HEADER HYDROLASE/DE NOVO PROTEIN 14-AUG-12 4GLA
TITLE OBODY NL8 BOUND TO HEN EGG-WHITE LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 19-147;
COMPND 5 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV;
COMPND 6 EC: 3.2.1.17;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: OBODY NL8;
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: EGG WHITE;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: PYROBACULUM AEROPHILUM;
SOURCE 8 ORGANISM_TAXID: 13773;
SOURCE 9 GENE: ASPS;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS BETA BARREL, OB-FOLD, PROTEIN-PROTEIN COMPLEX, NOVEL SCAFFOLD,
KEYWDS 2 MURAMINIDASE, ENZYME INHIBITION, ENGINEERED BINDING PROTEIN,
KEYWDS 3 HYDROLASE-DE NOVO PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.STEEMSON
REVDAT 2 12-FEB-14 4GLA 1 JRNL
REVDAT 1 14-AUG-13 4GLA 0
JRNL AUTH J.D.STEEMSON,M.BAAKE,J.RAKONJAC,V.L.ARCUS,M.T.LIDDAMENT
JRNL TITL TRACKING MOLECULAR RECOGNITION AT THE ATOMIC LEVEL WITH A
JRNL TITL 2 NEW PROTEIN SCAFFOLD BASED ON THE OB-FOLD.
JRNL REF PLOS ONE V. 9 86050 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 24465865
JRNL DOI 10.1371/JOURNAL.PONE.0086050
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 13456
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 667
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 908
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3334
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.04000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.428
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.321
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.116
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3399 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4600 ; 1.452 ; 1.926
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 431 ; 6.748 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;36.343 ;23.154
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 558 ;20.576 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;18.389 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 502 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2578 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1494 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2283 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 140 ; 0.152 ; 0.200
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): 67 ; 0.264 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.175 ; 0.200
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): 2185 ; 0.510 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3412 ; 0.879 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1419 ; 1.438 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1188 ; 2.373 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 129 3
REMARK 3 1 A 1 A 129 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 516 ; 0.060 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 B (A): 485 ; 0.580 ; 5.000
REMARK 3 TIGHT THERMAL 1 B (A**2): 516 ; 0.110 ; 0.500
REMARK 3 LOOSE THERMAL 1 B (A**2): 485 ; 1.390 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : D C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 20 D 45 2
REMARK 3 1 C 20 C 45 2
REMARK 3 2 D 54 D 88 2
REMARK 3 2 C 54 C 88 2
REMARK 3 3 D 97 D 111 2
REMARK 3 3 C 97 C 111 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 D (A): 284 ; 0.050 ; 0.050
REMARK 3 MEDIUM POSITIONAL 2 D (A): 271 ; 0.440 ; 0.500
REMARK 3 TIGHT THERMAL 2 D (A**2): 284 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 2 D (A**2): 271 ; 0.730 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 128
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4387 -18.8315 33.7942
REMARK 3 T TENSOR
REMARK 3 T11: -0.1085 T22: -0.0608
REMARK 3 T33: -0.1488 T12: 0.0977
REMARK 3 T13: 0.0413 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 6.3577 L22: 2.8069
REMARK 3 L33: 3.3455 L12: -1.0351
REMARK 3 L13: 0.3985 L23: -1.3234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0991 S12: -0.0696 S13: -0.2645
REMARK 3 S21: 0.2871 S22: 0.0321 S23: 0.2993
REMARK 3 S31: -0.0088 S32: 0.0496 S33: -0.1312
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 128
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3770 -13.1512 5.5895
REMARK 3 T TENSOR
REMARK 3 T11: -0.0592 T22: 0.2450
REMARK 3 T33: 0.2012 T12: -0.0492
REMARK 3 T13: 0.1520 T23: -0.0703
REMARK 3 L TENSOR
REMARK 3 L11: 6.5796 L22: 3.6591
REMARK 3 L33: 7.4093 L12: -1.7466
REMARK 3 L13: 1.8752 L23: -0.6230
REMARK 3 S TENSOR
REMARK 3 S11: -0.3895 S12: -0.4852 S13: -0.5751
REMARK 3 S21: 0.1231 S22: 0.2238 S23: -0.5051
REMARK 3 S31: -0.1281 S32: 1.3144 S33: 0.1657
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 22 C 104
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8605 -2.3282 1.1773
REMARK 3 T TENSOR
REMARK 3 T11: -0.0304 T22: -0.1012
REMARK 3 T33: -0.1554 T12: -0.1007
REMARK 3 T13: 0.0905 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 7.9393 L22: 6.7290
REMARK 3 L33: 1.8162 L12: -1.5249
REMARK 3 L13: -1.0459 L23: -0.3034
REMARK 3 S TENSOR
REMARK 3 S11: -0.2939 S12: -0.0374 S13: -0.4228
REMARK 3 S21: 0.1364 S22: 0.2334 S23: 0.2985
REMARK 3 S31: -0.0760 S32: -0.0884 S33: 0.0605
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 22 D 107
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1730 -8.0431 12.8408
REMARK 3 T TENSOR
REMARK 3 T11: -0.1618 T22: -0.0607
REMARK 3 T33: -0.1031 T12: 0.0020
REMARK 3 T13: 0.0242 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 6.6426 L22: 3.0558
REMARK 3 L33: 8.5727 L12: 0.5586
REMARK 3 L13: 0.3293 L23: -2.9053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: 0.0763 S13: 0.0021
REMARK 3 S21: -0.2058 S22: 0.1204 S23: 0.1009
REMARK 3 S31: -0.0960 S32: -0.0500 S33: -0.1677
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 4GLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB074325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95666
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : FLAT COLLIMATING RH COATED
REMARK 200 MIRROR, TOROIDAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16010
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.78800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M HEPES, 7% MPEG5000, PH 7.3,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.17200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.37950
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.37950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.58600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.37950
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.37950
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 124.75800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.37950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.37950
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.58600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.37950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.37950
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 124.75800
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 83.17200
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 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 GLY C -1
REMARK 465 SER C 0
REMARK 465 VAL C 1
REMARK 465 TYR C 2
REMARK 465 PRO C 3
REMARK 465 LYS C 4
REMARK 465 LYS C 5
REMARK 465 THR C 6
REMARK 465 HIS C 7
REMARK 465 TRP C 8
REMARK 465 THR C 9
REMARK 465 ALA C 10
REMARK 465 GLU C 11
REMARK 465 ILE C 12
REMARK 465 THR C 13
REMARK 465 PRO C 14
REMARK 465 ASN C 15
REMARK 465 GLU C 44A
REMARK 465 LYS C 105
REMARK 465 ALA C 106
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 VAL D 1
REMARK 465 TYR D 2
REMARK 465 PRO D 3
REMARK 465 LYS D 4
REMARK 465 LYS D 5
REMARK 465 THR D 6
REMARK 465 HIS D 7
REMARK 465 TRP D 8
REMARK 465 THR D 9
REMARK 465 ALA D 10
REMARK 465 GLU D 11
REMARK 465 ILE D 12
REMARK 465 THR D 13
REMARK 465 PRO D 14
REMARK 465 ASN D 15
REMARK 465 LEU D 16
REMARK 465 HIS D 17
REMARK 465 GLY D 18
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 LEU C 16 CG CD1 CD2
REMARK 470 HIS C 17 CB CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 106 CG CD CE NZ
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 OE1 GLU C 20 O HOH C 203 1.99
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 PHE A 38 -5.81 83.49
REMARK 500 ARG A 68 43.42 -104.39
REMARK 500 ARG A 128 32.06 -84.18
REMARK 500 SER B 36 10.46 -141.65
REMARK 500 ARG B 68 49.00 -109.00
REMARK 500 ARG B 128 37.04 -86.39
REMARK 500 HIS C 17 150.59 160.17
REMARK 500 SER C 84 121.01 -38.01
REMARK 500 LYS C 85 41.26 -79.34
REMARK 500 GLU D 45 39.79 -91.12
REMARK 500 LYS D 104 128.94 -39.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU C 16 HIS C 17 -112.79
REMARK 500 GLY C 18 THR C 19 -55.10
REMARK 500 GLY D 89 ARG D 90 -138.94
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 ARG A 14 0.25 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 C 201 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH D 202 DISTANCE = 6.29 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GLV RELATED DB: PDB
REMARK 900 RELATED ID: 4GN3 RELATED DB: PDB
REMARK 900 RELATED ID: 4GN4 RELATED DB: PDB
REMARK 900 RELATED ID: 4GN5 RELATED DB: PDB
DBREF 4GLA A 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 4GLA B 1 129 UNP P00698 LYSC_CHICK 19 147
DBREF 4GLA C -1 106 PDB 4GLA 4GLA -1 106
DBREF 4GLA D -1 107 PDB 4GLA 4GLA -1 107
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 B 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 B 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 B 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 B 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 B 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 B 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 B 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 B 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 B 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 B 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
SEQRES 1 C 109 GLY SER VAL TYR PRO LYS LYS THR HIS TRP THR ALA GLU
SEQRES 2 C 109 ILE THR PRO ASN LEU HIS GLY THR GLU VAL VAL VAL ALA
SEQRES 3 C 109 GLY TRP VAL ALA SER LEU GLY ASP TYR GLY ARG VAL LYS
SEQRES 4 C 109 ILE VAL LYS VAL SER ASP ARG GLU GLY GLY ALA ALA VAL
SEQRES 5 C 109 PRO VAL TYR LEU GLU ALA GLY LYS THR PRO ASP HIS LEU
SEQRES 6 C 109 PHE LYS VAL PHE ALA GLU LEU SER ARG GLU ASP VAL VAL
SEQRES 7 C 109 VAL ILE LYS GLY ILE VAL GLU ALA SER LYS GLY VAL GLY
SEQRES 8 C 109 ARG GLY VAL GLU ILE PHE PRO SER GLU ILE TRP ILE LEU
SEQRES 9 C 109 ASN LYS ALA LYS ALA
SEQRES 1 D 109 GLY SER VAL TYR PRO LYS LYS THR HIS TRP THR ALA GLU
SEQRES 2 D 109 ILE THR PRO ASN LEU HIS GLY THR GLU VAL VAL VAL ALA
SEQRES 3 D 109 GLY TRP VAL ALA SER LEU GLY ASP TYR GLY ARG VAL LYS
SEQRES 4 D 109 ILE VAL LYS VAL SER ASP ARG GLU GLY GLY ALA ALA VAL
SEQRES 5 D 109 PRO VAL TYR LEU GLU ALA GLY LYS THR PRO ASP HIS LEU
SEQRES 6 D 109 PHE LYS VAL PHE ALA GLU LEU SER ARG GLU ASP VAL VAL
SEQRES 7 D 109 VAL ILE LYS GLY ILE VAL GLU ALA SER LYS GLY VAL GLY
SEQRES 8 D 109 ARG GLY VAL GLU ILE PHE PRO SER GLU ILE TRP ILE LEU
SEQRES 9 D 109 ASN LYS ALA LYS ALA
FORMUL 5 HOH *45(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 ASN A 19 TYR A 23 5 5
HELIX 3 3 SER A 24 ASN A 37 1 14
HELIX 4 4 PRO A 79 SER A 85 5 7
HELIX 5 5 ILE A 88 SER A 100 1 13
HELIX 6 6 ASN A 103 ALA A 107 5 5
HELIX 7 7 TRP A 108 CYS A 115 1 8
HELIX 8 8 ASP A 119 ILE A 124 5 6
HELIX 9 9 GLY B 4 HIS B 15 1 12
HELIX 10 10 ASN B 19 TYR B 23 5 5
HELIX 11 11 SER B 24 ASN B 37 1 14
HELIX 12 12 PRO B 79 SER B 85 5 7
HELIX 13 13 ILE B 88 SER B 100 1 13
HELIX 14 14 ASN B 103 ALA B 107 5 5
HELIX 15 15 TRP B 108 CYS B 115 1 8
HELIX 16 16 ASP B 119 ILE B 124 5 6
HELIX 17 17 ASP C 60 ALA C 67 1 8
HELIX 18 18 PRO D 60 ALA D 68 1 9
SHEET 1 A 3 THR A 43 ARG A 45 0
SHEET 2 A 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 A 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SHEET 1 B 3 THR B 43 ARG B 45 0
SHEET 2 B 3 THR B 51 TYR B 53 -1 O ASP B 52 N ASN B 44
SHEET 3 B 3 ILE B 58 ASN B 59 -1 O ILE B 58 N TYR B 53
SHEET 1 C 6 GLU C 20 ASP C 32 0
SHEET 2 C 6 VAL C 36 SER C 42 -1 O LYS C 40 N ALA C 28
SHEET 3 C 6 VAL C 49 GLU C 54 -1 O LEU C 53 N LYS C 37
SHEET 4 C 6 VAL C 91 ILE C 100 1 O ILE C 93 N TYR C 52
SHEET 5 C 6 VAL C 74 ALA C 83 -1 N GLU C 82 O GLU C 92
SHEET 6 C 6 GLU C 20 ASP C 32 -1 N GLY C 25 O VAL C 75
SHEET 1 D 6 GLU D 20 ASP D 32 0
SHEET 2 D 6 VAL D 36 SER D 42 -1 O LYS D 40 N ALA D 28
SHEET 3 D 6 ALA D 49 GLU D 55 -1 O LEU D 54 N LYS D 37
SHEET 4 D 6 VAL D 92 ILE D 101 1 O ILE D 94 N TYR D 53
SHEET 5 D 6 VAL D 75 ALA D 84 -1 N GLU D 83 O GLU D 93
SHEET 6 D 6 GLU D 20 ASP D 32 -1 N GLY D 25 O VAL D 76
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.06
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.52
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.26
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.07
SSBOND 5 CYS B 6 CYS B 127 1555 1555 2.79
SSBOND 6 CYS B 30 CYS B 115 1555 1555 2.56
SSBOND 7 CYS B 64 CYS B 80 1555 1555 2.41
CISPEP 1 HIS C 17 GLY C 18 0 -12.66
CRYST1 76.759 76.759 166.344 90.00 90.00 90.00 P 41 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 0.013028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006012 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
