HEADER ANTIMICROBIAL PROTEIN 20-OCT-06 2NLG
TITLE HUMAN BETA-DEFENSIN-1 (MUTANT LYS22GLU)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-DEFENSIN 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: HUMAN BETA-DEFENSIN 1, RESIDUES 33-68;
COMPND 5 SYNONYM: BD-1, DEFENSIN, BETA 1, HBD-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DEFB1, BD1, HBD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAED4
KEYWDS ANTIMICROBIAL, CHEMOTACTIC, DEFENSIN, MUTANT, ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUBKOWSKI,M.PAZGIER
REVDAT 8 30-AUG-23 2NLG 1 REMARK
REVDAT 7 20-OCT-21 2NLG 1 REMARK SEQADV
REVDAT 6 18-OCT-17 2NLG 1 REMARK
REVDAT 5 13-JUL-11 2NLG 1 VERSN
REVDAT 4 24-FEB-09 2NLG 1 VERSN
REVDAT 3 30-JAN-07 2NLG 1 JRNL
REVDAT 2 19-DEC-06 2NLG 1 JRNL
REVDAT 1 31-OCT-06 2NLG 0
JRNL AUTH M.PAZGIER,A.PRAHL,D.M.HOOVER,J.LUBKOWSKI
JRNL TITL STUDIES OF THE BIOLOGICAL PROPERTIES OF HUMAN BETA-DEFENSIN
JRNL TITL 2 1.
JRNL REF J.BIOL.CHEM. V. 282 1819 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17071614
JRNL DOI 10.1074/JBC.M607210200
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 14844
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 751
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 903
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1084
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 259
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.29000
REMARK 3 B23 (A**2) : 0.76000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.014
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1155 ; 0.017 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1562 ; 1.601 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 140 ; 5.972 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 44 ;39.022 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 188 ;13.631 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;28.853 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 155 ; 0.100 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 840 ; 0.007 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 480 ; 0.227 ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 773 ; 0.303 ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.170 ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 88 ; 0.185 ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.116 ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 735 ; 1.097 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1133 ; 1.539 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 490 ; 2.742 ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 429 ; 3.706 ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 36
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5568 16.5533 12.1070
REMARK 3 T TENSOR
REMARK 3 T11: -0.0756 T22: -0.0682
REMARK 3 T33: -0.0663 T12: 0.0036
REMARK 3 T13: -0.0057 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.2072 L22: 0.1629
REMARK 3 L33: 0.1534 L12: 0.1495
REMARK 3 L13: 0.0517 L23: 0.1253
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0517 S13: -0.0430
REMARK 3 S21: -0.0116 S22: 0.0328 S23: -0.0041
REMARK 3 S31: -0.0154 S32: 0.0152 S33: -0.0215
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000040008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14844
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.15600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1IJV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM SULFATE, SODIUM
REMARK 280 CACODYLATE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 293K
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, 2, 3, 4, 5, 6, 7
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 300 REMARK: BIOLOGICAL ASSEMBLY IS A MONOMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 2.02559
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 33.11811
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 -3.43650
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 -11.65334
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -40.14167
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -25.78000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -3.43650
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -11.65334
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -40.14167
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 27.80559
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 33.11811
REMARK 350 BIOMT3 2 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 O HOH A 336 O HOH A 352 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 17 CB CYS C 17 SG -0.098
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 C 18 C - N - CA ANGL. DEV. = 10.4 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 SER A 15 -161.25 -124.72
REMARK 500 TYR A 28 64.06 61.89
REMARK 500 SER D 15 -167.07 -116.38
REMARK 500 TYR D 28 61.81 62.04
REMARK 500
REMARK 500 REMARK: NULL
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NLB RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT ASN4ALA)
REMARK 900 RELATED ID: 2NLC RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT SER8ALA)
REMARK 900 RELATED ID: 2NLD RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT GLN11ALA)
REMARK 900 RELATED ID: 2NLE RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT GLN11ALA)
REMARK 900 RELATED ID: 2NLF RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT LEU13GLU)
REMARK 900 RELATED ID: 2NLH RELATED DB: PDB
REMARK 900 HUMAN BETA-DEFENSIN-1 (MUTANT GLN24ALA)
REMARK 900 RELATED ID: 2NLP RELATED DB: PDB
REMARK 900 RELATED ID: 2NLQ RELATED DB: PDB
REMARK 900 RELATED ID: 2NLS RELATED DB: PDB
DBREF 2NLG A 1 36 UNP P60022 BD01_HUMAN 33 68
DBREF 2NLG B 1 36 UNP P60022 BD01_HUMAN 33 68
DBREF 2NLG C 1 36 UNP P60022 BD01_HUMAN 33 68
DBREF 2NLG D 1 36 UNP P60022 BD01_HUMAN 33 68
SEQADV 2NLG GLU A 22 UNP P60022 LYS 54 ENGINEERED MUTATION
SEQADV 2NLG GLU B 22 UNP P60022 LYS 54 ENGINEERED MUTATION
SEQADV 2NLG GLU C 22 UNP P60022 LYS 54 ENGINEERED MUTATION
SEQADV 2NLG GLU D 22 UNP P60022 LYS 54 ENGINEERED MUTATION
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 GLU 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 GLU ILE GLN GLY THR
SEQRES 3 B 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
SEQRES 1 C 36 ASP HIS TYR ASN CYS VAL SER SER GLY GLY GLN CYS LEU
SEQRES 2 C 36 TYR SER ALA CYS PRO ILE PHE THR GLU ILE GLN GLY THR
SEQRES 3 C 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
SEQRES 1 D 36 ASP HIS TYR ASN CYS VAL SER SER GLY GLY GLN CYS LEU
SEQRES 2 D 36 TYR SER ALA CYS PRO ILE PHE THR GLU ILE GLN GLY THR
SEQRES 3 D 36 CYS TYR ARG GLY LYS ALA LYS CYS CYS LYS
HET SO4 A 302 5
HET SO4 B 301 5
HET SO4 B 307 5
HET SO4 C 305 5
HET SO4 C 306 5
HET SO4 C 308 5
HET SO4 D 303 5
HET SO4 D 304 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 13 HOH *259(H2 O)
HELIX 1 1 ASP A 1 SER A 8 1 8
HELIX 2 2 ASP B 1 SER B 8 1 8
HELIX 3 3 ASP C 1 SER C 8 1 8
HELIX 4 4 ASP D 1 SER D 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 O CYS A 35 N GLN A 11
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 O LYS B 33 N LEU B 13
SHEET 3 B 3 ILE B 23 CYS B 27 -1 N GLY B 25 O CYS B 34
SHEET 1 C 3 GLN C 11 LEU C 13 0
SHEET 2 C 3 ALA C 32 CYS C 35 -1 O LYS C 33 N LEU C 13
SHEET 3 C 3 ILE C 23 CYS C 27 -1 N GLN C 24 O CYS C 34
SHEET 1 D 3 GLN D 11 LEU D 13 0
SHEET 2 D 3 ALA D 32 CYS D 35 -1 O CYS D 35 N GLN D 11
SHEET 3 D 3 ILE D 23 CYS D 27 -1 N GLN D 24 O CYS D 34
SSBOND 1 CYS A 5 CYS A 34 1555 1555 2.05
SSBOND 2 CYS A 12 CYS A 27 1555 1555 2.05
SSBOND 3 CYS A 17 CYS A 35 1555 1555 2.06
SSBOND 4 CYS B 5 CYS B 34 1555 1555 2.03
SSBOND 5 CYS B 12 CYS B 27 1555 1555 2.05
SSBOND 6 CYS B 17 CYS B 35 1555 1555 2.05
SSBOND 7 CYS C 5 CYS C 34 1555 1555 2.05
SSBOND 8 CYS C 12 CYS C 27 1555 1555 2.05
SSBOND 9 CYS C 17 CYS C 35 1555 1555 2.05
SSBOND 10 CYS D 5 CYS D 34 1555 1555 2.02
SSBOND 11 CYS D 12 CYS D 27 1555 1555 2.03
SSBOND 12 CYS D 17 CYS D 35 1555 1555 2.04
SITE 1 AC1 10 TYR A 3 HOH A 303 HOH A 314 ASP B 1
SITE 2 AC1 10 HIS B 2 CYS B 27 TYR B 28 ARG B 29
SITE 3 AC1 10 HOH B 310 HOH C 344
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 303 HOH A 311 HOH A 344
SITE 3 AC2 11 HOH A 353 TYR B 3 HOH B 310
SITE 1 AC3 8 ASP A 1 GLY A 25 THR A 26 HOH A 348
SITE 2 AC3 8 ARG C 29 ASN D 4 HOH D 315 HOH D 341
SITE 1 AC4 11 TYR C 3 HOH C 310 ASP D 1 HIS D 2
SITE 2 AC4 11 CYS D 27 TYR D 28 ARG D 29 HOH D 307
SITE 3 AC4 11 HOH D 310 HOH D 313 HOH D 358
SITE 1 AC5 11 HOH A 318 HOH B 328 ASP C 1 HIS C 2
SITE 2 AC5 11 CYS C 27 TYR C 28 ARG C 29 HOH C 310
SITE 3 AC5 11 HOH C 328 TYR D 3 HOH D 307
SITE 1 AC6 10 HOH A 304 ARG B 29 HOH B 313 HOH B 314
SITE 2 AC6 10 ASP C 1 GLY C 25 THR C 26 HOH C 311
SITE 3 AC6 10 HOH C 318 HOH C 334
SITE 1 AC7 5 ASP B 1 GLY B 25 THR B 26 HOH B 349
SITE 2 AC7 5 HOH B 354
SITE 1 AC8 5 SER C 8 LYS C 31 LYS C 36 HOH C 340
SITE 2 AC8 5 HOH C 343
CRYST1 25.780 33.180 41.940 73.60 85.30 86.50 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 0.038790 -0.002372 -0.002632 0.00000
SCALE2 0.000000 0.030195 -0.008766 0.00000
SCALE3 0.000000 0.000000 0.024912 0.00000
(ATOM LINES ARE NOT SHOWN.)
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