HEADER ANTIMICROBIAL PROTEIN 10-MAY-05 1ZMK
TITLE CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN-2 (VARIANT GLY16-> D-ALA), P
TITLE 2 42 21 2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL DEFENSIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 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: DEFA3, DEF3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-DEFENSIN, ANTIMICROBIAL, D-AMINO ACID SUBSTITUTIONS,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUBKOWSKI,A.PRAHL,W.LU
REVDAT 7 23-AUG-23 1ZMK 1 REMARK
REVDAT 6 20-OCT-21 1ZMK 1 REMARK SEQADV LINK
REVDAT 5 11-OCT-17 1ZMK 1 REMARK
REVDAT 4 13-JUL-11 1ZMK 1 VERSN
REVDAT 3 24-FEB-09 1ZMK 1 VERSN
REVDAT 2 20-DEC-05 1ZMK 1 JRNL
REVDAT 1 16-AUG-05 1ZMK 0
JRNL AUTH C.XIE,A.PRAHL,B.ERICKSEN,Z.WU,P.ZENG,X.LI,W.Y.LU,
JRNL AUTH 2 J.LUBKOWSKI,W.LU
JRNL TITL RECONSTRUCTION OF THE CONSERVED BETA-BULGE IN MAMMALIAN
JRNL TITL 2 DEFENSINS USING D-AMINO ACIDS.
JRNL REF J.BIOL.CHEM. V. 280 32921 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15894545
JRNL DOI 10.1074/JBC.M503084200
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 13688
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 734
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1921
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.1290
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.2010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 468
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.06000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.054
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.025
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.270
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 498 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 447 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 673 ; 1.721 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1020 ; 3.881 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 56 ; 8.149 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 22 ;19.488 ;18.182
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 73 ;10.723 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.136 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 65 ; 0.183 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 540 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 130 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 71 ; 0.288 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 422 ; 0.235 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 213 ; 0.197 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 342 ; 0.119 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 65 ; 0.245 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 4 ; 0.258 ; 0.500
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): 8 ; 0.306 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.279 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.424 ; 0.500
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): 369 ; 2.553 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 122 ; 1.012 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 458 ; 3.102 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 304 ; 3.017 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 215 ; 3.380 ; 3.000
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): 1307 ; 1.636 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 77 ; 9.842 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 929 ; 3.526 ; 3.000
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 : 2
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 : A 1 A 29
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4999 28.4337 42.5799
REMARK 3 T TENSOR
REMARK 3 T11: -0.0011 T22: -0.0016
REMARK 3 T33: -0.0322 T12: 0.0204
REMARK 3 T13: 0.0031 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 6.8732 L22: 0.4419
REMARK 3 L33: 0.5575 L12: 0.3533
REMARK 3 L13: 0.4303 L23: -0.0208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: -0.2616 S13: 0.0880
REMARK 3 S21: 0.0919 S22: 0.0528 S23: 0.0421
REMARK 3 S31: 0.0255 S32: 0.0022 S33: 0.0421
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 29
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1823 34.1961 32.6357
REMARK 3 T TENSOR
REMARK 3 T11: -0.0230 T22: -0.0105
REMARK 3 T33: -0.0096 T12: 0.0066
REMARK 3 T13: 0.0002 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.3516 L22: 2.9878
REMARK 3 L33: 1.3046 L12: 0.6794
REMARK 3 L13: 0.1297 L23: 0.9094
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: -0.0091 S13: 0.0399
REMARK 3 S21: 0.0054 S22: -0.0363 S23: 0.0902
REMARK 3 S31: -0.0180 S32: -0.0328 S33: 0.0415
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1ZMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24405
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.42900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: BASED ON MONOMER OF HNP-3 (PDB ID CODE 1DFN)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-SODIUM CITRATE DIHYDRATE,
REMARK 280 TRIS/HCL, PEG 8000, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 23.57400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 23.57400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.32150
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 23.57400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 23.57400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.32150
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 23.57400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 23.57400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.32150
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 23.57400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 23.57400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.32150
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -1.000000 0.000000 0.000000 47.14800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 47.14800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 50.64300
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 47.14800
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 47.14800
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 50.64300
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL B 102 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 135 LIES ON A SPECIAL POSITION.
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 N CYS A 1 CL CL A 101 2.01
REMARK 500 N CYS B 1 CL CL A 101 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 124 O HOH B 227 5546 1.56
REMARK 500 O HOH A 138 O HOH B 235 2665 1.96
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 B 29 CB CYS B 29 SG -0.110
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 CYS B 29 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
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 CL A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DFN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RELATED ALPHA-DEFENSIN
REMARK 900 RELATED ID: 1ZMI RELATED DB: PDB
REMARK 900 RELATED ID: 1ZMM RELATED DB: PDB
REMARK 900 RELATED ID: 1ZMP RELATED DB: PDB
REMARK 900 RELATED ID: 1ZMQ RELATED DB: PDB
DBREF 1ZMK A 1 29 UNP P59666 DEF3_HUMAN 66 94
DBREF 1ZMK B 1 29 UNP P59666 DEF3_HUMAN 66 94
SEQADV 1ZMK DAL A 16 UNP P59666 GLY 81 ENGINEERED MUTATION
SEQADV 1ZMK DAL B 16 UNP P59666 GLY 81 ENGINEERED MUTATION
SEQRES 1 A 29 CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU ARG
SEQRES 2 A 29 ARG TYR DAL THR CYS ILE TYR GLN GLY ARG LEU TRP ALA
SEQRES 3 A 29 PHE CYS CYS
SEQRES 1 B 29 CYS TYR CYS ARG ILE PRO ALA CYS ILE ALA GLY GLU ARG
SEQRES 2 B 29 ARG TYR DAL THR CYS ILE TYR GLN GLY ARG LEU TRP ALA
SEQRES 3 B 29 PHE CYS CYS
MODRES 1ZMK DAL A 16 ALA D-ALANINE
MODRES 1ZMK DAL B 16 ALA D-ALANINE
HET DAL A 16 5
HET DAL B 16 5
HET CL A 101 1
HET CL B 102 1
HET GOL B 201 12
HETNAM DAL D-ALANINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 DAL 2(C3 H7 N O2)
FORMUL 3 CL 2(CL 1-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *75(H2 O)
SHEET 1 A 6 TYR A 2 ARG A 4 0
SHEET 2 A 6 ARG A 23 CYS A 29 -1 O CYS A 28 N TYR A 2
SHEET 3 A 6 ARG A 13 TYR A 20 -1 N TYR A 15 O PHE A 27
SHEET 4 A 6 ARG B 13 TYR B 20 -1 O ILE B 19 N THR A 17
SHEET 5 A 6 ARG B 23 CYS B 29 -1 O PHE B 27 N TYR B 15
SHEET 6 A 6 TYR B 2 ARG B 4 -1 N TYR B 2 O CYS B 28
SSBOND 1 CYS A 1 CYS A 29 1555 1555 2.05
SSBOND 2 CYS A 3 CYS A 18 1555 1555 2.05
SSBOND 3 CYS A 8 CYS A 28 1555 1555 2.05
SSBOND 4 CYS B 1 CYS B 29 1555 1555 2.21
SSBOND 5 CYS B 3 CYS B 18 1555 1555 2.03
SSBOND 6 CYS B 8 CYS B 28 1555 1555 2.06
LINK C TYR A 15 N DAL A 16 1555 1555 1.33
LINK C DAL A 16 N THR A 17 1555 1555 1.33
LINK C TYR B 15 N DAL B 16 1555 1555 1.30
LINK C DAL B 16 N THR B 17 1555 1555 1.33
CISPEP 1 ILE A 5 PRO A 6 0 1.37
CISPEP 2 ILE B 5 PRO B 6 0 7.43
SITE 1 AC1 3 CYS A 1 CYS B 1 HOH B 223
SITE 1 AC2 1 HOH B 218
SITE 1 AC3 7 ARG B 14 THR B 17 ARG B 23 LEU B 24
SITE 2 AC3 7 TRP B 25 ALA B 26 HOH B 231
CRYST1 47.148 47.148 50.643 90.00 90.00 90.00 P 42 21 2 16
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 0.021210 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021210 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019746 0.00000
(ATOM LINES ARE NOT SHOWN.)
END