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HEADER LIPID BINDING PROTEIN 12-SEP-18 6IDY
TITLE CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS LIPASE B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE AFLB;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEOSARTORYA FUMIGATA;
SOURCE 3 ORGANISM_COMMON: ASPERGILLUS FUMIGATUS;
SOURCE 4 ORGANISM_TAXID: 746128;
SOURCE 5 GENE: CDV57_02421;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS GS115;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 644223
KEYWDS LIPASE, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,D.M.LAN
REVDAT 1 18-SEP-19 6IDY 0
JRNL AUTH Y.H.WANG,D.M.LAN
JRNL TITL CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS LIPASE B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 85809
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 + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 4276
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6304
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1951
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6005
REMARK 3 BIN R VALUE (WORKING SET) : 0.1934
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.74
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 299
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 : 9474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 592
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.77110
REMARK 3 B22 (A**2) : -2.77110
REMARK 3 B33 (A**2) : 5.54230
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) : 0.240
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.179
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.146
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.175
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.145
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9711 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 13274 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3144 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1632 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9711 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1311 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 12479 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.81
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.13
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0887 36.4001 -36.6729
REMARK 3 T TENSOR
REMARK 3 T11: -0.0743 T22: -0.0268
REMARK 3 T33: -0.0645 T12: -0.0295
REMARK 3 T13: -0.0236 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.6759 L22: 0.9496
REMARK 3 L33: 0.7292 L12: 0.1739
REMARK 3 L13: 0.1128 L23: 0.0428
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: -0.0011 S13: 0.0086
REMARK 3 S21: 0.0966 S22: 0.0228 S23: -0.1254
REMARK 3 S31: -0.0270 S32: 0.1292 S33: -0.0251
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4185 33.3866 12.3772
REMARK 3 T TENSOR
REMARK 3 T11: -0.0603 T22: -0.0405
REMARK 3 T33: -0.0788 T12: 0.0038
REMARK 3 T13: -0.0142 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.6372 L22: 0.7638
REMARK 3 L33: 1.0496 L12: -0.0492
REMARK 3 L13: 0.0795 L23: 0.2377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0067 S12: -0.0290 S13: -0.0282
REMARK 3 S21: 0.0334 S22: -0.0204 S23: -0.0344
REMARK 3 S31: 0.0536 S32: -0.0403 S33: 0.0137
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7494 64.9542 -10.6250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0511 T22: -0.1863
REMARK 3 T33: -0.1219 T12: 0.0135
REMARK 3 T13: 0.0111 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 0.7778 L22: 1.8119
REMARK 3 L33: 0.9597 L12: -0.4236
REMARK 3 L13: 0.1457 L23: -0.1374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.0480 S13: 0.1776
REMARK 3 S21: -0.2305 S22: -0.0437 S23: -0.0675
REMARK 3 S31: -0.2839 S32: -0.0003 S33: -0.0141
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1300009025.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97737
REMARK 200 MONOCHROMATOR : MD2
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 47.799
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.14
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 10.86
REMARK 200 R MERGE FOR SHELL (I) : 0.80800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.320
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: 4K6G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIA SULFATE, 0.1 M TRIS.CL,
REMARK 280 PH 6.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 67.14500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 76.09500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 76.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.57250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 76.09500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 76.09500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 100.71750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 76.09500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 76.09500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.57250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 76.09500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 76.09500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 100.71750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.14500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -67.14500
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 1
REMARK 465 VAL A 2
REMARK 465 ILE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 VAL A 8
REMARK 465 PRO A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 ASP A 13
REMARK 465 GLY A 49
REMARK 465 LYS A 50
REMARK 465 THR A 51
REMARK 465 GLU A 52
REMARK 465 PHE A 53
REMARK 465 SER A 54
REMARK 465 ALA B 1
REMARK 465 VAL B 2
REMARK 465 ILE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 GLY B 6
REMARK 465 ALA B 7
REMARK 465 VAL B 8
REMARK 465 PRO B 9
REMARK 465 VAL B 10
REMARK 465 ALA B 11
REMARK 465 SER B 12
REMARK 465 ASP B 13
REMARK 465 SER B 54
REMARK 465 ARG B 55
REMARK 465 SER B 56
REMARK 465 THR B 57
REMARK 465 LYS B 58
REMARK 465 ASP B 59
REMARK 465 ALA B 60
REMARK 465 ALA C 1
REMARK 465 VAL C 2
REMARK 465 ILE C 3
REMARK 465 PRO C 4
REMARK 465 ARG C 5
REMARK 465 GLY C 6
REMARK 465 ALA C 7
REMARK 465 VAL C 8
REMARK 465 PRO C 9
REMARK 465 VAL C 10
REMARK 465 ALA C 11
REMARK 465 SER C 12
REMARK 465 LYS C 50
REMARK 465 THR C 51
REMARK 465 GLU C 52
REMARK 465 PHE C 53
REMARK 465 SER C 54
REMARK 465 ARG C 55
REMARK 465 SER C 56
REMARK 465 THR C 57
REMARK 465 LYS C 58
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 170 7.86 58.66
REMARK 500 ASN A 180 -109.77 -158.30
REMARK 500 SER A 233 -124.72 54.08
REMARK 500 ASP A 262 64.93 -108.78
REMARK 500 TRP A 275 -83.15 69.76
REMARK 500 CYS A 281 -142.13 -130.72
REMARK 500 THR A 348 -60.13 -95.59
REMARK 500 ALA B 170 9.43 59.42
REMARK 500 ASN B 180 -107.29 -159.91
REMARK 500 SER B 233 -127.97 55.14
REMARK 500 ASP B 262 68.46 -108.53
REMARK 500 TRP B 275 -80.86 68.56
REMARK 500 CYS B 281 -140.42 -131.98
REMARK 500 THR B 348 -63.69 -94.30
REMARK 500 ALA C 170 14.36 56.63
REMARK 500 ASN C 180 -110.25 -157.18
REMARK 500 PHE C 181 0.61 -65.18
REMARK 500 SER C 201 19.94 58.08
REMARK 500 ASP C 204 120.83 -38.71
REMARK 500 SER C 233 -125.97 53.19
REMARK 500 ASP C 262 66.45 -106.15
REMARK 500 TRP C 275 -76.39 70.77
REMARK 500 CYS C 281 -134.30 -131.50
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 B 832 DISTANCE = 6.27 ANGSTROMS
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 255 OD1
REMARK 620 2 ASP A 255 OD2 53.2
REMARK 620 3 ALA A 377 O 88.0 83.3
REMARK 620 4 HIS A 380 O 159.5 141.0 81.0
REMARK 620 5 GLY A 382 O 79.0 131.7 103.6 86.8
REMARK 620 6 HOH A 635 O 86.9 83.6 166.5 107.4 87.7
REMARK 620 7 HOH A 658 O 125.9 72.9 90.7 71.8 152.2 82.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 255 OD1
REMARK 620 2 ASP B 255 OD2 53.2
REMARK 620 3 ALA B 377 O 87.1 84.2
REMARK 620 4 HIS B 380 O 159.9 141.1 81.9
REMARK 620 5 GLY B 382 O 79.6 131.6 105.3 87.2
REMARK 620 6 HOH B 711 O 90.7 85.7 168.9 103.2 85.0
REMARK 620 7 HOH B 726 O 122.9 69.8 89.5 74.0 154.3 82.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 255 OD1
REMARK 620 2 ASP C 255 OD2 54.4
REMARK 620 3 ALA C 377 O 82.4 88.4
REMARK 620 4 HIS C 380 O 152.8 143.1 78.6
REMARK 620 5 GLY C 382 O 75.7 127.1 102.5 89.6
REMARK 620 6 HOH C 639 O 92.4 82.7 171.0 108.7 83.2
REMARK 620 7 HOH C 703 O 129.4 75.5 90.8 70.4 153.4 86.9
REMARK 620 N 1 2 3 4 5 6
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 502
DBREF1 6IDY A 1 440 UNP A0A229Y729_ASPFM
DBREF2 6IDY A A0A229Y729 24 463
DBREF1 6IDY B 1 440 UNP A0A229Y729_ASPFM
DBREF2 6IDY B A0A229Y729 24 463
DBREF1 6IDY C 1 440 UNP A0A229Y729_ASPFM
DBREF2 6IDY C A0A229Y729 24 463
SEQRES 1 A 440 ALA VAL ILE PRO ARG GLY ALA VAL PRO VAL ALA SER ASP
SEQRES 2 A 440 LEU SER LEU VAL SER ILE LEU SER SER ALA ALA ASN ASP
SEQRES 3 A 440 SER SER ILE GLU SER GLU ALA ARG SER ILE ALA SER LEU
SEQRES 4 A 440 ILE ALA SER GLU ILE VAL SER LYS ILE GLY LYS THR GLU
SEQRES 5 A 440 PHE SER ARG SER THR LYS ASP ALA LYS SER VAL GLN GLU
SEQRES 6 A 440 ALA PHE ASP LYS ILE GLN SER ILE PHE ALA ASP GLY THR
SEQRES 7 A 440 PRO ASP PHE LEU LYS MET THR ARG GLU ILE LEU THR VAL
SEQRES 8 A 440 GLY LEU ILE PRO ALA ASP ILE LEU SER PHE LEU ASN GLY
SEQRES 9 A 440 TYR LEU ASN LEU ASP LEU ASN SER ILE HIS ASN ARG ASN
SEQRES 10 A 440 PRO SER PRO LYS GLY GLN ALA ILE TYR PRO VAL LYS ALA
SEQRES 11 A 440 PRO GLY ASP ALA ARG TYR SER VAL ALA GLU ASN ALA LEU
SEQRES 12 A 440 ARG ALA ALA ILE HIS ILE PRO ALA SER PHE GLY TYR GLY
SEQRES 13 A 440 LYS ASN GLY LYS LYS PRO VAL ILE LEU VAL PRO GLY THR
SEQRES 14 A 440 ALA THR PRO ALA GLY THR THR TYR TYR PHE ASN PHE GLY
SEQRES 15 A 440 LYS LEU GLY SER ALA ALA ASP ALA ASP VAL VAL TRP LEU
SEQRES 16 A 440 ASN ILE PRO GLN ALA SER LEU ASN ASP VAL GLN ILE ASN
SEQRES 17 A 440 SER GLU TYR VAL ALA TYR ALA ILE ASN TYR ILE SER ALA
SEQRES 18 A 440 ILE SER GLU SER ASN VAL ALA VAL LEU SER TRP SER GLN
SEQRES 19 A 440 GLY GLY LEU ASP THR GLN TRP ALA LEU LYS TYR TRP PRO
SEQRES 20 A 440 SER THR ARG LYS VAL VAL ASP ASP PHE ILE ALA ILE SER
SEQRES 21 A 440 PRO ASP PHE HIS GLY THR VAL MET ARG SER LEU VAL CYS
SEQRES 22 A 440 PRO TRP LEU ALA ALA LEU ALA CYS THR PRO SER LEU TRP
SEQRES 23 A 440 GLN GLN GLY TRP ASN THR GLU PHE ILE ARG THR LEU ARG
SEQRES 24 A 440 GLY GLY GLY GLY ASP SER ALA TYR VAL PRO THR THR THR
SEQRES 25 A 440 ILE TYR SER THR PHE ASP GLU ILE VAL GLN PRO MET SER
SEQRES 26 A 440 GLY SER GLN ALA SER ALA ILE LEU SER ASP SER ARG ALA
SEQRES 27 A 440 VAL GLY VAL SER ASN ASN HIS LEU GLN THR ILE CYS GLY
SEQRES 28 A 440 GLY LYS PRO ALA GLY GLY VAL TYR THR HIS GLU GLY VAL
SEQRES 29 A 440 LEU TYR ASN PRO LEU ALA TRP ALA LEU ALA VAL ASP ALA
SEQRES 30 A 440 LEU SER HIS ASP GLY PRO GLY ASP PRO SER ARG LEU ASP
SEQRES 31 A 440 LEU ASP VAL VAL CYS GLY ARG VAL LEU PRO PRO GLN LEU
SEQRES 32 A 440 GLY LEU ASP ASP LEU LEU GLY THR GLU GLY LEU LEU LEU
SEQRES 33 A 440 ILE ALA LEU ALA GLU VAL LEU ALA TYR LYS PRO LYS THR
SEQRES 34 A 440 PHE GLY GLU PRO ALA ILE ALA SER TYR ALA HIS
SEQRES 1 B 440 ALA VAL ILE PRO ARG GLY ALA VAL PRO VAL ALA SER ASP
SEQRES 2 B 440 LEU SER LEU VAL SER ILE LEU SER SER ALA ALA ASN ASP
SEQRES 3 B 440 SER SER ILE GLU SER GLU ALA ARG SER ILE ALA SER LEU
SEQRES 4 B 440 ILE ALA SER GLU ILE VAL SER LYS ILE GLY LYS THR GLU
SEQRES 5 B 440 PHE SER ARG SER THR LYS ASP ALA LYS SER VAL GLN GLU
SEQRES 6 B 440 ALA PHE ASP LYS ILE GLN SER ILE PHE ALA ASP GLY THR
SEQRES 7 B 440 PRO ASP PHE LEU LYS MET THR ARG GLU ILE LEU THR VAL
SEQRES 8 B 440 GLY LEU ILE PRO ALA ASP ILE LEU SER PHE LEU ASN GLY
SEQRES 9 B 440 TYR LEU ASN LEU ASP LEU ASN SER ILE HIS ASN ARG ASN
SEQRES 10 B 440 PRO SER PRO LYS GLY GLN ALA ILE TYR PRO VAL LYS ALA
SEQRES 11 B 440 PRO GLY ASP ALA ARG TYR SER VAL ALA GLU ASN ALA LEU
SEQRES 12 B 440 ARG ALA ALA ILE HIS ILE PRO ALA SER PHE GLY TYR GLY
SEQRES 13 B 440 LYS ASN GLY LYS LYS PRO VAL ILE LEU VAL PRO GLY THR
SEQRES 14 B 440 ALA THR PRO ALA GLY THR THR TYR TYR PHE ASN PHE GLY
SEQRES 15 B 440 LYS LEU GLY SER ALA ALA ASP ALA ASP VAL VAL TRP LEU
SEQRES 16 B 440 ASN ILE PRO GLN ALA SER LEU ASN ASP VAL GLN ILE ASN
SEQRES 17 B 440 SER GLU TYR VAL ALA TYR ALA ILE ASN TYR ILE SER ALA
SEQRES 18 B 440 ILE SER GLU SER ASN VAL ALA VAL LEU SER TRP SER GLN
SEQRES 19 B 440 GLY GLY LEU ASP THR GLN TRP ALA LEU LYS TYR TRP PRO
SEQRES 20 B 440 SER THR ARG LYS VAL VAL ASP ASP PHE ILE ALA ILE SER
SEQRES 21 B 440 PRO ASP PHE HIS GLY THR VAL MET ARG SER LEU VAL CYS
SEQRES 22 B 440 PRO TRP LEU ALA ALA LEU ALA CYS THR PRO SER LEU TRP
SEQRES 23 B 440 GLN GLN GLY TRP ASN THR GLU PHE ILE ARG THR LEU ARG
SEQRES 24 B 440 GLY GLY GLY GLY ASP SER ALA TYR VAL PRO THR THR THR
SEQRES 25 B 440 ILE TYR SER THR PHE ASP GLU ILE VAL GLN PRO MET SER
SEQRES 26 B 440 GLY SER GLN ALA SER ALA ILE LEU SER ASP SER ARG ALA
SEQRES 27 B 440 VAL GLY VAL SER ASN ASN HIS LEU GLN THR ILE CYS GLY
SEQRES 28 B 440 GLY LYS PRO ALA GLY GLY VAL TYR THR HIS GLU GLY VAL
SEQRES 29 B 440 LEU TYR ASN PRO LEU ALA TRP ALA LEU ALA VAL ASP ALA
SEQRES 30 B 440 LEU SER HIS ASP GLY PRO GLY ASP PRO SER ARG LEU ASP
SEQRES 31 B 440 LEU ASP VAL VAL CYS GLY ARG VAL LEU PRO PRO GLN LEU
SEQRES 32 B 440 GLY LEU ASP ASP LEU LEU GLY THR GLU GLY LEU LEU LEU
SEQRES 33 B 440 ILE ALA LEU ALA GLU VAL LEU ALA TYR LYS PRO LYS THR
SEQRES 34 B 440 PHE GLY GLU PRO ALA ILE ALA SER TYR ALA HIS
SEQRES 1 C 440 ALA VAL ILE PRO ARG GLY ALA VAL PRO VAL ALA SER ASP
SEQRES 2 C 440 LEU SER LEU VAL SER ILE LEU SER SER ALA ALA ASN ASP
SEQRES 3 C 440 SER SER ILE GLU SER GLU ALA ARG SER ILE ALA SER LEU
SEQRES 4 C 440 ILE ALA SER GLU ILE VAL SER LYS ILE GLY LYS THR GLU
SEQRES 5 C 440 PHE SER ARG SER THR LYS ASP ALA LYS SER VAL GLN GLU
SEQRES 6 C 440 ALA PHE ASP LYS ILE GLN SER ILE PHE ALA ASP GLY THR
SEQRES 7 C 440 PRO ASP PHE LEU LYS MET THR ARG GLU ILE LEU THR VAL
SEQRES 8 C 440 GLY LEU ILE PRO ALA ASP ILE LEU SER PHE LEU ASN GLY
SEQRES 9 C 440 TYR LEU ASN LEU ASP LEU ASN SER ILE HIS ASN ARG ASN
SEQRES 10 C 440 PRO SER PRO LYS GLY GLN ALA ILE TYR PRO VAL LYS ALA
SEQRES 11 C 440 PRO GLY ASP ALA ARG TYR SER VAL ALA GLU ASN ALA LEU
SEQRES 12 C 440 ARG ALA ALA ILE HIS ILE PRO ALA SER PHE GLY TYR GLY
SEQRES 13 C 440 LYS ASN GLY LYS LYS PRO VAL ILE LEU VAL PRO GLY THR
SEQRES 14 C 440 ALA THR PRO ALA GLY THR THR TYR TYR PHE ASN PHE GLY
SEQRES 15 C 440 LYS LEU GLY SER ALA ALA ASP ALA ASP VAL VAL TRP LEU
SEQRES 16 C 440 ASN ILE PRO GLN ALA SER LEU ASN ASP VAL GLN ILE ASN
SEQRES 17 C 440 SER GLU TYR VAL ALA TYR ALA ILE ASN TYR ILE SER ALA
SEQRES 18 C 440 ILE SER GLU SER ASN VAL ALA VAL LEU SER TRP SER GLN
SEQRES 19 C 440 GLY GLY LEU ASP THR GLN TRP ALA LEU LYS TYR TRP PRO
SEQRES 20 C 440 SER THR ARG LYS VAL VAL ASP ASP PHE ILE ALA ILE SER
SEQRES 21 C 440 PRO ASP PHE HIS GLY THR VAL MET ARG SER LEU VAL CYS
SEQRES 22 C 440 PRO TRP LEU ALA ALA LEU ALA CYS THR PRO SER LEU TRP
SEQRES 23 C 440 GLN GLN GLY TRP ASN THR GLU PHE ILE ARG THR LEU ARG
SEQRES 24 C 440 GLY GLY GLY GLY ASP SER ALA TYR VAL PRO THR THR THR
SEQRES 25 C 440 ILE TYR SER THR PHE ASP GLU ILE VAL GLN PRO MET SER
SEQRES 26 C 440 GLY SER GLN ALA SER ALA ILE LEU SER ASP SER ARG ALA
SEQRES 27 C 440 VAL GLY VAL SER ASN ASN HIS LEU GLN THR ILE CYS GLY
SEQRES 28 C 440 GLY LYS PRO ALA GLY GLY VAL TYR THR HIS GLU GLY VAL
SEQRES 29 C 440 LEU TYR ASN PRO LEU ALA TRP ALA LEU ALA VAL ASP ALA
SEQRES 30 C 440 LEU SER HIS ASP GLY PRO GLY ASP PRO SER ARG LEU ASP
SEQRES 31 C 440 LEU ASP VAL VAL CYS GLY ARG VAL LEU PRO PRO GLN LEU
SEQRES 32 C 440 GLY LEU ASP ASP LEU LEU GLY THR GLU GLY LEU LEU LEU
SEQRES 33 C 440 ILE ALA LEU ALA GLU VAL LEU ALA TYR LYS PRO LYS THR
SEQRES 34 C 440 PHE GLY GLU PRO ALA ILE ALA SER TYR ALA HIS
HET CA A 501 1
HET SO4 A 502 5
HET CA B 501 1
HET CA C 501 1
HET SO4 C 502 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 4 CA 3(CA 2+)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 HOH *592(H2 O)
HELIX 1 AA1 SER A 15 ASN A 25 1 11
HELIX 2 AA2 GLU A 30 ILE A 48 1 19
HELIX 3 AA3 SER A 62 PHE A 74 1 13
HELIX 4 AA4 ALA A 75 GLY A 77 5 3
HELIX 5 AA5 ASP A 80 VAL A 91 1 12
HELIX 6 AA6 PRO A 95 GLY A 104 1 10
HELIX 7 AA7 LEU A 108 SER A 112 5 5
HELIX 8 AA8 ALA A 139 ALA A 146 1 8
HELIX 9 AA9 PRO A 172 PHE A 179 1 8
HELIX 10 AB1 ASN A 180 ALA A 187 5 8
HELIX 11 AB2 ILE A 197 LEU A 202 5 6
HELIX 12 AB3 ASP A 204 GLU A 224 1 21
HELIX 13 AB4 GLN A 234 TRP A 246 1 13
HELIX 14 AB5 PRO A 247 LYS A 251 5 5
HELIX 15 AB6 THR A 282 GLN A 288 1 7
HELIX 16 AB7 THR A 292 GLY A 300 1 9
HELIX 17 AB8 GLY A 301 GLY A 303 5 3
HELIX 18 AB9 LEU A 346 CYS A 350 1 5
HELIX 19 AC1 LYS A 353 GLY A 357 5 5
HELIX 20 AC2 GLU A 362 TYR A 366 5 5
HELIX 21 AC3 ASN A 367 HIS A 380 1 14
HELIX 22 AC4 ASP A 385 LEU A 389 5 5
HELIX 23 AC5 ASP A 390 ARG A 397 1 8
HELIX 24 AC6 GLY A 404 GLY A 413 1 10
HELIX 25 AC7 GLY A 413 TYR A 425 1 13
HELIX 26 AC8 ALA A 436 HIS A 440 5 5
HELIX 27 AC9 SER B 15 ASN B 25 1 11
HELIX 28 AD1 GLU B 30 LYS B 50 1 21
HELIX 29 AD2 SER B 62 PHE B 74 1 13
HELIX 30 AD3 ASP B 80 VAL B 91 1 12
HELIX 31 AD4 PRO B 95 GLY B 104 1 10
HELIX 32 AD5 TYR B 105 SER B 112 5 8
HELIX 33 AD6 ALA B 139 ALA B 146 1 8
HELIX 34 AD7 PRO B 172 PHE B 179 1 8
HELIX 35 AD8 ASN B 180 ALA B 187 5 8
HELIX 36 AD9 ILE B 197 LEU B 202 5 6
HELIX 37 AE1 ASP B 204 GLU B 224 1 21
HELIX 38 AE2 GLN B 234 TRP B 246 1 13
HELIX 39 AE3 PRO B 247 LYS B 251 5 5
HELIX 40 AE4 THR B 282 GLN B 288 1 7
HELIX 41 AE5 THR B 292 GLY B 300 1 9
HELIX 42 AE6 LEU B 346 CYS B 350 1 5
HELIX 43 AE7 LYS B 353 GLY B 357 5 5
HELIX 44 AE8 GLU B 362 TYR B 366 5 5
HELIX 45 AE9 ASN B 367 HIS B 380 1 14
HELIX 46 AF1 ASP B 385 LEU B 389 5 5
HELIX 47 AF2 ASP B 390 ARG B 397 1 8
HELIX 48 AF3 GLY B 404 TYR B 425 1 22
HELIX 49 AF4 SER C 15 ASN C 25 1 11
HELIX 50 AF5 GLU C 30 GLY C 49 1 20
HELIX 51 AF6 SER C 62 ALA C 75 1 14
HELIX 52 AF7 ASP C 80 VAL C 91 1 12
HELIX 53 AF8 PRO C 95 GLY C 104 1 10
HELIX 54 AF9 TYR C 105 SER C 112 5 8
HELIX 55 AG1 ALA C 139 ALA C 146 1 8
HELIX 56 AG2 PRO C 172 TYR C 178 1 7
HELIX 57 AG3 ASN C 180 ALA C 187 5 8
HELIX 58 AG4 ASP C 204 GLU C 224 1 21
HELIX 59 AG5 GLN C 234 TRP C 246 1 13
HELIX 60 AG6 PRO C 247 LYS C 251 5 5
HELIX 61 AG7 THR C 282 GLN C 288 1 7
HELIX 62 AG8 THR C 292 GLY C 300 1 9
HELIX 63 AG9 GLY C 301 GLY C 303 5 3
HELIX 64 AH1 LEU C 346 CYS C 350 1 5
HELIX 65 AH2 LYS C 353 GLY C 357 5 5
HELIX 66 AH3 GLU C 362 TYR C 366 5 5
HELIX 67 AH4 ASN C 367 HIS C 380 1 14
HELIX 68 AH5 ASP C 385 LEU C 389 5 5
HELIX 69 AH6 ASP C 390 ARG C 397 1 8
HELIX 70 AH7 GLY C 404 GLY C 413 1 10
HELIX 71 AH8 GLY C 413 TYR C 425 1 13
SHEET 1 AA1 7 ILE A 147 HIS A 148 0
SHEET 2 AA1 7 ALA A 190 LEU A 195 -1 O TRP A 194 N HIS A 148
SHEET 3 AA1 7 LYS A 161 VAL A 166 1 N LEU A 165 O VAL A 193
SHEET 4 AA1 7 VAL A 227 TRP A 232 1 O LEU A 230 N ILE A 164
SHEET 5 AA1 7 VAL A 253 ILE A 259 1 O ILE A 257 N VAL A 229
SHEET 6 AA1 7 THR A 310 TYR A 314 1 O THR A 311 N ALA A 258
SHEET 7 AA1 7 VAL A 341 HIS A 345 1 O ASN A 344 N THR A 312
SHEET 1 AA2 7 ILE B 147 HIS B 148 0
SHEET 2 AA2 7 ALA B 190 LEU B 195 -1 O TRP B 194 N HIS B 148
SHEET 3 AA2 7 LYS B 161 VAL B 166 1 N LEU B 165 O VAL B 193
SHEET 4 AA2 7 VAL B 227 TRP B 232 1 O ALA B 228 N ILE B 164
SHEET 5 AA2 7 VAL B 253 ILE B 259 1 O ILE B 257 N VAL B 229
SHEET 6 AA2 7 THR B 310 TYR B 314 1 O THR B 311 N PHE B 256
SHEET 7 AA2 7 VAL B 341 HIS B 345 1 O SER B 342 N THR B 312
SHEET 1 AA3 7 ILE C 147 HIS C 148 0
SHEET 2 AA3 7 ALA C 190 LEU C 195 -1 O TRP C 194 N HIS C 148
SHEET 3 AA3 7 LYS C 161 VAL C 166 1 N LEU C 165 O VAL C 193
SHEET 4 AA3 7 VAL C 227 TRP C 232 1 O ALA C 228 N PRO C 162
SHEET 5 AA3 7 VAL C 253 ILE C 259 1 O ILE C 257 N VAL C 229
SHEET 6 AA3 7 THR C 310 TYR C 314 1 O THR C 311 N ALA C 258
SHEET 7 AA3 7 VAL C 341 HIS C 345 1 O ASN C 344 N THR C 312
SSBOND 1 CYS A 273 CYS A 281 1555 1555 2.03
SSBOND 2 CYS A 350 CYS A 395 1555 1555 2.04
SSBOND 3 CYS B 273 CYS B 281 1555 1555 2.03
SSBOND 4 CYS B 350 CYS B 395 1555 1555 2.04
SSBOND 5 CYS C 273 CYS C 281 1555 1555 2.03
SSBOND 6 CYS C 350 CYS C 395 1555 1555 2.04
LINK OD1 ASP A 255 CA CA A 501 1555 1555 2.45
LINK OD2 ASP A 255 CA CA A 501 1555 1555 2.46
LINK O ALA A 377 CA CA A 501 1555 1555 2.22
LINK O HIS A 380 CA CA A 501 1555 1555 2.29
LINK O GLY A 382 CA CA A 501 1555 1555 2.39
LINK OD1 ASP B 255 CA CA B 501 1555 1555 2.42
LINK OD2 ASP B 255 CA CA B 501 1555 1555 2.50
LINK O ALA B 377 CA CA B 501 1555 1555 2.20
LINK O HIS B 380 CA CA B 501 1555 1555 2.28
LINK O GLY B 382 CA CA B 501 1555 1555 2.39
LINK OD1 ASP C 255 CA CA C 501 1555 1555 2.44
LINK OD2 ASP C 255 CA CA C 501 1555 1555 2.36
LINK O ALA C 377 CA CA C 501 1555 1555 2.15
LINK O HIS C 380 CA CA C 501 1555 1555 2.45
LINK O GLY C 382 CA CA C 501 1555 1555 2.46
LINK CA CA A 501 O HOH A 635 1555 1555 2.40
LINK CA CA A 501 O HOH A 658 1555 1555 2.35
LINK CA CA B 501 O HOH B 711 1555 1555 2.39
LINK CA CA B 501 O HOH B 726 1555 1555 2.42
LINK CA CA C 501 O HOH C 639 1555 1555 2.34
LINK CA CA C 501 O HOH C 703 1555 1555 2.58
CISPEP 1 TYR A 126 PRO A 127 0 1.48
CISPEP 2 GLN A 322 PRO A 323 0 -1.50
CISPEP 3 LYS A 426 PRO A 427 0 -1.25
CISPEP 4 TYR B 126 PRO B 127 0 0.73
CISPEP 5 GLN B 322 PRO B 323 0 -0.50
CISPEP 6 LYS B 426 PRO B 427 0 -5.53
CISPEP 7 TYR C 126 PRO C 127 0 -0.06
CISPEP 8 GLN C 322 PRO C 323 0 -0.82
CISPEP 9 LYS C 426 PRO C 427 0 -1.58
SITE 1 AC1 6 ASP A 255 ALA A 377 HIS A 380 GLY A 382
SITE 2 AC1 6 HOH A 635 HOH A 658
SITE 1 AC2 8 ARG A 250 ARG A 337 HOH A 625 HOH A 757
SITE 2 AC2 8 THR B 429 PHE B 430 GLY B 431 HOH B 678
SITE 1 AC3 6 ASP B 255 ALA B 377 HIS B 380 GLY B 382
SITE 2 AC3 6 HOH B 711 HOH B 726
SITE 1 AC4 6 ASP C 255 ALA C 377 HIS C 380 GLY C 382
SITE 2 AC4 6 HOH C 639 HOH C 703
SITE 1 AC5 7 THR A 429 PHE A 430 GLY A 431 HOH A 649
SITE 2 AC5 7 ARG C 250 ARG C 337 HOH C 633
CRYST1 152.190 152.190 134.290 90.00 90.00 90.00 P 41 21 2 24
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 0.006571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007447 0.00000
TER 3168 HIS A 440
TER 6330 HIS B 440
TER 9477 HIS C 440
MASTER 465 0 5 71 21 0 10 610079 3 49 102
END |