HEADER IMMUNE SYSTEM 17-MAR-14 4P5K
TITLE STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: BRIDGING THE GAP
TITLE 2 BETWEEN ALLERGY AND AUTOIMMUNITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 32-214;
COMPND 5 SYNONYM: DP(W3),DP(W4),HLA-SB ALPHA CHAIN,MHC CLASS II DP3-ALPHA,MHC
COMPND 6 CLASS II DPA1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: RAS PEPTIDE,HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP
COMPND 10 BETA 1 CHAIN;
COMPND 11 CHAIN: B, E;
COMPND 12 FRAGMENT: UNP RESIDUES 32-218;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-DPA1, HLA-DP1A, HLASB;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: HLA-DPB1;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MHC, TCR, COMPLEX, HLA, CHRONIC BERYLLIUM DISEASE, ALLERGY,
KEYWDS 2 AUTOIMMUNITY, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,J.S.KIEFT,
AUTHOR 2 M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,S.DAI,J.W.KAPPLER
REVDAT 3 21-MAR-18 4P5K 1 REMARK
REVDAT 2 22-NOV-17 4P5K 1 SOURCE REMARK
REVDAT 1 21-JAN-15 4P5K 0
JRNL AUTH G.M.CLAYTON,Y.WANG,F.CRAWFORD,A.NOVIKOV,B.T.WIMBERLY,
JRNL AUTH 2 J.S.KIEFT,M.T.FALTA,N.A.BOWERMAN,P.MARRACK,A.P.FONTENOT,
JRNL AUTH 3 S.DAI,J.W.KAPPLER
JRNL TITL STRUCTURAL BASIS OF CHRONIC BERYLLIUM DISEASE: LINKING
JRNL TITL 2 ALLERGIC HYPERSENSITIVITY AND AUTOIMMUNITY.
JRNL REF CELL V. 158 132 2014
JRNL REFN ISSN 1097-4172
JRNL PMID 24995984
JRNL DOI 10.1016/J.CELL.2014.04.048
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 24286
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1243
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) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 724
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 39
REMARK 3 BIN FREE R VALUE : 0.4180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : 0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
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): 0.397
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.331
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.305
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6400 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8706 ; 1.626 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 750 ; 7.599 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 360 ;37.097 ;24.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1014 ;21.840 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 38 ;23.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 914 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5080 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; 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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; 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): 3784 ; 0.609 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6146 ; 1.185 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2616 ; 1.732 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2560 ; 2.899 ; 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 : NULL
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 181
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0540 -30.4426 -18.1314
REMARK 3 T TENSOR
REMARK 3 T11: 0.0656 T22: 0.1976
REMARK 3 T33: 0.0872 T12: 0.0121
REMARK 3 T13: 0.0009 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.9910 L22: 1.7754
REMARK 3 L33: 0.9057 L12: -1.0432
REMARK 3 L13: -0.3888 L23: -0.2581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: -0.0164 S13: 0.0348
REMARK 3 S21: -0.0610 S22: -0.1827 S23: 0.0554
REMARK 3 S31: 0.0653 S32: -0.0390 S33: 0.1542
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 3 B 189
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8812 -28.1655 -5.3167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.2575
REMARK 3 T33: 0.1092 T12: -0.0553
REMARK 3 T13: -0.0634 T23: 0.1005
REMARK 3 L TENSOR
REMARK 3 L11: 1.5708 L22: 3.4139
REMARK 3 L33: 1.5096 L12: 0.2573
REMARK 3 L13: -0.9278 L23: 0.7139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0621 S12: -0.4779 S13: -0.0503
REMARK 3 S21: 0.2191 S22: -0.1390 S23: -0.1742
REMARK 3 S31: -0.0230 S32: 0.4011 S33: 0.0769
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 : D 1 D 181
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2423 -2.1799 -39.9001
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.1618
REMARK 3 T33: 0.0917 T12: -0.0145
REMARK 3 T13: 0.0021 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.8451 L22: 2.3842
REMARK 3 L33: 0.2289 L12: 0.9059
REMARK 3 L13: 0.0931 L23: -0.2452
REMARK 3 S TENSOR
REMARK 3 S11: -0.0724 S12: -0.0294 S13: 0.0122
REMARK 3 S21: 0.0654 S22: 0.0718 S23: 0.1896
REMARK 3 S31: 0.0462 S32: -0.0898 S33: 0.0006
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 : E 3 E 189
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9597 -2.2451 -47.5694
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: 0.1116
REMARK 3 T33: 0.0438 T12: 0.0026
REMARK 3 T13: -0.0169 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.0390 L22: 3.5225
REMARK 3 L33: 1.3190 L12: -0.5823
REMARK 3 L13: -0.3434 L23: 0.6104
REMARK 3 S TENSOR
REMARK 3 S11: -0.1488 S12: 0.0822 S13: 0.0640
REMARK 3 S21: 0.0549 S22: 0.1521 S23: -0.0665
REMARK 3 S31: 0.1616 S32: 0.1901 S33: -0.0033
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4P5K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000200739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26282
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 (%) : 92.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <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 (%): 49.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FORMATE AND 25 % PEG
REMARK 280 4000 IN 0.1 M HEPES BUFFER, PH 6.8, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 316K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 91.38950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.36900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.38950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.36900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 GLU A 182
REMARK 465 PRO A 183
REMARK 465 LEU B -10
REMARK 465 VAL B -9
REMARK 465 PRO B -8
REMARK 465 ARG B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 GLY B -2
REMARK 465 GLY B -1
REMARK 465 PRO B 106
REMARK 465 LEU B 107
REMARK 465 GLN B 108
REMARK 465 HIS B 109
REMARK 465 GLU D 182
REMARK 465 PRO D 183
REMARK 465 LEU E -10
REMARK 465 VAL E -9
REMARK 465 PRO E -8
REMARK 465 ARG E -7
REMARK 465 GLY E -6
REMARK 465 SER E -5
REMARK 465 GLY E -4
REMARK 465 GLY E -3
REMARK 465 GLY E -2
REMARK 465 GLY E -1
REMARK 465 PRO E 106
REMARK 465 LEU E 107
REMARK 465 GLN E 108
REMARK 465 HIS E 109
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 PHE B -18 NE2 GLN D 57 1545 2.12
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 LEU D 73 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 HIS E -17 CB - CA - C ANGL. DEV. = -12.4 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 LYS A 2 79.96 71.60
REMARK 500 ARG A 17 -101.19 53.65
REMARK 500 GLU A 28 -13.24 87.97
REMARK 500 ASP A 37 -64.34 -92.17
REMARK 500 HIS A 79 41.06 77.09
REMARK 500 LEU A 136 -179.22 -65.88
REMARK 500 TYR A 143 -4.61 78.42
REMARK 500 SER A 144 -166.66 -72.08
REMARK 500 ALA A 180 97.43 -46.15
REMARK 500 ASN B 19 87.86 -14.10
REMARK 500 ASN B 31 83.39 31.89
REMARK 500 ARG B 32 -3.30 67.03
REMARK 500 GLN B 62 21.48 173.15
REMARK 500 LYS B 63 -30.32 -27.70
REMARK 500 ARG B 75 -96.88 -109.32
REMARK 500 THR B 88 -81.35 -130.14
REMARK 500 SER B 102 41.05 -167.13
REMARK 500 ASN B 111 94.12 145.74
REMARK 500 ASN B 132 58.97 30.41
REMARK 500 THR B 162 82.44 -154.71
REMARK 500 GLN B 165 -77.13 -157.63
REMARK 500 ALA B 188 45.07 -101.46
REMARK 500 LYS D 2 122.33 72.03
REMARK 500 ARG D 17 -110.43 44.97
REMARK 500 ASP D 27 49.50 26.13
REMARK 500 GLU D 28 3.80 82.63
REMARK 500 SER D 77 5.30 -67.68
REMARK 500 LEU D 99 126.01 -23.20
REMARK 500 TRP D 168 -24.16 -38.38
REMARK 500 PHE E 18 -90.65 -136.25
REMARK 500 ASN E 31 95.72 8.92
REMARK 500 ARG E 32 -10.13 59.80
REMARK 500 LEU E 66 -33.68 -38.65
REMARK 500 ARG E 75 -96.67 -102.02
REMARK 500 PRO E 86 -71.30 -53.08
REMARK 500 THR E 88 -67.99 -96.99
REMARK 500 LYS E 103 10.59 -177.05
REMARK 500 ASN E 111 101.52 152.31
REMARK 500 GLN E 165 -73.25 130.59
REMARK 500 SER E 180 110.59 -160.67
REMARK 500 ALA E 188 44.20 -71.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P4K RELATED DB: PDB
REMARK 900 RELATED ID: 4P4R RELATED DB: PDB
REMARK 900 RELATED ID: 4P57 RELATED DB: PDB
DBREF 4P5K A 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5K B -25 -14 PDB 4P5K 4P5K -25 -14
DBREF 4P5K B 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
DBREF 4P5K D 1 183 UNP P20036 DPA1_HUMAN 32 214
DBREF 4P5K E -25 -14 PDB 4P5K 4P5K -25 -14
DBREF 4P5K E 3 189 UNP Q5EP54 Q5EP54_HUMAN 32 218
SEQADV 4P5K GLY B -13 PDB LINKER
SEQADV 4P5K GLY B -12 PDB LINKER
SEQADV 4P5K SER B -11 PDB LINKER
SEQADV 4P5K LEU B -10 PDB LINKER
SEQADV 4P5K VAL B -9 PDB LINKER
SEQADV 4P5K PRO B -8 PDB LINKER
SEQADV 4P5K ARG B -7 PDB LINKER
SEQADV 4P5K GLY B -6 PDB LINKER
SEQADV 4P5K SER B -5 PDB LINKER
SEQADV 4P5K GLY B -4 PDB LINKER
SEQADV 4P5K GLY B -3 PDB LINKER
SEQADV 4P5K GLY B -2 PDB LINKER
SEQADV 4P5K GLY B -1 PDB LINKER
SEQADV 4P5K SER B 3 UNP Q5EP54 THR 32 VARIANT
SEQADV 4P5K GLY E -13 PDB LINKER
SEQADV 4P5K GLY E -12 PDB LINKER
SEQADV 4P5K SER E -11 PDB LINKER
SEQADV 4P5K LEU E -10 PDB LINKER
SEQADV 4P5K VAL E -9 PDB LINKER
SEQADV 4P5K PRO E -8 PDB LINKER
SEQADV 4P5K ARG E -7 PDB LINKER
SEQADV 4P5K GLY E -6 PDB LINKER
SEQADV 4P5K SER E -5 PDB LINKER
SEQADV 4P5K GLY E -4 PDB LINKER
SEQADV 4P5K GLY E -3 PDB LINKER
SEQADV 4P5K GLY E -2 PDB LINKER
SEQADV 4P5K GLY E -1 PDB LINKER
SEQADV 4P5K SER E 3 UNP Q5EP54 THR 32 VARIANT
SEQRES 1 A 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 A 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 A 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 A 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 A 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 A 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 A 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 A 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 A 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 A 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 A 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 A 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 A 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 A 183 PRO
SEQRES 1 B 212 ASN LYS PHE ASP THR GLN LEU PHE HIS THR ILE THR GLY
SEQRES 2 B 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 B 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 B 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 B 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 B 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 B 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 B 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 B 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 B 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 B 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 B 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 B 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 B 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 B 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 B 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 B 212 TRP LYS ALA GLN
SEQRES 1 D 183 ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL
SEQRES 2 D 183 GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE
SEQRES 3 D 183 ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS
SEQRES 4 D 183 GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE
SEQRES 5 D 183 SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE
SEQRES 6 D 183 LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN
SEQRES 7 D 183 HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL
SEQRES 8 D 183 PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR
SEQRES 9 D 183 LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU
SEQRES 10 D 183 ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU
SEQRES 11 D 183 GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR
SEQRES 12 D 183 SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER
SEQRES 13 D 183 ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 D 183 LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN GLU
SEQRES 15 D 183 PRO
SEQRES 1 E 212 ASN LYS PHE ASP THR GLN LEU PHE HIS THR ILE THR GLY
SEQRES 2 E 212 GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER
SEQRES 3 E 212 PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR
SEQRES 4 E 212 ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE
SEQRES 5 E 212 TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL
SEQRES 6 E 212 GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP
SEQRES 7 E 212 GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU
SEQRES 8 E 212 GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR
SEQRES 9 E 212 GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN
SEQRES 10 E 212 PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU
SEQRES 11 E 212 GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE
SEQRES 12 E 212 TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY
SEQRES 13 E 212 GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE
SEQRES 14 E 212 ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU
SEQRES 15 E 212 GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN
SEQRES 16 E 212 VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU
SEQRES 17 E 212 TRP LYS ALA GLN
HELIX 1 AA1 LEU A 45 GLN A 50 1 6
HELIX 2 AA2 ALA A 56 ASN A 78 1 23
HELIX 3 AA3 GLY B 52 ASN B 60 1 9
HELIX 4 AA4 GLN B 62 VAL B 72 1 11
HELIX 5 AA5 ARG B 75 GLY B 85 1 11
HELIX 6 AA6 PRO B 86 THR B 88 5 3
HELIX 7 AA7 LEU D 45 PHE D 52 1 8
HELIX 8 AA8 ALA D 56 SER D 77 1 22
HELIX 9 AA9 THR E 49 LEU E 51 5 3
HELIX 10 AB1 GLY E 52 ASN E 60 1 9
HELIX 11 AB2 GLN E 62 ALA E 71 1 10
HELIX 12 AB3 ARG E 75 GLN E 90 1 16
SHEET 1 AA1 8 GLU A 40 TRP A 43 0
SHEET 2 AA1 8 ASP A 29 ASP A 35 -1 N TYR A 33 O VAL A 42
SHEET 3 AA1 8 GLY A 20 PHE A 26 -1 N PHE A 24 O MET A 31
SHEET 4 AA1 8 VAL A 6 GLN A 14 -1 N PHE A 12 O GLU A 21
SHEET 5 AA1 8 LEU B 8 TYR B 16 -1 O CYS B 15 N SER A 7
SHEET 6 AA1 8 ARG B 23 TYR B 30 -1 O ILE B 29 N GLN B 10
SHEET 7 AA1 8 GLU B 33 ASP B 39 -1 O PHE B 38 N GLU B 26
SHEET 8 AA1 8 GLU B 44 ALA B 47 -1 O ARG B 46 N ARG B 37
SHEET 1 AA2 4 GLU A 88 PRO A 93 0
SHEET 2 AA2 4 ASN A 103 PHE A 112 -1 O ILE A 106 N PHE A 92
SHEET 3 AA2 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA2 4 VAL A 132 GLU A 134 -1 N ALA A 133 O TYR A 150
SHEET 1 AA3 4 GLU A 88 PRO A 93 0
SHEET 2 AA3 4 ASN A 103 PHE A 112 -1 O ILE A 106 N PHE A 92
SHEET 3 AA3 4 PHE A 145 PHE A 153 -1 O LEU A 151 N LEU A 105
SHEET 4 AA3 4 LEU A 138 PRO A 139 -1 N LEU A 138 O HIS A 146
SHEET 1 AA4 4 GLU A 126 LEU A 127 0
SHEET 2 AA4 4 ASN A 118 CYS A 123 -1 N CYS A 123 O GLU A 126
SHEET 3 AA4 4 PHE A 160 GLU A 166 -1 O ARG A 164 N THR A 120
SHEET 4 AA4 4 LEU A 174 GLU A 179 -1 O LEU A 174 N VAL A 165
SHEET 1 AA5 4 ARG B 96 SER B 102 0
SHEET 2 AA5 4 LEU B 112 PHE B 120 -1 O THR B 118 N ARG B 96
SHEET 3 AA5 4 PHE B 153 GLU B 160 -1 O ILE B 155 N VAL B 117
SHEET 4 AA5 4 VAL B 140 SER B 142 -1 N VAL B 141 O MET B 158
SHEET 1 AA6 4 ARG B 96 SER B 102 0
SHEET 2 AA6 4 LEU B 112 PHE B 120 -1 O THR B 118 N ARG B 96
SHEET 3 AA6 4 PHE B 153 GLU B 160 -1 O ILE B 155 N VAL B 117
SHEET 4 AA6 4 ILE B 146 ARG B 147 -1 N ILE B 146 O GLN B 154
SHEET 1 AA7 4 GLN B 134 GLU B 135 0
SHEET 2 AA7 4 GLN B 126 LEU B 131 -1 N LEU B 131 O GLN B 134
SHEET 3 AA7 4 ASP B 167 GLU B 174 -1 O THR B 170 N PHE B 130
SHEET 4 AA7 4 VAL B 182 ALA B 188 -1 O ALA B 188 N ASP B 167
SHEET 1 AA8 8 GLU D 40 TRP D 43 0
SHEET 2 AA8 8 ASP D 29 ASP D 35 -1 N TYR D 33 O VAL D 42
SHEET 3 AA8 8 GLY D 20 PHE D 26 -1 N PHE D 24 O MET D 31
SHEET 4 AA8 8 HIS D 5 GLN D 14 -1 N THR D 8 O GLU D 25
SHEET 5 AA8 8 LEU E 8 ALA E 17 -1 O ALA E 17 N HIS D 5
SHEET 6 AA8 8 GLN E 22 TYR E 30 -1 O LEU E 25 N GLU E 14
SHEET 7 AA8 8 GLU E 33 ASP E 39 -1 O GLU E 33 N TYR E 30
SHEET 8 AA8 8 PHE E 45 ALA E 47 -1 O ARG E 46 N ARG E 37
SHEET 1 AA9 4 GLU D 88 PRO D 93 0
SHEET 2 AA9 4 ASN D 103 PHE D 112 -1 O ILE D 106 N PHE D 92
SHEET 3 AA9 4 PHE D 145 PHE D 153 -1 O PHE D 153 N ASN D 103
SHEET 4 AA9 4 VAL D 132 GLU D 134 -1 N ALA D 133 O TYR D 150
SHEET 1 AB1 4 GLU D 88 PRO D 93 0
SHEET 2 AB1 4 ASN D 103 PHE D 112 -1 O ILE D 106 N PHE D 92
SHEET 3 AB1 4 PHE D 145 PHE D 153 -1 O PHE D 153 N ASN D 103
SHEET 4 AB1 4 LEU D 138 PRO D 139 -1 N LEU D 138 O HIS D 146
SHEET 1 AB2 4 GLU D 126 VAL D 128 0
SHEET 2 AB2 4 ASN D 118 CYS D 123 -1 N CYS D 123 O GLU D 126
SHEET 3 AB2 4 TYR D 161 GLU D 166 -1 O ARG D 164 N THR D 120
SHEET 4 AB2 4 LEU D 174 TRP D 178 -1 O TRP D 178 N TYR D 161
SHEET 1 AB3 4 ARG E 96 SER E 100 0
SHEET 2 AB3 4 LEU E 112 PHE E 120 -1 O VAL E 114 N SER E 100
SHEET 3 AB3 4 PHE E 153 GLU E 160 -1 O VAL E 157 N CYS E 115
SHEET 4 AB3 4 VAL E 140 SER E 142 -1 N VAL E 141 O MET E 158
SHEET 1 AB4 4 ARG E 96 SER E 100 0
SHEET 2 AB4 4 LEU E 112 PHE E 120 -1 O VAL E 114 N SER E 100
SHEET 3 AB4 4 PHE E 153 GLU E 160 -1 O VAL E 157 N CYS E 115
SHEET 4 AB4 4 ILE E 146 ARG E 147 -1 N ILE E 146 O GLN E 154
SHEET 1 AB5 4 GLN E 134 GLU E 136 0
SHEET 2 AB5 4 GLN E 126 LEU E 131 -1 N TRP E 129 O GLU E 136
SHEET 3 AB5 4 VAL E 168 GLU E 174 -1 O GLN E 172 N ARG E 128
SHEET 4 AB5 4 VAL E 182 LYS E 187 -1 O TRP E 186 N TYR E 169
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.01
SSBOND 2 CYS B 15 CYS B 77 1555 1555 2.07
SSBOND 3 CYS B 115 CYS B 171 1555 1555 2.04
SSBOND 4 CYS D 107 CYS D 163 1555 1555 2.07
SSBOND 5 CYS E 15 CYS E 77 1555 1555 2.06
SSBOND 6 CYS E 115 CYS E 171 1555 1555 2.05
CISPEP 1 PHE A 113 PRO A 114 0 -1.99
CISPEP 2 TYR B 121 PRO B 122 0 6.85
CISPEP 3 PHE D 113 PRO D 114 0 4.09
CISPEP 4 TYR E 121 PRO E 122 0 -2.00
CRYST1 182.779 68.738 71.133 90.00 105.72 90.00 C 1 2 1 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 0.005471 0.000000 0.001540 0.00000
SCALE2 0.000000 0.014548 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014604 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
