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HEADER HYDROLASE 18-JUN-14 4QNN
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE A 1 FROM HORNET(VESPA BASALIS)
TITLE 2 VENOM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A 1 FROM HORNET(VESPA BASALIS) VENOM;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VESPA BASALIS;
SOURCE 3 ORGANISM_TAXID: 7444;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA / BATA HYDROLASE FAMILY FOLD, PHOSPHOLIPASE A1, PHOSPHOLIPID,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.CHUANG,T.P.KO,A.H.J.WANG,M.H.HOU
REVDAT 1 24-JUN-15 4QNN 0
JRNL AUTH C.Y.CHUANG,T.P.KO,A.H.J.WANG,M.H.HOU
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHOLIPASE A 1 FROM HORNET(VESPA
JRNL TITL 2 BASALIS) VENOM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35409
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) : 0.204
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1936
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 : 9168
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 477
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) : NULL
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) : 1.270 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.166 ; 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 4QNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-14.
REMARK 100 THE RCSB ID CODE IS RCSB086282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-04
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL17B2
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 : WATER-COOLED, FIXED-EXIT DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : SCINTILLATION COUNTER
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35849
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M
REMARK 280 TRIS HCL PH 8.0, 25% PEG4000 500ML PRECIPITATION, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -341.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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 PHE A 1
REMARK 465 ASN A 2
REMARK 465 ILE A 300
REMARK 465 PHE B 1
REMARK 465 ASN B 2
REMARK 465 ILE B 300
REMARK 465 PHE C 1
REMARK 465 ASN C 2
REMARK 465 ILE C 300
REMARK 465 PHE D 1
REMARK 465 ASN D 2
REMARK 465 ILE D 300
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 242 CB CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 242 CB CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 242 CB CG ND1 CD2 CE1 NE2
REMARK 470 HIS D 242 CB CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASN A 211 O HOH A 525 2.00
REMARK 500 O ASN A 295 O HOH A 576 2.02
REMARK 500 NZ LYS A 241 O HOH A 513 2.07
REMARK 500 O PRO A 221 O HOH A 540 2.09
REMARK 500 NE2 HIS D 196 O HOH D 623 2.12
REMARK 500 NE2 HIS A 196 O HOH A 501 2.13
REMARK 500 O ASN D 211 O HOH D 563 2.17
REMARK 500 O HOH D 596 O HOH D 626 2.17
REMARK 500 OH TYR A 101 O HOH A 555 2.18
REMARK 500 CL CL B 402 O HOH A 577 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 5 C - N - CA ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO B 5 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 CYS B 87 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO C 5 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 CYS C 227 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 PRO D 5 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 PRO D 221 C - N - CA ANGL. DEV. = 9.1 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 SER A 7 137.72 -170.48
REMARK 500 GLU A 19 50.44 -105.37
REMARK 500 ASN A 20 66.75 -176.59
REMARK 500 LYS A 22 109.91 -53.43
REMARK 500 PHE A 53 131.26 -37.76
REMARK 500 ASP A 58 38.42 -92.86
REMARK 500 ASN A 74 54.85 -100.91
REMARK 500 GLU A 90 -2.55 -160.82
REMARK 500 MET A 91 87.31 -21.95
REMARK 500 ILE A 94 87.74 -49.21
REMARK 500 SER A 137 -112.42 39.27
REMARK 500 ASP A 165 63.67 39.20
REMARK 500 SER A 170 7.36 80.60
REMARK 500 PHE A 171 -40.23 -142.12
REMARK 500 LYS A 172 -53.13 -26.80
REMARK 500 ASN A 211 -52.87 104.24
REMARK 500 PRO A 221 -41.96 -29.58
REMARK 500 ARG A 263 -6.92 -55.04
REMARK 500 TYR A 292 -19.95 62.23
REMARK 500 CYS A 293 137.19 -30.53
REMARK 500 SER B 7 140.82 -176.86
REMARK 500 ASN B 20 69.39 -171.67
REMARK 500 HIS B 23 48.22 -75.50
REMARK 500 THR B 30 5.03 -62.12
REMARK 500 ASP B 58 41.64 -92.00
REMARK 500 GLU B 89 42.80 -83.74
REMARK 500 GLU B 90 13.35 175.50
REMARK 500 MET B 91 79.56 -44.93
REMARK 500 SER B 92 73.01 -117.87
REMARK 500 ILE B 94 75.14 -27.38
REMARK 500 SER B 137 -111.03 48.07
REMARK 500 ASP B 165 68.43 36.43
REMARK 500 SER B 170 1.90 86.53
REMARK 500 PHE B 171 -35.76 -137.06
REMARK 500 LYS B 172 -63.67 -27.91
REMARK 500 THR B 193 -34.00 -133.62
REMARK 500 ASN B 211 -58.44 105.69
REMARK 500 PRO B 221 -50.37 -18.01
REMARK 500 ARG B 263 0.51 -69.24
REMARK 500 TYR B 292 -14.86 61.27
REMARK 500 CYS B 293 141.45 -36.98
REMARK 500 ASN B 295 147.93 176.10
REMARK 500 ASN C 20 77.71 -158.81
REMARK 500 ASP C 29 -73.60 -89.72
REMARK 500 THR C 30 -0.18 -58.30
REMARK 500 SER C 55 -168.33 -127.30
REMARK 500 ASP C 58 49.75 -82.85
REMARK 500 ASN C 74 45.18 -96.18
REMARK 500 GLU C 89 35.85 -70.12
REMARK 500 GLU C 90 31.04 177.02
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 6 0.07 SIDE CHAIN
REMARK 500 TYR B 283 0.08 SIDE CHAIN
REMARK 500 TYR C 6 0.07 SIDE CHAIN
REMARK 500 TYR D 6 0.07 SIDE CHAIN
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 A 554 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH A 558 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH A 567 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 568 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A 569 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 570 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH A 609 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH B 514 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH B 517 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH B 519 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH B 538 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH B 539 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH B 542 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH B 551 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B 554 DISTANCE = 8.52 ANGSTROMS
REMARK 525 HOH B 557 DISTANCE = 8.89 ANGSTROMS
REMARK 525 HOH B 559 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH B 560 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH B 600 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH B 607 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH C 601 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH C 618 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH C 628 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH C 666 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH C 670 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH C 677 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH C 680 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH C 681 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 685 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH C 696 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH C 709 DISTANCE = 9.21 ANGSTROMS
REMARK 525 HOH C 715 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH C 717 DISTANCE = 11.38 ANGSTROMS
REMARK 525 HOH D 544 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH D 547 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH D 548 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH D 554 DISTANCE = 9.73 ANGSTROMS
REMARK 525 HOH D 561 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH D 568 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH D 579 DISTANCE = 5.78 ANGSTROMS
REMARK 525 HOH D 580 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH D 601 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH D 613 DISTANCE = 6.19 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 403
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT
REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION.
DBREF 4QNN A 1 300 PDB 4QNN 4QNN 1 300
DBREF 4QNN B 1 300 PDB 4QNN 4QNN 1 300
DBREF 4QNN C 1 300 PDB 4QNN 4QNN 1 300
DBREF 4QNN D 1 300 PDB 4QNN 4QNN 1 300
SEQRES 1 A 300 PHE ASN PRO CYS PRO TYR SER ASP ASP THR VAL LYS MET
SEQRES 2 A 300 ILE ILE LEU THR ARG GLU ASN LYS LYS HIS ASP PHE TYR
SEQRES 3 A 300 THR LEU ASP THR ILE LYS LYS HIS ASN GLU PHE LYS LYS
SEQRES 4 A 300 SER THR ILE LYS HIS GLN VAL VAL PHE ILE THR HIS GLY
SEQRES 5 A 300 PHE THR SER SER ALA ASP THR GLU ASN PHE LEU ALA MET
SEQRES 6 A 300 ALA LYS ALA LEU SER ASP LYS GLY ASN TYR LEU VAL ILE
SEQRES 7 A 300 LEU ILE ASP TRP ARG VAL ALA ALA CYS THR GLU GLU MET
SEQRES 8 A 300 SER GLY ILE GLN LEU ALA TYR TYR SER TYR ALA ALA SER
SEQRES 9 A 300 ASN THR ARG LEU VAL GLY ASN TYR ILE ALA THR VAL THR
SEQRES 10 A 300 LYS MET LEU VAL GLN LYS TYR ASN VAL PRO MET ALA ASN
SEQRES 11 A 300 ILE ARG LEU ILE GLY HIS SER LEU GLY ALA HIS THR SER
SEQRES 12 A 300 GLY PHE ALA GLY LYS LYS VAL GLN GLU LEU GLY LEU GLY
SEQRES 13 A 300 LYS TYR SER GLU ILE ILE GLY LEU ASP PRO ALA GLY PRO
SEQRES 14 A 300 SER PHE LYS SER ASN ASP CYS SER GLU ARG ILE CYS LYS
SEQRES 15 A 300 THR ASP ALA HIS TYR VAL GLN ILE ILE HIS THR SER ASN
SEQRES 16 A 300 HIS LEU GLY THR LEU VAL THR LEU GLY THR VAL ASP PHE
SEQRES 17 A 300 MET ASN ASN GLY TYR ASN GLN PRO GLY CYS GLY LEU PRO
SEQRES 18 A 300 LEU ILE GLY GLU THR CYS SER HIS THR ARG ALA VAL LYS
SEQRES 19 A 300 TYR PHE THR GLU CYS ILE LYS HIS GLU CYS CYS LEU ILE
SEQRES 20 A 300 GLY VAL PRO GLN SER LYS LYS PRO GLN PRO VAL SER LYS
SEQRES 21 A 300 CYS THR ARG ASN GLU CYS VAL CYS VAL GLY LEU ASN ALA
SEQRES 22 A 300 LYS THR TYR PRO LYS THR GLY SER PHE TYR VAL PRO VAL
SEQRES 23 A 300 GLU SER LYS ALA PRO TYR CYS ASN ASN LYS GLY LYS ILE
SEQRES 24 A 300 ILE
SEQRES 1 B 300 PHE ASN PRO CYS PRO TYR SER ASP ASP THR VAL LYS MET
SEQRES 2 B 300 ILE ILE LEU THR ARG GLU ASN LYS LYS HIS ASP PHE TYR
SEQRES 3 B 300 THR LEU ASP THR ILE LYS LYS HIS ASN GLU PHE LYS LYS
SEQRES 4 B 300 SER THR ILE LYS HIS GLN VAL VAL PHE ILE THR HIS GLY
SEQRES 5 B 300 PHE THR SER SER ALA ASP THR GLU ASN PHE LEU ALA MET
SEQRES 6 B 300 ALA LYS ALA LEU SER ASP LYS GLY ASN TYR LEU VAL ILE
SEQRES 7 B 300 LEU ILE ASP TRP ARG VAL ALA ALA CYS THR GLU GLU MET
SEQRES 8 B 300 SER GLY ILE GLN LEU ALA TYR TYR SER TYR ALA ALA SER
SEQRES 9 B 300 ASN THR ARG LEU VAL GLY ASN TYR ILE ALA THR VAL THR
SEQRES 10 B 300 LYS MET LEU VAL GLN LYS TYR ASN VAL PRO MET ALA ASN
SEQRES 11 B 300 ILE ARG LEU ILE GLY HIS SER LEU GLY ALA HIS THR SER
SEQRES 12 B 300 GLY PHE ALA GLY LYS LYS VAL GLN GLU LEU GLY LEU GLY
SEQRES 13 B 300 LYS TYR SER GLU ILE ILE GLY LEU ASP PRO ALA GLY PRO
SEQRES 14 B 300 SER PHE LYS SER ASN ASP CYS SER GLU ARG ILE CYS LYS
SEQRES 15 B 300 THR ASP ALA HIS TYR VAL GLN ILE ILE HIS THR SER ASN
SEQRES 16 B 300 HIS LEU GLY THR LEU VAL THR LEU GLY THR VAL ASP PHE
SEQRES 17 B 300 MET ASN ASN GLY TYR ASN GLN PRO GLY CYS GLY LEU PRO
SEQRES 18 B 300 LEU ILE GLY GLU THR CYS SER HIS THR ARG ALA VAL LYS
SEQRES 19 B 300 TYR PHE THR GLU CYS ILE LYS HIS GLU CYS CYS LEU ILE
SEQRES 20 B 300 GLY VAL PRO GLN SER LYS LYS PRO GLN PRO VAL SER LYS
SEQRES 21 B 300 CYS THR ARG ASN GLU CYS VAL CYS VAL GLY LEU ASN ALA
SEQRES 22 B 300 LYS THR TYR PRO LYS THR GLY SER PHE TYR VAL PRO VAL
SEQRES 23 B 300 GLU SER LYS ALA PRO TYR CYS ASN ASN LYS GLY LYS ILE
SEQRES 24 B 300 ILE
SEQRES 1 C 300 PHE ASN PRO CYS PRO TYR SER ASP ASP THR VAL LYS MET
SEQRES 2 C 300 ILE ILE LEU THR ARG GLU ASN LYS LYS HIS ASP PHE TYR
SEQRES 3 C 300 THR LEU ASP THR ILE LYS LYS HIS ASN GLU PHE LYS LYS
SEQRES 4 C 300 SER THR ILE LYS HIS GLN VAL VAL PHE ILE THR HIS GLY
SEQRES 5 C 300 PHE THR SER SER ALA ASP THR GLU ASN PHE LEU ALA MET
SEQRES 6 C 300 ALA LYS ALA LEU SER ASP LYS GLY ASN TYR LEU VAL ILE
SEQRES 7 C 300 LEU ILE ASP TRP ARG VAL ALA ALA CYS THR GLU GLU MET
SEQRES 8 C 300 SER GLY ILE GLN LEU ALA TYR TYR SER TYR ALA ALA SER
SEQRES 9 C 300 ASN THR ARG LEU VAL GLY ASN TYR ILE ALA THR VAL THR
SEQRES 10 C 300 LYS MET LEU VAL GLN LYS TYR ASN VAL PRO MET ALA ASN
SEQRES 11 C 300 ILE ARG LEU ILE GLY HIS SER LEU GLY ALA HIS THR SER
SEQRES 12 C 300 GLY PHE ALA GLY LYS LYS VAL GLN GLU LEU GLY LEU GLY
SEQRES 13 C 300 LYS TYR SER GLU ILE ILE GLY LEU ASP PRO ALA GLY PRO
SEQRES 14 C 300 SER PHE LYS SER ASN ASP CYS SER GLU ARG ILE CYS LYS
SEQRES 15 C 300 THR ASP ALA HIS TYR VAL GLN ILE ILE HIS THR SER ASN
SEQRES 16 C 300 HIS LEU GLY THR LEU VAL THR LEU GLY THR VAL ASP PHE
SEQRES 17 C 300 MET ASN ASN GLY TYR ASN GLN PRO GLY CYS GLY LEU PRO
SEQRES 18 C 300 LEU ILE GLY GLU THR CYS SER HIS THR ARG ALA VAL LYS
SEQRES 19 C 300 TYR PHE THR GLU CYS ILE LYS HIS GLU CYS CYS LEU ILE
SEQRES 20 C 300 GLY VAL PRO GLN SER LYS LYS PRO GLN PRO VAL SER LYS
SEQRES 21 C 300 CYS THR ARG ASN GLU CYS VAL CYS VAL GLY LEU ASN ALA
SEQRES 22 C 300 LYS THR TYR PRO LYS THR GLY SER PHE TYR VAL PRO VAL
SEQRES 23 C 300 GLU SER LYS ALA PRO TYR CYS ASN ASN LYS GLY LYS ILE
SEQRES 24 C 300 ILE
SEQRES 1 D 300 PHE ASN PRO CYS PRO TYR SER ASP ASP THR VAL LYS MET
SEQRES 2 D 300 ILE ILE LEU THR ARG GLU ASN LYS LYS HIS ASP PHE TYR
SEQRES 3 D 300 THR LEU ASP THR ILE LYS LYS HIS ASN GLU PHE LYS LYS
SEQRES 4 D 300 SER THR ILE LYS HIS GLN VAL VAL PHE ILE THR HIS GLY
SEQRES 5 D 300 PHE THR SER SER ALA ASP THR GLU ASN PHE LEU ALA MET
SEQRES 6 D 300 ALA LYS ALA LEU SER ASP LYS GLY ASN TYR LEU VAL ILE
SEQRES 7 D 300 LEU ILE ASP TRP ARG VAL ALA ALA CYS THR GLU GLU MET
SEQRES 8 D 300 SER GLY ILE GLN LEU ALA TYR TYR SER TYR ALA ALA SER
SEQRES 9 D 300 ASN THR ARG LEU VAL GLY ASN TYR ILE ALA THR VAL THR
SEQRES 10 D 300 LYS MET LEU VAL GLN LYS TYR ASN VAL PRO MET ALA ASN
SEQRES 11 D 300 ILE ARG LEU ILE GLY HIS SER LEU GLY ALA HIS THR SER
SEQRES 12 D 300 GLY PHE ALA GLY LYS LYS VAL GLN GLU LEU GLY LEU GLY
SEQRES 13 D 300 LYS TYR SER GLU ILE ILE GLY LEU ASP PRO ALA GLY PRO
SEQRES 14 D 300 SER PHE LYS SER ASN ASP CYS SER GLU ARG ILE CYS LYS
SEQRES 15 D 300 THR ASP ALA HIS TYR VAL GLN ILE ILE HIS THR SER ASN
SEQRES 16 D 300 HIS LEU GLY THR LEU VAL THR LEU GLY THR VAL ASP PHE
SEQRES 17 D 300 MET ASN ASN GLY TYR ASN GLN PRO GLY CYS GLY LEU PRO
SEQRES 18 D 300 LEU ILE GLY GLU THR CYS SER HIS THR ARG ALA VAL LYS
SEQRES 19 D 300 TYR PHE THR GLU CYS ILE LYS HIS GLU CYS CYS LEU ILE
SEQRES 20 D 300 GLY VAL PRO GLN SER LYS LYS PRO GLN PRO VAL SER LYS
SEQRES 21 D 300 CYS THR ARG ASN GLU CYS VAL CYS VAL GLY LEU ASN ALA
SEQRES 22 D 300 LYS THR TYR PRO LYS THR GLY SER PHE TYR VAL PRO VAL
SEQRES 23 D 300 GLU SER LYS ALA PRO TYR CYS ASN ASN LYS GLY LYS ILE
SEQRES 24 D 300 ILE
HET CL A 401 1
HET CL A 402 1
HET CL A 403 1
HET CL A 404 1
HET CL A 405 1
HET HG A 406 1
HET CL B 401 1
HET CL B 402 1
HET CL B 403 1
HET CL B 404 1
HET CL B 405 1
HET CL B 406 1
HET CL B 407 1
HET CL B 408 1
HET CL B 409 1
HET CL B 410 1
HET CL B 411 1
HET CL B 412 1
HET HG B 413 1
HET CL C 501 1
HET CL C 502 1
HET CL C 503 1
HET CL C 504 1
HET HG C 505 1
HET CL D 401 1
HET CL D 402 1
HET CL D 403 1
HETNAM CL CHLORIDE ION
HETNAM HG MERCURY (II) ION
FORMUL 5 CL 24(CL 1-)
FORMUL 10 HG 3(HG 2+)
FORMUL 32 HOH *477(H2 O)
HELIX 1 1 SER A 7 VAL A 11 5 5
HELIX 2 2 ASP A 29 LYS A 38 5 10
HELIX 3 3 THR A 59 ASP A 71 1 13
HELIX 4 4 ILE A 94 ASN A 125 1 32
HELIX 5 5 PRO A 127 ALA A 129 5 3
HELIX 6 6 SER A 137 LEU A 153 1 17
HELIX 7 7 ASP A 175 ARG A 179 5 5
HELIX 8 8 GLY A 224 HIS A 242 1 19
HELIX 9 9 ASN A 272 TYR A 276 5 5
HELIX 10 10 SER B 7 VAL B 11 5 5
HELIX 11 11 ASP B 29 LYS B 38 5 10
HELIX 12 12 THR B 59 ASP B 71 1 13
HELIX 13 13 CYS B 87 MET B 91 5 5
HELIX 14 14 ILE B 94 ASN B 125 1 32
HELIX 15 15 PRO B 127 ALA B 129 5 3
HELIX 16 16 LEU B 138 LEU B 153 1 16
HELIX 17 17 ASP B 175 ARG B 179 5 5
HELIX 18 18 GLY B 224 HIS B 242 1 19
HELIX 19 19 PRO B 257 CYS B 261 5 5
HELIX 20 20 ASN B 272 TYR B 276 5 5
HELIX 21 21 SER C 7 VAL C 11 5 5
HELIX 22 22 ASP C 29 LYS C 39 5 11
HELIX 23 23 THR C 59 ASP C 71 1 13
HELIX 24 24 CYS C 87 MET C 91 5 5
HELIX 25 25 ILE C 94 ASN C 125 1 32
HELIX 26 26 PRO C 127 ALA C 129 5 3
HELIX 27 27 SER C 137 LEU C 153 1 17
HELIX 28 28 ASP C 175 ARG C 179 5 5
HELIX 29 29 CYS C 181 THR C 183 5 3
HELIX 30 30 GLY C 224 HIS C 242 1 19
HELIX 31 31 PRO C 257 CYS C 261 5 5
HELIX 32 32 ASN C 272 TYR C 276 5 5
HELIX 33 33 SER D 7 VAL D 11 5 5
HELIX 34 34 ASP D 29 LYS D 38 5 10
HELIX 35 35 THR D 59 ASP D 71 1 13
HELIX 36 36 CYS D 87 MET D 91 5 5
HELIX 37 37 ILE D 94 ASN D 125 1 32
HELIX 38 38 PRO D 127 ALA D 129 5 3
HELIX 39 39 SER D 137 LEU D 153 1 17
HELIX 40 40 ASP D 175 ARG D 179 5 5
HELIX 41 41 GLY D 224 HIS D 242 1 19
HELIX 42 42 PRO D 257 CYS D 261 5 5
HELIX 43 43 ASN D 272 TYR D 276 5 5
SHEET 1 A11 PHE A 25 TYR A 26 0
SHEET 2 A11 LYS A 12 LEU A 16 -1 N MET A 13 O TYR A 26
SHEET 3 A11 TYR A 75 ASP A 81 -1 O VAL A 77 N LEU A 16
SHEET 4 A11 GLN A 45 THR A 50 1 N ILE A 49 O ILE A 80
SHEET 5 A11 ILE A 131 HIS A 136 1 O ARG A 132 N PHE A 48
SHEET 6 A11 TYR A 158 LEU A 164 1 O LEU A 164 N GLY A 135
SHEET 7 A11 ALA A 185 HIS A 192 1 O GLN A 189 N GLY A 163
SHEET 8 A11 VAL A 206 MET A 209 1 O PHE A 208 N ILE A 190
SHEET 9 A11 GLY A 280 TYR A 283 1 O PHE A 282 N MET A 209
SHEET 10 A11 ILE A 247 PRO A 250 -1 N VAL A 249 O TYR A 283
SHEET 11 A11 VAL A 267 CYS A 268 -1 O VAL A 267 N GLY A 248
SHEET 1 B10 LYS B 12 LEU B 16 0
SHEET 2 B10 TYR B 75 ASP B 81 -1 O VAL B 77 N LEU B 16
SHEET 3 B10 GLN B 45 THR B 50 1 N GLN B 45 O LEU B 76
SHEET 4 B10 ILE B 131 HIS B 136 1 O ILE B 134 N THR B 50
SHEET 5 B10 TYR B 158 LEU B 164 1 O LEU B 164 N GLY B 135
SHEET 6 B10 ALA B 185 HIS B 192 1 O ILE B 191 N GLY B 163
SHEET 7 B10 VAL B 206 MET B 209 1 O PHE B 208 N ILE B 190
SHEET 8 B10 GLY B 280 TYR B 283 1 O PHE B 282 N MET B 209
SHEET 9 B10 ILE B 247 PRO B 250 -1 N VAL B 249 O TYR B 283
SHEET 10 B10 VAL B 267 CYS B 268 -1 O VAL B 267 N GLY B 248
SHEET 1 C10 LYS C 12 LEU C 16 0
SHEET 2 C10 TYR C 75 ASP C 81 -1 O VAL C 77 N LEU C 16
SHEET 3 C10 GLN C 45 THR C 50 1 N GLN C 45 O LEU C 76
SHEET 4 C10 ILE C 131 HIS C 136 1 O ARG C 132 N PHE C 48
SHEET 5 C10 TYR C 158 LEU C 164 1 O ILE C 162 N LEU C 133
SHEET 6 C10 ALA C 185 HIS C 192 1 O TYR C 187 N ILE C 161
SHEET 7 C10 VAL C 206 MET C 209 1 O PHE C 208 N HIS C 192
SHEET 8 C10 GLY C 280 TYR C 283 1 O GLY C 280 N ASP C 207
SHEET 9 C10 ILE C 247 PRO C 250 -1 N VAL C 249 O TYR C 283
SHEET 10 C10 VAL C 267 CYS C 268 -1 O VAL C 267 N GLY C 248
SHEET 1 D10 LYS D 12 LEU D 16 0
SHEET 2 D10 TYR D 75 ASP D 81 -1 O VAL D 77 N LEU D 16
SHEET 3 D10 GLN D 45 THR D 50 1 N ILE D 49 O ILE D 80
SHEET 4 D10 ILE D 131 HIS D 136 1 O ILE D 134 N PHE D 48
SHEET 5 D10 GLU D 160 LEU D 164 1 O ILE D 162 N LEU D 133
SHEET 6 D10 VAL D 188 HIS D 192 1 O GLN D 189 N GLY D 163
SHEET 7 D10 VAL D 206 MET D 209 1 O PHE D 208 N HIS D 192
SHEET 8 D10 GLY D 280 TYR D 283 1 O PHE D 282 N MET D 209
SHEET 9 D10 ILE D 247 PRO D 250 -1 N VAL D 249 O TYR D 283
SHEET 10 D10 VAL D 267 CYS D 268 -1 O VAL D 267 N GLY D 248
SSBOND 1 CYS A 4 CYS A 87 1555 1555 2.02
SSBOND 2 CYS A 176 CYS A 181 1555 1555 2.05
SSBOND 3 CYS A 218 CYS A 227 1555 1555 2.05
SSBOND 4 CYS A 244 CYS A 268 1555 1555 2.05
SSBOND 5 CYS A 245 CYS A 293 1555 1555 2.05
SSBOND 6 CYS A 261 CYS A 266 1555 1555 2.03
SSBOND 7 CYS B 4 CYS B 87 1555 1555 2.02
SSBOND 8 CYS B 176 CYS B 181 1555 1555 2.04
SSBOND 9 CYS B 218 CYS B 227 1555 1555 2.04
SSBOND 10 CYS B 244 CYS B 268 1555 1555 2.04
SSBOND 11 CYS B 245 CYS B 293 1555 1555 2.04
SSBOND 12 CYS B 261 CYS B 266 1555 1555 2.03
SSBOND 13 CYS C 4 CYS C 87 1555 1555 2.03
SSBOND 14 CYS C 176 CYS C 181 1555 1555 2.04
SSBOND 15 CYS C 218 CYS C 227 1555 1555 2.03
SSBOND 16 CYS C 244 CYS C 268 1555 1555 2.04
SSBOND 17 CYS C 245 CYS C 293 1555 1555 2.04
SSBOND 18 CYS C 261 CYS C 266 1555 1555 2.05
SSBOND 19 CYS D 4 CYS D 87 1555 1555 2.02
SSBOND 20 CYS D 176 CYS D 181 1555 1555 2.05
SSBOND 21 CYS D 218 CYS D 227 1555 1555 2.03
SSBOND 22 CYS D 244 CYS D 268 1555 1555 2.06
SSBOND 23 CYS D 245 CYS D 293 1555 1555 2.04
SSBOND 24 CYS D 261 CYS D 266 1555 1555 2.02
LINK ND2 ASN B 272 HG HG B 413 1555 1555 2.70
LINK HG HG A 406 O HOH A 577 1555 1555 2.91
CISPEP 1 ASN A 211 GLY A 212 0 -1.83
CISPEP 2 ALA A 290 PRO A 291 0 0.55
CISPEP 3 ASN B 211 GLY B 212 0 -1.65
CISPEP 4 ALA B 290 PRO B 291 0 0.09
CISPEP 5 ASN C 211 GLY C 212 0 1.43
CISPEP 6 ALA C 290 PRO C 291 0 0.02
CISPEP 7 ASN D 211 GLY D 212 0 -0.90
CISPEP 8 ALA D 290 PRO D 291 0 0.53
SITE 1 AC1 3 LYS A 241 HG A 406 CL B 402
SITE 1 AC2 5 LYS A 298 HOH A 577 CL B 402 CL B 407
SITE 2 AC2 5 HG B 413
SITE 1 AC3 5 GLU A 238 LYS A 241 CL A 404 HOH A 513
SITE 2 AC3 5 HOH C 676
SITE 1 AC4 2 CL A 403 HOH C 676
SITE 1 AC5 4 LYS A 241 CL A 401 HOH A 577 CL B 402
SITE 1 AC6 4 LYS B 241 HIS B 242 CL B 405 HOH C 682
SITE 1 AC7 6 CL A 401 CL A 402 HG A 406 HOH A 577
SITE 2 AC7 6 CL B 407 HG B 413
SITE 1 AC8 4 GLU B 238 LYS B 241 CL B 404 CL B 410
SITE 1 AC9 4 GLU B 238 LYS B 241 CL B 403 CL B 410
SITE 1 BC1 4 CL B 401 HOH C 643 HOH C 682 HOH C 694
SITE 1 BC2 2 CL B 409 HOH C 635
SITE 1 BC3 4 CL A 402 LYS B 72 CL B 402 HG B 413
SITE 1 BC4 4 CL B 411 CL C 502 HOH D 544 HOH D 545
SITE 1 BC5 1 CL B 406
SITE 1 BC6 4 LYS B 241 CL B 403 CL B 404 HOH D 543
SITE 1 BC7 2 CL B 408 CL C 502
SITE 1 BC8 3 LYS B 298 HOH C 682 HOH C 694
SITE 1 BC9 5 CL A 402 GLU B 243 ASN B 272 CL B 402
SITE 2 BC9 5 CL B 407
SITE 1 CC1 4 LYS C 298 CL C 502 CL C 504 HG C 505
SITE 1 CC2 5 CL B 408 CL B 411 CL C 501 CL C 504
SITE 2 CC2 5 HG C 505
SITE 1 CC3 1 GLU C 238
SITE 1 CC4 3 CL C 501 CL C 502 HG C 505
SITE 1 CC5 4 HIS C 242 CL C 501 CL C 502 CL C 504
SITE 1 CC6 1 HOH C 650
SITE 1 CC7 1 CL D 403
SITE 1 CC8 4 GLU D 238 CL D 402 HOH D 592 HOH D 597
CRYST1 57.276 70.147 81.724 107.14 109.99 100.90 P 1 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 0.017459 0.003362 0.008317 0.00000
SCALE2 0.000000 0.014518 0.006138 0.00000
SCALE3 0.000000 0.000000 0.014137 0.00000
TER 2293 ILE A 299
TER 4586 ILE B 299
TER 6879 ILE C 299
TER 9172 ILE D 299
MASTER 528 0 27 43 41 0 31 6 9672 4 52 96
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