HEADER TRANSFERASE 12-NOV-07 3BCE
TITLE CRYSTAL STRUCTURE OF THE ERBB4 KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-4;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: ERBB4 KINASE DOMAIN (UNP RESIDUES 702-1029);
COMPND 5 SYNONYM: P180ERBB4, TYROSINE KINASE-TYPE CELL SURFACE RECEPTOR HER4;
COMPND 6 EC: 2.7.10.1;
COMPND 7 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: ERBB4, HER4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS ACTIVE CONFORMATION, ATP-BINDING, GLYCOPROTEIN, KINASE, MEMBRANE,
KEYWDS 2 NUCLEOTIDE-BINDING, PHOSPHORYLATION, RECEPTOR, TRANSFERASE,
KEYWDS 3 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.QIU
REVDAT 6 21-FEB-24 3BCE 1 REMARK
REVDAT 5 25-OCT-17 3BCE 1 REMARK
REVDAT 4 13-JUL-11 3BCE 1 VERSN
REVDAT 3 24-FEB-09 3BCE 1 VERSN
REVDAT 2 25-MAR-08 3BCE 1 JRNL
REVDAT 1 12-FEB-08 3BCE 0
JRNL AUTH C.QIU,M.K.TARRANT,S.H.CHOI,A.SATHYAMURTHY,R.BOSE,S.BANJADE,
JRNL AUTH 2 A.PAL,W.G.BORNMANN,M.A.LEMMON,P.A.COLE,D.J.LEAHY
JRNL TITL MECHANISM OF ACTIVATION AND INHIBITION OF THE HER4/ERBB4
JRNL TITL 2 KINASE.
JRNL REF STRUCTURE V. 16 460 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18334220
JRNL DOI 10.1016/J.STR.2007.12.016
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34814
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1750
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2438
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6865
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 216
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) : 19.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90000
REMARK 3 B22 (A**2) : 0.90000
REMARK 3 B33 (A**2) : -1.36000
REMARK 3 B12 (A**2) : 0.45000
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): 0.612
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.296
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.619
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7031 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9500 ; 1.297 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 848 ; 8.598 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;35.334 ;23.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1295 ;17.553 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;19.282 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1059 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5167 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3180 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4655 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 272 ; 0.207 ; 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): 101 ; 0.238 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.167 ; 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): 4385 ; 0.471 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6927 ; 0.767 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3000 ; 1.120 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2573 ; 1.815 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 678 A 965 4
REMARK 3 1 B 678 B 965 4
REMARK 3 1 C 678 C 965 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2259 ; 0.430 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2259 ; 0.480 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2259 ; 0.370 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2259 ; 0.390 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2259 ; 0.380 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2259 ; 0.400 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
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 678 A 737
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4140 15.8472 30.1679
REMARK 3 T TENSOR
REMARK 3 T11: 0.1281 T22: 0.0347
REMARK 3 T33: -0.0387 T12: -0.0379
REMARK 3 T13: -0.0406 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.3871 L22: 7.5498
REMARK 3 L33: 2.4336 L12: 0.8120
REMARK 3 L13: 0.3687 L23: -0.1180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: -0.2190 S13: 0.1729
REMARK 3 S21: 0.0297 S22: 0.1080 S23: 0.1043
REMARK 3 S31: -0.0058 S32: -0.0112 S33: -0.0236
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 : A 738 A 846
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0154 11.4382 16.0801
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.0670
REMARK 3 T33: 0.0492 T12: -0.0657
REMARK 3 T13: -0.0099 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.3068 L22: 0.8412
REMARK 3 L33: 3.6086 L12: -0.1260
REMARK 3 L13: 1.0635 L23: -0.1558
REMARK 3 S TENSOR
REMARK 3 S11: -0.1186 S12: 0.0859 S13: -0.0159
REMARK 3 S21: 0.0468 S22: 0.0257 S23: -0.0972
REMARK 3 S31: -0.0566 S32: 0.3223 S33: 0.0929
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 : A 847 A 965
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4092 9.0557 4.5834
REMARK 3 T TENSOR
REMARK 3 T11: 0.0914 T22: 0.0428
REMARK 3 T33: 0.0155 T12: -0.0527
REMARK 3 T13: -0.0274 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 2.8078 L22: 1.4825
REMARK 3 L33: 3.4039 L12: 0.0124
REMARK 3 L13: 0.1099 L23: 0.1049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: -0.0139 S13: -0.1139
REMARK 3 S21: 0.0134 S22: 0.0346 S23: 0.0825
REMARK 3 S31: -0.0067 S32: -0.0848 S33: -0.0184
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 : B 678 B 750
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5616 33.0773 65.5748
REMARK 3 T TENSOR
REMARK 3 T11: -0.0060 T22: 0.0073
REMARK 3 T33: -0.0868 T12: 0.0301
REMARK 3 T13: 0.0146 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 6.0449 L22: 2.8575
REMARK 3 L33: 2.8880 L12: -2.1790
REMARK 3 L13: -0.2559 L23: 0.4465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.1493 S13: 0.1377
REMARK 3 S21: 0.0759 S22: 0.0395 S23: -0.0862
REMARK 3 S31: 0.0580 S32: 0.0243 S33: -0.0589
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 751 B 846
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7857 38.0189 50.5291
REMARK 3 T TENSOR
REMARK 3 T11: 0.0343 T22: -0.0304
REMARK 3 T33: 0.0496 T12: 0.0249
REMARK 3 T13: -0.0156 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.9438 L22: 0.8630
REMARK 3 L33: 3.6703 L12: -0.0323
REMARK 3 L13: -0.2783 L23: -0.5068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: -0.1323 S13: -0.0875
REMARK 3 S21: -0.0753 S22: 0.0922 S23: 0.0630
REMARK 3 S31: 0.1673 S32: 0.0181 S33: -0.0906
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 847 B 967
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3927 51.0852 40.3243
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: -0.0186
REMARK 3 T33: 0.0154 T12: 0.0273
REMARK 3 T13: -0.0087 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.9258 L22: 3.5711
REMARK 3 L33: 1.9216 L12: 0.0909
REMARK 3 L13: -0.4982 L23: 0.1673
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: -0.0669 S13: 0.1246
REMARK 3 S21: 0.0003 S22: 0.1021 S23: -0.0054
REMARK 3 S31: -0.0778 S32: 0.0684 S33: -0.1089
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 678 C 708
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5849 42.8090 4.6601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0035 T22: -0.0136
REMARK 3 T33: -0.0648 T12: -0.0316
REMARK 3 T13: -0.0017 T23: 0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 7.7695 L22: 1.7634
REMARK 3 L33: 2.4821 L12: 2.3420
REMARK 3 L13: 1.7605 L23: 0.9999
REMARK 3 S TENSOR
REMARK 3 S11: 0.1746 S12: -0.0357 S13: -0.1380
REMARK 3 S21: 0.0377 S22: -0.1321 S23: -0.1296
REMARK 3 S31: -0.1373 S32: 0.0969 S33: -0.0425
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 709 C 846
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0754 38.3852 15.3062
REMARK 3 T TENSOR
REMARK 3 T11: -0.0020 T22: -0.0247
REMARK 3 T33: 0.0348 T12: -0.0025
REMARK 3 T13: 0.0023 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.9603 L22: 1.5767
REMARK 3 L33: 3.3610 L12: 0.2867
REMARK 3 L13: 0.2597 L23: -0.7955
REMARK 3 S TENSOR
REMARK 3 S11: -0.0583 S12: 0.0868 S13: 0.0267
REMARK 3 S21: 0.0286 S22: 0.0803 S23: 0.0146
REMARK 3 S31: -0.1467 S32: 0.0370 S33: -0.0220
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 847 C 965
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3192 24.0445 29.6079
REMARK 3 T TENSOR
REMARK 3 T11: 0.0132 T22: -0.0371
REMARK 3 T33: 0.0097 T12: -0.0415
REMARK 3 T13: 0.0095 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.2170 L22: 2.4704
REMARK 3 L33: 2.3542 L12: -0.3143
REMARK 3 L13: 0.0320 L23: 0.1225
REMARK 3 S TENSOR
REMARK 3 S11: -0.0427 S12: 0.0161 S13: -0.0525
REMARK 3 S21: -0.0635 S22: 0.0950 S23: 0.0452
REMARK 3 S31: -0.0504 S32: 0.0613 S33: -0.0523
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3BCE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045347.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97893
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 34855
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.45700
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: NULL
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 (%): 46.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.1 M TRIS, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.00533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.00267
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 677
REMARK 465 THR A 732
REMARK 465 GLY A 733
REMARK 465 ASP A 853
REMARK 465 GLY A 854
REMARK 465 ARG A 967
REMARK 465 MET A 968
REMARK 465 LYS A 969
REMARK 465 LEU A 970
REMARK 465 PRO A 971
REMARK 465 SER A 972
REMARK 465 PRO A 973
REMARK 465 ASN A 974
REMARK 465 ASP A 975
REMARK 465 SER A 976
REMARK 465 LYS A 977
REMARK 465 PHE A 978
REMARK 465 PHE A 979
REMARK 465 GLN A 980
REMARK 465 ASN A 981
REMARK 465 LEU A 982
REMARK 465 LEU A 983
REMARK 465 ASP A 984
REMARK 465 GLU A 985
REMARK 465 GLU A 986
REMARK 465 ASP A 987
REMARK 465 LEU A 988
REMARK 465 GLU A 989
REMARK 465 ASP A 990
REMARK 465 MET A 991
REMARK 465 MET A 992
REMARK 465 ASP A 993
REMARK 465 ALA A 994
REMARK 465 GLU A 995
REMARK 465 GLU A 996
REMARK 465 TYR A 997
REMARK 465 LEU A 998
REMARK 465 VAL A 999
REMARK 465 PRO A 1000
REMARK 465 GLN A 1001
REMARK 465 ALA A 1002
REMARK 465 PHE A 1003
REMARK 465 ASN A 1004
REMARK 465 GLY B 677
REMARK 465 THR B 732
REMARK 465 GLY B 733
REMARK 465 PRO B 734
REMARK 465 ASP B 853
REMARK 465 GLY B 854
REMARK 465 LYS B 969
REMARK 465 LEU B 970
REMARK 465 PRO B 971
REMARK 465 SER B 972
REMARK 465 PRO B 973
REMARK 465 ASN B 974
REMARK 465 ASP B 975
REMARK 465 SER B 976
REMARK 465 LYS B 977
REMARK 465 PHE B 978
REMARK 465 PHE B 979
REMARK 465 GLN B 980
REMARK 465 ASN B 981
REMARK 465 LEU B 982
REMARK 465 LEU B 983
REMARK 465 ASP B 984
REMARK 465 GLU B 985
REMARK 465 GLU B 986
REMARK 465 ASP B 987
REMARK 465 LEU B 988
REMARK 465 GLU B 989
REMARK 465 ASP B 990
REMARK 465 MET B 991
REMARK 465 MET B 992
REMARK 465 ASP B 993
REMARK 465 ALA B 994
REMARK 465 GLU B 995
REMARK 465 GLU B 996
REMARK 465 TYR B 997
REMARK 465 LEU B 998
REMARK 465 VAL B 999
REMARK 465 PRO B 1000
REMARK 465 GLN B 1001
REMARK 465 ALA B 1002
REMARK 465 PHE B 1003
REMARK 465 ASN B 1004
REMARK 465 GLY C 677
REMARK 465 GLY C 845
REMARK 465 GLY C 854
REMARK 465 ASP C 966
REMARK 465 ARG C 967
REMARK 465 MET C 968
REMARK 465 LYS C 969
REMARK 465 LEU C 970
REMARK 465 PRO C 971
REMARK 465 SER C 972
REMARK 465 PRO C 973
REMARK 465 ASN C 974
REMARK 465 ASP C 975
REMARK 465 SER C 976
REMARK 465 LYS C 977
REMARK 465 PHE C 978
REMARK 465 PHE C 979
REMARK 465 GLN C 980
REMARK 465 ASN C 981
REMARK 465 LEU C 982
REMARK 465 LEU C 983
REMARK 465 ASP C 984
REMARK 465 GLU C 985
REMARK 465 GLU C 986
REMARK 465 ASP C 987
REMARK 465 LEU C 988
REMARK 465 GLU C 989
REMARK 465 ASP C 990
REMARK 465 MET C 991
REMARK 465 MET C 992
REMARK 465 ASP C 993
REMARK 465 ALA C 994
REMARK 465 GLU C 995
REMARK 465 GLU C 996
REMARK 465 TYR C 997
REMARK 465 LEU C 998
REMARK 465 VAL C 999
REMARK 465 PRO C 1000
REMARK 465 GLN C 1001
REMARK 465 ALA C 1002
REMARK 465 PHE C 1003
REMARK 465 ASN C 1004
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 785 CG CD OE1 OE2
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 ARG A 817 -10.91 71.02
REMARK 500 ASP A 818 36.47 -143.64
REMARK 500 TYR A 896 65.48 34.86
REMARK 500 ARG B 817 -8.26 73.77
REMARK 500 ASP B 818 43.04 -145.34
REMARK 500 ASP B 955 66.17 -151.20
REMARK 500 LYS C 787 -67.20 -16.13
REMARK 500 ARG C 817 -9.03 76.29
REMARK 500 ASP C 818 43.09 -143.32
REMARK 500 ASP C 836 58.98 72.61
REMARK 500 ALA C 852 136.33 -24.63
REMARK 500 ASP C 935 98.53 -67.40
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 B 759 GLY B 760 138.77
REMARK 500 ALA C 852 ASP C 853 145.10
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 MN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BBT RELATED DB: PDB
REMARK 900 RELATED ID: 3BBW RELATED DB: PDB
DBREF 3BCE A 677 1004 UNP Q15303 ERBB4_HUMAN 702 1029
DBREF 3BCE B 677 1004 UNP Q15303 ERBB4_HUMAN 702 1029
DBREF 3BCE C 677 1004 UNP Q15303 ERBB4_HUMAN 702 1029
SEQRES 1 A 328 GLY THR ALA PRO ASN GLN ALA GLN LEU ARG ILE LEU LYS
SEQRES 2 A 328 GLU THR GLU LEU LYS ARG VAL LYS VAL LEU GLY SER GLY
SEQRES 3 A 328 ALA PHE GLY THR VAL TYR LYS GLY ILE TRP VAL PRO GLU
SEQRES 4 A 328 GLY GLU THR VAL LYS ILE PRO VAL ALA ILE LYS ILE LEU
SEQRES 5 A 328 ASN GLU THR THR GLY PRO LYS ALA ASN VAL GLU PHE MET
SEQRES 6 A 328 ASP GLU ALA LEU ILE MET ALA SER MET ASP HIS PRO HIS
SEQRES 7 A 328 LEU VAL ARG LEU LEU GLY VAL CYS LEU SER PRO THR ILE
SEQRES 8 A 328 GLN LEU VAL THR GLN LEU MET PRO HIS GLY CYS LEU LEU
SEQRES 9 A 328 GLU TYR VAL HIS GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 A 328 LEU LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 A 328 MET TYR LEU GLU GLU ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 A 328 ALA ALA ARG ASN VAL LEU VAL LYS SER PRO ASN HIS VAL
SEQRES 13 A 328 LYS ILE THR ASP PHE GLY LEU ALA ARG LEU LEU GLU GLY
SEQRES 14 A 328 ASP GLU LYS GLU TYR ASN ALA ASP GLY GLY LYS MET PRO
SEQRES 15 A 328 ILE LYS TRP MET ALA LEU GLU CYS ILE HIS TYR ARG LYS
SEQRES 16 A 328 PHE THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 A 328 ILE TRP GLU LEU MET THR PHE GLY GLY LYS PRO TYR ASP
SEQRES 18 A 328 GLY ILE PRO THR ARG GLU ILE PRO ASP LEU LEU GLU LYS
SEQRES 19 A 328 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 A 328 VAL TYR MET VAL MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 A 328 ASP SER ARG PRO LYS PHE LYS GLU LEU ALA ALA GLU PHE
SEQRES 22 A 328 SER ARG MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 A 328 GLN GLY ASP ASP ARG MET LYS LEU PRO SER PRO ASN ASP
SEQRES 24 A 328 SER LYS PHE PHE GLN ASN LEU LEU ASP GLU GLU ASP LEU
SEQRES 25 A 328 GLU ASP MET MET ASP ALA GLU GLU TYR LEU VAL PRO GLN
SEQRES 26 A 328 ALA PHE ASN
SEQRES 1 B 328 GLY THR ALA PRO ASN GLN ALA GLN LEU ARG ILE LEU LYS
SEQRES 2 B 328 GLU THR GLU LEU LYS ARG VAL LYS VAL LEU GLY SER GLY
SEQRES 3 B 328 ALA PHE GLY THR VAL TYR LYS GLY ILE TRP VAL PRO GLU
SEQRES 4 B 328 GLY GLU THR VAL LYS ILE PRO VAL ALA ILE LYS ILE LEU
SEQRES 5 B 328 ASN GLU THR THR GLY PRO LYS ALA ASN VAL GLU PHE MET
SEQRES 6 B 328 ASP GLU ALA LEU ILE MET ALA SER MET ASP HIS PRO HIS
SEQRES 7 B 328 LEU VAL ARG LEU LEU GLY VAL CYS LEU SER PRO THR ILE
SEQRES 8 B 328 GLN LEU VAL THR GLN LEU MET PRO HIS GLY CYS LEU LEU
SEQRES 9 B 328 GLU TYR VAL HIS GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 B 328 LEU LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 B 328 MET TYR LEU GLU GLU ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 B 328 ALA ALA ARG ASN VAL LEU VAL LYS SER PRO ASN HIS VAL
SEQRES 13 B 328 LYS ILE THR ASP PHE GLY LEU ALA ARG LEU LEU GLU GLY
SEQRES 14 B 328 ASP GLU LYS GLU TYR ASN ALA ASP GLY GLY LYS MET PRO
SEQRES 15 B 328 ILE LYS TRP MET ALA LEU GLU CYS ILE HIS TYR ARG LYS
SEQRES 16 B 328 PHE THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 B 328 ILE TRP GLU LEU MET THR PHE GLY GLY LYS PRO TYR ASP
SEQRES 18 B 328 GLY ILE PRO THR ARG GLU ILE PRO ASP LEU LEU GLU LYS
SEQRES 19 B 328 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 B 328 VAL TYR MET VAL MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 B 328 ASP SER ARG PRO LYS PHE LYS GLU LEU ALA ALA GLU PHE
SEQRES 22 B 328 SER ARG MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 B 328 GLN GLY ASP ASP ARG MET LYS LEU PRO SER PRO ASN ASP
SEQRES 24 B 328 SER LYS PHE PHE GLN ASN LEU LEU ASP GLU GLU ASP LEU
SEQRES 25 B 328 GLU ASP MET MET ASP ALA GLU GLU TYR LEU VAL PRO GLN
SEQRES 26 B 328 ALA PHE ASN
SEQRES 1 C 328 GLY THR ALA PRO ASN GLN ALA GLN LEU ARG ILE LEU LYS
SEQRES 2 C 328 GLU THR GLU LEU LYS ARG VAL LYS VAL LEU GLY SER GLY
SEQRES 3 C 328 ALA PHE GLY THR VAL TYR LYS GLY ILE TRP VAL PRO GLU
SEQRES 4 C 328 GLY GLU THR VAL LYS ILE PRO VAL ALA ILE LYS ILE LEU
SEQRES 5 C 328 ASN GLU THR THR GLY PRO LYS ALA ASN VAL GLU PHE MET
SEQRES 6 C 328 ASP GLU ALA LEU ILE MET ALA SER MET ASP HIS PRO HIS
SEQRES 7 C 328 LEU VAL ARG LEU LEU GLY VAL CYS LEU SER PRO THR ILE
SEQRES 8 C 328 GLN LEU VAL THR GLN LEU MET PRO HIS GLY CYS LEU LEU
SEQRES 9 C 328 GLU TYR VAL HIS GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 C 328 LEU LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 C 328 MET TYR LEU GLU GLU ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 C 328 ALA ALA ARG ASN VAL LEU VAL LYS SER PRO ASN HIS VAL
SEQRES 13 C 328 LYS ILE THR ASP PHE GLY LEU ALA ARG LEU LEU GLU GLY
SEQRES 14 C 328 ASP GLU LYS GLU TYR ASN ALA ASP GLY GLY LYS MET PRO
SEQRES 15 C 328 ILE LYS TRP MET ALA LEU GLU CYS ILE HIS TYR ARG LYS
SEQRES 16 C 328 PHE THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 C 328 ILE TRP GLU LEU MET THR PHE GLY GLY LYS PRO TYR ASP
SEQRES 18 C 328 GLY ILE PRO THR ARG GLU ILE PRO ASP LEU LEU GLU LYS
SEQRES 19 C 328 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 C 328 VAL TYR MET VAL MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 C 328 ASP SER ARG PRO LYS PHE LYS GLU LEU ALA ALA GLU PHE
SEQRES 22 C 328 SER ARG MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 C 328 GLN GLY ASP ASP ARG MET LYS LEU PRO SER PRO ASN ASP
SEQRES 24 C 328 SER LYS PHE PHE GLN ASN LEU LEU ASP GLU GLU ASP LEU
SEQRES 25 C 328 GLU ASP MET MET ASP ALA GLU GLU TYR LEU VAL PRO GLN
SEQRES 26 C 328 ALA PHE ASN
HET MN A 1 1
HET PG4 C 502 13
HET PEG C 501 7
HETNAM MN MANGANESE (II) ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 4 MN MN 2+
FORMUL 5 PG4 C8 H18 O5
FORMUL 6 PEG C4 H10 O3
FORMUL 7 HOH *216(H2 O)
HELIX 1 1 LYS A 689 THR A 691 5 3
HELIX 2 2 LYS A 735 SER A 749 1 15
HELIX 3 3 CYS A 778 HIS A 786 1 9
HELIX 4 4 GLY A 791 ARG A 812 1 22
HELIX 5 5 ALA A 820 ARG A 822 5 3
HELIX 6 6 PRO A 858 MET A 862 5 5
HELIX 7 7 ALA A 863 ARG A 870 1 8
HELIX 8 8 THR A 873 THR A 890 1 18
HELIX 9 9 PRO A 900 ARG A 902 5 3
HELIX 10 10 GLU A 903 LYS A 910 1 8
HELIX 11 11 THR A 921 TRP A 932 1 12
HELIX 12 12 ASP A 935 ARG A 939 5 5
HELIX 13 13 LYS A 941 ARG A 954 1 14
HELIX 14 14 ASP A 955 TYR A 959 5 5
HELIX 15 15 LYS B 689 THR B 691 5 3
HELIX 16 16 LYS B 735 SER B 749 1 15
HELIX 17 17 CYS B 778 HIS B 786 1 9
HELIX 18 18 GLY B 791 ARG B 812 1 22
HELIX 19 19 ALA B 820 ARG B 822 5 3
HELIX 20 20 PRO B 858 MET B 862 5 5
HELIX 21 21 ALA B 863 ARG B 870 1 8
HELIX 22 22 THR B 873 THR B 890 1 18
HELIX 23 23 PRO B 900 ARG B 902 5 3
HELIX 24 24 GLU B 903 LYS B 910 1 8
HELIX 25 25 THR B 921 CYS B 931 1 11
HELIX 26 26 ASP B 935 ARG B 939 5 5
HELIX 27 27 LYS B 941 ARG B 954 1 14
HELIX 28 28 ASP B 955 TYR B 959 5 5
HELIX 29 29 LYS C 689 THR C 691 5 3
HELIX 30 30 LYS C 735 SER C 749 1 15
HELIX 31 31 CYS C 778 HIS C 786 1 9
HELIX 32 32 GLY C 791 ARG C 812 1 22
HELIX 33 33 ALA C 820 ARG C 822 5 3
HELIX 34 34 PRO C 858 MET C 862 5 5
HELIX 35 35 ALA C 863 ARG C 870 1 8
HELIX 36 36 THR C 873 THR C 890 1 18
HELIX 37 37 PRO C 900 ARG C 902 5 3
HELIX 38 38 GLU C 903 LYS C 910 1 8
HELIX 39 39 THR C 921 CYS C 931 1 11
HELIX 40 40 ASP C 935 ARG C 939 5 5
HELIX 41 41 LYS C 941 ARG C 954 1 14
HELIX 42 42 ASP C 955 LEU C 960 1 6
SHEET 1 A 6 ILE A 687 LEU A 688 0
SHEET 2 A 6 LEU A 758 CYS A 762 1 O VAL A 761 N LEU A 688
SHEET 3 A 6 GLN A 768 GLN A 772 -1 O VAL A 770 N GLY A 760
SHEET 4 A 6 ILE A 721 ILE A 727 -1 N ALA A 724 O THR A 771
SHEET 5 A 6 THR A 706 TRP A 712 -1 N TYR A 708 O ILE A 725
SHEET 6 A 6 LEU A 693 GLY A 700 -1 N LEU A 699 O VAL A 707
SHEET 1 B 2 LEU A 814 VAL A 815 0
SHEET 2 B 2 ARG A 841 LEU A 842 -1 O ARG A 841 N VAL A 815
SHEET 1 C 2 VAL A 824 SER A 828 0
SHEET 2 C 2 HIS A 831 ILE A 834 -1 O LYS A 833 N LEU A 825
SHEET 1 D 2 TYR A 850 ASN A 851 0
SHEET 2 D 2 LYS A 871 PHE A 872 -1 O PHE A 872 N TYR A 850
SHEET 1 E 6 ILE B 687 LEU B 688 0
SHEET 2 E 6 LEU B 758 CYS B 762 1 O VAL B 761 N LEU B 688
SHEET 3 E 6 GLN B 768 GLN B 772 -1 O GLN B 768 N CYS B 762
SHEET 4 E 6 ILE B 721 ILE B 727 -1 N ALA B 724 O THR B 771
SHEET 5 E 6 GLY B 705 TRP B 712 -1 N TYR B 708 O ILE B 725
SHEET 6 E 6 LEU B 693 GLY B 702 -1 N LEU B 699 O VAL B 707
SHEET 1 F 2 LEU B 814 VAL B 815 0
SHEET 2 F 2 ARG B 841 LEU B 842 -1 O ARG B 841 N VAL B 815
SHEET 1 G 2 VAL B 824 SER B 828 0
SHEET 2 G 2 HIS B 831 ILE B 834 -1 O LYS B 833 N LEU B 825
SHEET 1 H 6 ILE C 687 LEU C 688 0
SHEET 2 H 6 LEU C 758 CYS C 762 1 O VAL C 761 N LEU C 688
SHEET 3 H 6 GLN C 768 GLN C 772 -1 O VAL C 770 N LEU C 759
SHEET 4 H 6 ILE C 721 ILE C 727 -1 N ALA C 724 O THR C 771
SHEET 5 H 6 GLY C 705 TRP C 712 -1 N TYR C 708 O ILE C 725
SHEET 6 H 6 LEU C 693 GLY C 702 -1 N VAL C 696 O LYS C 709
SHEET 1 I 2 LEU C 814 VAL C 815 0
SHEET 2 I 2 ARG C 841 LEU C 842 -1 O ARG C 841 N VAL C 815
SHEET 1 J 2 VAL C 824 SER C 828 0
SHEET 2 J 2 HIS C 831 ILE C 834 -1 O LYS C 833 N LEU C 825
SHEET 1 K 2 TYR C 850 ASN C 851 0
SHEET 2 K 2 LYS C 871 PHE C 872 -1 O PHE C 872 N TYR C 850
CISPEP 1 GLU A 715 GLY A 716 0 -25.10
CISPEP 2 LEU A 759 GLY A 760 0 -22.81
CISPEP 3 SER A 764 PRO A 765 0 2.19
CISPEP 4 SER B 764 PRO B 765 0 0.90
CISPEP 5 SER C 764 PRO C 765 0 5.79
SITE 1 AC1 2 THR A 901 THR C 901
SITE 1 AC2 3 GLN C 793 ASN C 797 ASN C 830
SITE 1 AC3 7 MET C 747 VAL C 756 THR C 771 GLN C 772
SITE 2 AC3 7 MET C 774 LEU C 825 THR C 835
CRYST1 86.723 86.723 120.008 90.00 90.00 120.00 P 32 9
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 0.011531 0.006657 0.000000 0.00000
SCALE2 0.000000 0.013315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008333 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
