HEADER IMMUNE SYSTEM 17-JUL-17 5WHJ
TITLE CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTI-FCRN ANTIBODY DX-2507
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DX-2507 FAB HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DX-2507 FAB LIGHT CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: IGL@;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS FABRICATOR, FCRN, B2M, BETA-2-MICROGLOBULIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.EDWARDS,J.W.FAIRMAN,A.E.NIXON,J.A.KENNISTON
REVDAT 3 04-OCT-23 5WHJ 1 REMARK
REVDAT 2 21-MAR-18 5WHJ 1 JRNL
REVDAT 1 06-SEP-17 5WHJ 0
JRNL AUTH J.A.KENNISTON,B.M.TAYLOR,G.P.CONLEY,J.COSIC,K.J.KOPACZ,
JRNL AUTH 2 A.P.LINDBERG,S.R.COMEAU,K.ATKINS,J.BULLEN,C.TENHOOR,
JRNL AUTH 3 B.A.ADELMAN,D.J.SEXTON,T.E.EDWARDS,A.E.NIXON
JRNL TITL STRUCTURAL BASIS FOR PH-INSENSITIVE INHIBITION OF
JRNL TITL 2 IMMUNOGLOBULIN G RECYCLING BY AN ANTI-NEONATAL FC RECEPTOR
JRNL TITL 3 ANTIBODY.
JRNL REF J. BIOL. CHEM. V. 292 17449 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28878017
JRNL DOI 10.1074/JBC.M117.807396
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2863)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 29840
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.0798 - 4.6298 0.96 2932 162 0.1593 0.1818
REMARK 3 2 4.6298 - 3.6756 0.98 2852 152 0.1398 0.1711
REMARK 3 3 3.6756 - 3.2112 0.99 2855 150 0.1851 0.2437
REMARK 3 4 3.2112 - 2.9177 1.00 2845 130 0.2110 0.2705
REMARK 3 5 2.9177 - 2.7086 1.00 2850 130 0.2075 0.3017
REMARK 3 6 2.7086 - 2.5489 1.00 2817 147 0.2082 0.2827
REMARK 3 7 2.5489 - 2.4213 1.00 2817 143 0.2071 0.2527
REMARK 3 8 2.4213 - 2.3159 1.00 2802 155 0.2112 0.2933
REMARK 3 9 2.3159 - 2.2267 1.00 2807 142 0.2082 0.2697
REMARK 3 10 2.2267 - 2.1499 1.00 2824 128 0.2087 0.2430
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3176
REMARK 3 ANGLE : 0.838 4345
REMARK 3 CHIRALITY : 0.055 495
REMARK 3 PLANARITY : 0.005 562
REMARK 3 DIHEDRAL : 4.988 2175
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5403 -10.1881 4.0730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3444 T22: 0.3228
REMARK 3 T33: 0.2366 T12: -0.0536
REMARK 3 T13: -0.0189 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.5148 L22: 1.1245
REMARK 3 L33: 1.2536 L12: -0.6327
REMARK 3 L13: 0.5533 L23: -0.1285
REMARK 3 S TENSOR
REMARK 3 S11: 0.0808 S12: -0.1847 S13: -0.1846
REMARK 3 S21: -0.0558 S22: 0.0960 S23: -0.1048
REMARK 3 S31: 0.4586 S32: -0.3614 S33: -0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 62 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.9993 -6.3440 5.4131
REMARK 3 T TENSOR
REMARK 3 T11: 0.2813 T22: 0.3498
REMARK 3 T33: 0.1883 T12: -0.0240
REMARK 3 T13: 0.0069 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.5858 L22: 1.7076
REMARK 3 L33: 0.4408 L12: 0.0076
REMARK 3 L13: 0.5584 L23: -0.2145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.3497 S13: -0.0784
REMARK 3 S21: 0.1138 S22: 0.1690 S23: -0.3584
REMARK 3 S31: 0.1718 S32: -0.2721 S33: 0.0006
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 123 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.4716 19.2948 -25.2615
REMARK 3 T TENSOR
REMARK 3 T11: 0.6752 T22: 0.5366
REMARK 3 T33: 0.2467 T12: 0.1343
REMARK 3 T13: 0.0674 T23: 0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 0.1710 L22: 0.0279
REMARK 3 L33: 0.4131 L12: 0.0352
REMARK 3 L13: -0.1127 L23: 0.0494
REMARK 3 S TENSOR
REMARK 3 S11: 0.5734 S12: 0.4072 S13: 0.4039
REMARK 3 S21: -0.7089 S22: 0.1497 S23: 0.2949
REMARK 3 S31: -0.5409 S32: -0.0982 S33: 0.1731
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 138 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7397 11.0400 -16.6061
REMARK 3 T TENSOR
REMARK 3 T11: 0.2116 T22: 0.2793
REMARK 3 T33: 0.1892 T12: 0.0326
REMARK 3 T13: 0.0202 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 1.4817 L22: 1.3209
REMARK 3 L33: 0.8759 L12: 0.3394
REMARK 3 L13: -0.5845 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0839 S12: 0.0802 S13: 0.0016
REMARK 3 S21: -0.1255 S22: 0.0071 S23: -0.0170
REMARK 3 S31: -0.1792 S32: -0.1987 S33: 0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8670 -1.3335 -3.4501
REMARK 3 T TENSOR
REMARK 3 T11: 0.2079 T22: 0.2667
REMARK 3 T33: 0.5344 T12: -0.0383
REMARK 3 T13: 0.0614 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 2.2961 L22: 2.6725
REMARK 3 L33: 1.2704 L12: 0.6530
REMARK 3 L13: -0.4715 L23: -0.1555
REMARK 3 S TENSOR
REMARK 3 S11: -0.3454 S12: -0.1925 S13: -0.5701
REMARK 3 S21: 0.2604 S22: -0.0135 S23: -0.5914
REMARK 3 S31: 0.1242 S32: -0.1460 S33: -0.0304
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 94 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1496 13.6068 -9.5339
REMARK 3 T TENSOR
REMARK 3 T11: 0.2116 T22: 0.2088
REMARK 3 T33: 0.2770 T12: 0.0095
REMARK 3 T13: 0.0495 T23: -0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.7876 L22: 0.4891
REMARK 3 L33: 1.1180 L12: -0.3376
REMARK 3 L13: 0.5165 L23: 0.0652
REMARK 3 S TENSOR
REMARK 3 S11: 0.0538 S12: 0.0875 S13: -0.0926
REMARK 3 S21: 0.1530 S22: 0.0222 S23: 0.0271
REMARK 3 S31: -0.2687 S32: 0.0303 S33: -0.0012
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 134 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6580 27.1312 -14.4811
REMARK 3 T TENSOR
REMARK 3 T11: 0.4963 T22: 0.2985
REMARK 3 T33: 0.4300 T12: -0.0609
REMARK 3 T13: 0.0555 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.6874 L22: 0.6714
REMARK 3 L33: 2.6012 L12: 0.8953
REMARK 3 L13: -0.2137 L23: -0.8146
REMARK 3 S TENSOR
REMARK 3 S11: 0.1677 S12: 0.0585 S13: 0.6923
REMARK 3 S21: 0.4104 S22: -0.0382 S23: 0.1477
REMARK 3 S31: -0.9180 S32: 0.2164 S33: 0.0033
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229033.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100.000
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29879
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.58900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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: 3IDX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DX-2507 FAB AT 9.5 MG/ML AGAINST
REMARK 280 MORPHEUS SCREEN CONDITION G5 WITH 10% PEG 20000, 20% PEG 550, PH
REMARK 280 7.50, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 39.61000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.41500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.80500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.61000
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 19.80500
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 59.41500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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 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 HOH L 356 LIES ON A SPECIAL POSITION.
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 SER H 218
REMARK 465 CYS H 219
REMARK 465 GLN L 1
REMARK 465 THR L 213
REMARK 465 GLU L 214
REMARK 465 CYS L 215
REMARK 465 SER L 216
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 LYS H 43 CG CD CE NZ
REMARK 470 GLN H 57 CG CD OE1 NE2
REMARK 470 LYS H 59 CG CD CE NZ
REMARK 470 LYS H 65 CG CD CE NZ
REMARK 470 LYS H 132 CG CD CE NZ
REMARK 470 THR H 134 OG1 CG2
REMARK 470 LYS H 204 CG CD CE NZ
REMARK 470 LYS H 217 CG CD CE NZ
REMARK 470 LEU L 34 CG CD1 CD2
REMARK 470 LYS L 106 CG CD CE NZ
REMARK 470 GLN L 130 CG CD OE1 NE2
REMARK 470 LYS L 153 CG CD CE NZ
REMARK 470 LYS L 160 CG CD CE NZ
REMARK 470 LYS L 167 CG CD CE NZ
REMARK 470 LYS L 190 CG CD CE NZ
REMARK 470 ARG L 193 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU L 127 O HOH L 301 2.16
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 ASP H 147 60.47 64.17
REMARK 500 ASP L 28 -72.47 -129.98
REMARK 500 ASP L 53 -48.64 69.33
REMARK 500 LYS L 68 136.39 -171.41
REMARK 500 ALA L 94 31.69 -147.25
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 H 458 DISTANCE = 6.24 ANGSTROMS
DBREF 5WHJ H 1 105 PDB 5WHJ 5WHJ 1 105
DBREF 5WHJ H 106 219 UNP S6BAN1 S6BAN1_HUMAN 133 246
DBREF 5WHJ L 1 98 PDB 5WHJ 5WHJ 1 98
DBREF 5WHJ L 99 216 UNP Q6NS95 Q6NS95_HUMAN 117 234
SEQRES 1 H 219 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 219 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 219 PHE THR PHE SER GLU TYR ALA MET GLY TRP VAL ARG GLN
SEQRES 4 H 219 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE GLY
SEQRES 5 H 219 SER SER GLY GLY GLN THR LYS TYR ALA ASP SER VAL LYS
SEQRES 6 H 219 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 H 219 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 219 ALA VAL TYR TYR CYS ALA ARG LEU ALA ILE GLY ASP SER
SEQRES 9 H 219 TYR TRP GLY GLN GLY THR MET VAL THR VAL SER SER ALA
SEQRES 10 H 219 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER
SEQRES 11 H 219 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS
SEQRES 12 H 219 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER
SEQRES 13 H 219 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE
SEQRES 14 H 219 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER
SEQRES 15 H 219 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN
SEQRES 16 H 219 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR
SEQRES 17 H 219 LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS
SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER
SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR GLY
SEQRES 3 L 216 SER ASP VAL GLY SER TYR ASN LEU VAL SER TRP TYR GLN
SEQRES 4 L 216 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLY
SEQRES 5 L 216 ASP SER GLN ARG PRO SER GLY VAL SER ASN ARG PHE SER
SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER
SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS ALA
SEQRES 8 L 216 SER TYR ALA GLY SER GLY ILE TYR VAL PHE GLY THR GLY
SEQRES 9 L 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO
SEQRES 10 L 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN
SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE
SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP GLY
SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS PRO SER
SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU
SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR
SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS
SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER
FORMUL 3 HOH *255(H2 O)
HELIX 1 AA1 THR H 28 TYR H 32 5 5
HELIX 2 AA2 ASP H 62 LYS H 65 5 4
HELIX 3 AA3 ASN H 74 LYS H 76 5 3
HELIX 4 AA4 ARG H 87 THR H 91 5 5
HELIX 5 AA5 SER H 159 ALA H 161 5 3
HELIX 6 AA6 SER H 190 THR H 194 5 5
HELIX 7 AA7 LYS H 204 ASN H 207 5 4
HELIX 8 AA8 ASP L 28 TYR L 32 5 5
HELIX 9 AA9 GLN L 81 GLU L 85 5 5
HELIX 10 AB1 SER L 125 ALA L 131 1 7
HELIX 11 AB2 THR L 185 SER L 191 1 7
SHEET 1 AA1 4 GLN H 3 SER H 7 0
SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3
SHEET 3 AA1 4 THR H 78 MET H 83 -1 O MET H 83 N LEU H 18
SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80
SHEET 1 AA2 6 LEU H 11 VAL H 12 0
SHEET 2 AA2 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12
SHEET 3 AA2 6 ALA H 92 LEU H 99 -1 N ALA H 92 O VAL H 112
SHEET 4 AA2 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 95
SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AA2 6 LYS H 59 TYR H 60 -1 O LYS H 59 N SER H 50
SHEET 1 AA3 4 SER H 123 LEU H 127 0
SHEET 2 AA3 4 THR H 138 TYR H 148 -1 O LYS H 146 N SER H 123
SHEET 3 AA3 4 TYR H 179 PRO H 188 -1 O TYR H 179 N TYR H 148
SHEET 4 AA3 4 VAL H 166 THR H 168 -1 N HIS H 167 O VAL H 184
SHEET 1 AA4 4 SER H 123 LEU H 127 0
SHEET 2 AA4 4 THR H 138 TYR H 148 -1 O LYS H 146 N SER H 123
SHEET 3 AA4 4 TYR H 179 PRO H 188 -1 O TYR H 179 N TYR H 148
SHEET 4 AA4 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180
SHEET 1 AA5 3 THR H 154 TRP H 157 0
SHEET 2 AA5 3 ILE H 198 HIS H 203 -1 O ASN H 200 N SER H 156
SHEET 3 AA5 3 THR H 208 ARG H 213 -1 O VAL H 210 N VAL H 201
SHEET 1 AA6 5 SER L 9 GLY L 12 0
SHEET 2 AA6 5 THR L 105 VAL L 109 1 O THR L 108 N GLY L 12
SHEET 3 AA6 5 ALA L 86 TYR L 93 -1 N ALA L 86 O VAL L 107
SHEET 4 AA6 5 SER L 36 GLN L 40 -1 N GLN L 40 O ASP L 87
SHEET 5 AA6 5 LYS L 47 ILE L 50 -1 O MET L 49 N TRP L 37
SHEET 1 AA7 4 SER L 9 GLY L 12 0
SHEET 2 AA7 4 THR L 105 VAL L 109 1 O THR L 108 N GLY L 12
SHEET 3 AA7 4 ALA L 86 TYR L 93 -1 N ALA L 86 O VAL L 107
SHEET 4 AA7 4 TYR L 99 PHE L 101 -1 O VAL L 100 N SER L 92
SHEET 1 AA8 3 ILE L 18 THR L 23 0
SHEET 2 AA8 3 THR L 72 ILE L 77 -1 O LEU L 75 N ILE L 20
SHEET 3 AA8 3 PHE L 64 SER L 69 -1 N SER L 65 O THR L 76
SHEET 1 AA9 4 THR L 118 PHE L 122 0
SHEET 2 AA9 4 ALA L 134 PHE L 143 -1 O LEU L 139 N THR L 120
SHEET 3 AA9 4 TYR L 176 LEU L 184 -1 O SER L 180 N CYS L 138
SHEET 4 AA9 4 VAL L 163 THR L 165 -1 N GLU L 164 O TYR L 181
SHEET 1 AB1 4 THR L 118 PHE L 122 0
SHEET 2 AB1 4 ALA L 134 PHE L 143 -1 O LEU L 139 N THR L 120
SHEET 3 AB1 4 TYR L 176 LEU L 184 -1 O SER L 180 N CYS L 138
SHEET 4 AB1 4 SER L 169 LYS L 170 -1 N SER L 169 O ALA L 177
SHEET 1 AB2 4 SER L 157 VAL L 159 0
SHEET 2 AB2 4 THR L 149 ALA L 154 -1 N ALA L 154 O SER L 157
SHEET 3 AB2 4 TYR L 195 HIS L 201 -1 O GLN L 198 N ALA L 151
SHEET 4 AB2 4 SER L 204 VAL L 210 -1 O VAL L 206 N VAL L 199
SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 2 CYS H 143 CYS H 199 1555 1555 2.04
SSBOND 3 CYS L 22 CYS L 90 1555 1555 2.05
SSBOND 4 CYS L 138 CYS L 197 1555 1555 2.05
CISPEP 1 PHE H 149 PRO H 150 0 -4.02
CISPEP 2 GLU H 151 PRO H 152 0 2.73
CISPEP 3 TYR L 144 PRO L 145 0 -0.88
CRYST1 116.170 116.170 79.220 90.00 90.00 90.00 P 43 2 2 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 0.008608 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008608 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012623 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
