448 HIS MET ALA ILE ASN LYS GLU ASP SER THR LEU THR ALA
SEQRES 31 A 448 THR VAL GLN THR ASP MET ALA SER GLY GLN TYR CYS ASN
SEQRES 32 A 448 VAL LEU LYS GLY GLU LEU SER ALA ASP ALA LYS SER CYS
SEQRES 33 A 448 SER GLY GLU VAL ILE THR VAL ASN SER ASP GLY THR ILE
SEQRES 34 A 448 ASN LEU ASN ILE GLY ALA TRP ASP ALA MET ALA ILE HIS
SEQRES 35 A 448 LYS ASN ALA LYS LEU ASN
HET CA A 800 1
HET NO3 A 901 4
HETNAM CA CALCIUM ION
HETNAM NO3 NITRATE ION
FORMUL 2 CA CA 2+
FORMUL 3 NO3 N O3 1-
FORMUL 4 HOH *217(H2 O)
HELIX 1 1 ASN A 12 TYR A 23 1 12
HELIX 2 2 TYR A 23 GLY A 28 1 6
HELIX 3 3 GLN A 45 GLN A 51 5 7
HELIX 4 4 ASN A 63 ALA A 77 1 15
HELIX 5 5 SER A 112 PHE A 116 5 5
HELIX 6 6 SER A 125 ASP A 130 1 6
HELIX 7 7 ASP A 130 CYS A 137 1 8
HELIX 8 8 SER A 149 GLY A 167 1 19
HELIX 9 9 ALA A 175 VAL A 179 5 5
HELIX 10 10 ALA A 180 ALA A 189 1 10
HELIX 11 11 GLY A 210 LEU A 215 5 6
HELIX 12 12 GLU A 222 GLY A 236 1 15
HELIX 13 13 SER A 237 PHE A 244 5 8
HELIX 14 14 GLY A 245 GLY A 249 5 5
HELIX 15 15 PRO A 252 SER A 254 5 3
HELIX 16 16 ASP A 264 GLY A 268 5 5
HELIX 17 17 THR A 277 ASP A 280 5 4
HELIX 18 18 GLY A 281 TYR A 294 1 14
HELIX 19 19 CYS A 335 ARG A 338 5 4
HELIX 20 20 TRP A 339 THR A 352 1 14
SHEET 1 A 9 PHE A 5 LEU A 8 0
SHEET 2 A 9 ALA A 31 VAL A 34 1 O GLN A 33 N VAL A 6
SHEET 3 A 9 ASP A 80 LEU A 86 1 O TYR A 82 N VAL A 32
SHEET 4 A 9 GLY A 170 ASP A 174 1 O ARG A 172 N THR A 85
SHEET 5 A 9 VAL A 196 GLN A 199 1 O PHE A 198 N PHE A 173
SHEET 6 A 9 LEU A 219 THR A 221 1 O LEU A 219 N GLN A 199
SHEET 7 A 9 ALA A 256 VAL A 258 1 O VAL A 257 N VAL A 220
SHEET 8 A 9 TYR A 298 SER A 303 1 O LYS A 300 N VAL A 258
SHEET 9 A 9 PHE A 5 LEU A 8 1 N PHE A 5 O VAL A 301
SHEET 1 B 2 HIS A 89 MET A 90 0
SHEET 2 B 2 ALA A 143 ASP A 144 -1 O ALA A 143 N MET A 90
SHEET 1 C 2 GLY A 95 THR A 96 0
SHEET 2 C 2 SER A 102 PHE A 103 -1 O PHE A 103 N GLY A 95
SHEET 1 D 2 HIS A 321 ASN A 322 0
SHEET 2 D 2 ASN A 325 LEU A 326 -1 O ASN A 325 N ASN A 322
SHEET 1 E 4 THR A 359 ASP A 363 0
SHEET 2 E 4 GLN A 368 GLY A 372 -1 O GLY A 372 N THR A 359
SHEET 3 E 4 GLY A 377 ASN A 382 -1 O ILE A 381 N ILE A 369
SHEET 4 E 4 ASP A 437 HIS A 442 -1 O ASP A 437 N ASN A 382
SHEET 1 F 2 THR A 391 GLN A 393 0
SHEET 2 F 2 THR A 428 ASN A 430 -1 O ILE A 429 N VAL A 392
SHEET 1 G 2 GLY A 399 CYS A 402 0
SHEET 2 G 2 VAL A 420 VAL A 423 -1 O ILE A 421 N TYR A 401
SSBOND 1 CYS A 20 CYS A 74 1555 1555 2.04
SSBOND 2 CYS A 120 CYS A 137 1555 1555 2.03
SSBOND 3 CYS A 328 CYS A 335 1555 1555 2.04
SSBOND 4 CYS A 402 CYS A 416 1555 1555 2.03
LINK OD1 ASN A 88 CA CA A 800 1555 1555 2.33
LINK O GLN A 135 CA CA A 800 1555 1555 2.63
LINK OD1 ASP A 144 CA CA A 800 1555 1555 2.60
LINK OD2 ASP A 144 CA CA A 800 1555 1555 2.41
LINK O HIS A 178 CA CA A 800 1555 1555 2.42
LINK CA CA A 800 O HOH A1091 1555 1555 2.30
LINK CA CA A 800 O HOH A1107 1555 1555 2.61
LINK CA CA A 800 O HOH A1108 1555 1555 2.46
SITE 1 AC1 7 ASN A 88 GLN A 135 ASP A 144 HIS A 178
SITE 2 AC1 7 HOH A1091 HOH A1107 HOH A1108
SITE 1 AC2 7 ARG A 172 GLU A 200 THR A 221 PHE A 259
SITE 2 AC2 7 ASN A 262 LYS A 300 HOH A1003
CRYST1 71.300 138.400 114.900 90.00 90.00 90.00 C 2 2 21 8
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 0.014025 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008703 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
