HEADER DEFENSIN 30-APR-01 1IJV
TITLE HUMAN BETA-DEFENSIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HBD-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE OCCURS NATURALLY IN HUMANS (HOMO SAPIENS).
KEYWDS DEFENSIN, HUMAN BETA-DEFENSIN-1, BETA-DEFENSIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.HOOVER,J.LUBKOWSKI
REVDAT 4 13-JUL-11 1IJV 1 VERSN
REVDAT 3 24-FEB-09 1IJV 1 VERSN
REVDAT 2 01-APR-03 1IJV 1 JRNL
REVDAT 1 24-OCT-01 1IJV 0
JRNL AUTH D.M.HOOVER,O.CHERTOV,J.LUBKOWSKI
JRNL TITL THE STRUCTURE OF HUMAN BETA-DEFENSIN-1: NEW INSIGHTS INTO
JRNL TITL 2 STRUCTURAL PROPERTIES OF BETA-DEFENSINS.
JRNL REF J.BIOL.CHEM. V. 276 39021 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11486002
JRNL DOI 10.1074/JBC.M103830200
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.157
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.161
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 760
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 3966
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.131
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.139
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 635
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 31736
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 542
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 738.00
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 536.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 7167
REMARK 3 NUMBER OF RESTRAINTS : 9055
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.070
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.080
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.030
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.060
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.090
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IJV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-01.
REMARK 100 THE RCSB ID CODE IS RCSB013346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X9B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92021
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40500
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: SHELX, SHARP, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: ANOMALOUS DATA USED FOR REFINEMENT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM SULFATE, SODIUM
REMARK 280 ACETATE, POTASSIUM BROMIDE, GLYCEROL, PH 4.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 285K
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 13.56050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.92650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.62150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 26.92650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.56050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.62150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 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 BR BR B 104 O HOH B 290 0.84
REMARK 500 BR BR B 107 O HOH B 289 1.61
REMARK 500 NE2 GLN B 24 BR BR B 103 1.83
REMARK 500 BR BR A 106 O HOH A 330 1.97
REMARK 500 BR BR B 107 O HOH B 242 2.03
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 TYR B 14 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR B 14 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 PHE B 20 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 29 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 28 62.30 64.72
REMARK 500 PHE B 20 -2.43 75.57
REMARK 500 GLN B 24 36.06 -149.22
REMARK 500 TYR B 28 62.91 61.39
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 359 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 333 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH B 350 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH B 368 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 369 DISTANCE = 5.17 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 K B 109 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 B 101 O2
REMARK 620 2 SO4 B 101 O3 44.5
REMARK 620 3 HOH B 202 O 84.6 51.0
REMARK 620 4 HOH B 201 O 133.1 92.1 75.8
REMARK 620 5 HIS A 2 ND1 150.3 158.6 108.1 76.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 109
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IJU RELATED DB: PDB
REMARK 900 1IJU IS HUMAN BETA-DEFENSIN-1
DBREF 1IJV A 1 36 UNP P60022 BD01_HUMAN 33 68
DBREF 1IJV B 1 36 UNP P60022 BD01_HUMAN 33 68
SEQRES 1 A 36 ASP HIS TYR ASN CYS VAL SER SER GLY GLY GLN CYS LEU
SEQRES 2 A 36 TYR SER ALA CYS PRO ILE PHE THR LYS ILE GLN GLY THR
SEQRES 3 A 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
SEQRES 1 B 36 ASP HIS TYR ASN CYS VAL SER SER GLY GLY GLN CYS LEU
SEQRES 2 B 36 TYR SER ALA CYS PRO ILE PHE THR LYS ILE GLN GLY THR
SEQRES 3 B 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
HET SO4 B 101 5
HET SO4 A 102 5
HET BR B 103 1
HET BR B 104 1
HET BR A 105 1
HET BR A 106 1
HET BR B 107 1
HET BR A 108 1
HET K B 109 1
HETNAM SO4 SULFATE ION
HETNAM BR BROMIDE ION
HETNAM K POTASSIUM ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 BR 6(BR 1-)
FORMUL 11 K K 1+
FORMUL 12 HOH *176(H2 O)
HELIX 1 1 ASP A 1 SER A 8 1 8
HELIX 2 2 ASP B 1 SER B 8 1 8
SHEET 1 A 3 GLN A 11 LEU A 13 0
SHEET 2 A 3 ALA A 32 CYS A 35 -1 N LYS A 33 O LEU A 13
SHEET 3 A 3 ILE A 23 CYS A 27 -1 N GLN A 24 O CYS A 34
SHEET 1 B 3 GLN B 11 LEU B 13 0
SHEET 2 B 3 ALA B 32 CYS B 35 -1 N LYS B 33 O LEU B 13
SHEET 3 B 3 ILE B 23 CYS B 27 -1 N GLN B 24 O CYS B 34
SSBOND 1 CYS A 5 CYS A 34 1555 1555 2.04
SSBOND 2 CYS A 12 CYS A 27 1555 1555 2.05
SSBOND 3 CYS A 17 CYS A 35 1555 1555 2.05
SSBOND 4 CYS B 5 CYS B 34 1555 1555 2.06
SSBOND 5 CYS B 12 CYS B 27 1555 1555 2.05
SSBOND 6 CYS B 17 CYS B 35 1555 1555 2.06
LINK K K B 109 O2 SO4 B 101 1555 1555 2.69
LINK K K B 109 O3 SO4 B 101 1555 1555 3.42
LINK K K B 109 O HOH B 202 1555 1555 2.79
LINK K K B 109 O HOH B 201 1555 1555 3.16
LINK K K B 109 ND1 HIS A 2 1555 3655 2.70
SITE 1 AC1 10 TYR A 3 HOH A 209 ASP B 1 HIS B 2
SITE 2 AC1 10 CYS B 27 TYR B 28 ARG B 29 K B 109
SITE 3 AC1 10 HOH B 202 HOH B 204
SITE 1 AC2 11 ASP A 1 HIS A 2 CYS A 27 TYR A 28
SITE 2 AC2 11 ARG A 29 HOH A 205 HOH A 209 HOH A 281
SITE 3 AC2 11 TYR B 3 HOH B 201 HOH B 202
SITE 1 AC3 4 ASP B 1 ASN B 4 GLN B 24 HOH B 341
SITE 1 AC4 3 ALA B 16 CYS B 17 HOH B 290
SITE 1 AC5 2 CYS A 12 HOH A 235
SITE 1 AC6 3 CYS A 17 HOH A 330 HOH A 346
SITE 1 AC7 6 HOH B 211 HOH B 219 HOH B 242 HOH B 258
SITE 2 AC7 6 HOH B 289 HOH B 350
SITE 1 AC8 3 ASP A 1 ASN A 4 GLY A 25
SITE 1 AC9 5 HIS A 2 TYR A 3 HIS B 2 SO4 B 101
SITE 2 AC9 5 HOH B 202
CRYST1 27.121 47.243 53.853 90.00 90.00 90.00 P 21 21 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 0.036872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
