HEADER CELL ADHESION 09-JUL-09 3I84
TITLE THE CRYSTAL STRUCTURE OF HUMAN EMMPRIN N-TERMINAL DOMAIN 1 IN P6(1)22
TITLE 2 SPACE GROUP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CERVICAL EMMPRIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 13-103;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 9 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCEP4
KEYWDS EMMPRIN; CD147; DIMERIZATION; CELL ADHESION; BETA-STRAND SWAPPING,
KEYWDS 2 CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUO,G.L.GILLILAND
REVDAT 5 06-SEP-23 3I84 1 REMARK
REVDAT 4 13-OCT-21 3I84 1 SEQADV
REVDAT 3 31-MAR-21 3I84 1 SOURCE SEQADV
REVDAT 2 03-NOV-09 3I84 1 JRNL
REVDAT 1 06-OCT-09 3I84 0
JRNL AUTH J.LUO,A.TEPLYAKOV,G.OBMOLOVA,T.MALIA,S.J.WU,E.BEIL,A.BAKER,
JRNL AUTH 2 B.SWENCKI-UNDERWOOD,Y.ZHAO,J.SPRENKLE,K.DIXON,R.SWEET,
JRNL AUTH 3 G.L.GILLILAND
JRNL TITL STRUCTURE OF THE EMMPRIN N-TERMINAL DOMAIN 1: DIMERIZATION
JRNL TITL 2 VIA BETA-STRAND SWAPPING.
JRNL REF PROTEINS V. 77 1009 2009
JRNL REFN ISSN 0887-3585
JRNL PMID 19768682
JRNL DOI 10.1002/PROT.22577
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 19841
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 987
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 27.7673 - 3.8233 0.84 2628 128 0.1999 0.2086
REMARK 3 2 3.8233 - 3.0359 0.93 2736 148 0.1504 0.1673
REMARK 3 3 3.0359 - 2.6524 0.96 2778 140 0.1763 0.2146
REMARK 3 4 2.6524 - 2.4101 0.95 2711 143 0.2026 0.2289
REMARK 3 5 2.4101 - 2.2374 0.95 2716 142 0.2072 0.2309
REMARK 3 6 2.2374 - 2.1056 0.94 2664 151 0.1891 0.2391
REMARK 3 7 2.1056 - 2.0000 0.92 2621 135 0.1947 0.2171
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 : 0.40
REMARK 3 B_SOL : 91.03
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.15000
REMARK 3 B22 (A**2) : -6.15000
REMARK 3 B33 (A**2) : 12.30000
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 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 : 0.013 1293
REMARK 3 ANGLE : 1.354 1758
REMARK 3 CHIRALITY : 0.105 204
REMARK 3 PLANARITY : 0.006 222
REMARK 3 DIHEDRAL : 18.426 454
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 22:92
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9754 -34.6048 -3.0256
REMARK 3 T TENSOR
REMARK 3 T11: 0.2244 T22: 0.3823
REMARK 3 T33: 0.2186 T12: -0.0438
REMARK 3 T13: -0.0071 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 4.0112 L22: 1.1649
REMARK 3 L33: 0.5783 L12: 0.4694
REMARK 3 L13: 1.7585 L23: -0.4110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0285 S12: 0.5601 S13: 0.1335
REMARK 3 S21: -0.0545 S22: -0.0631 S23: 0.0610
REMARK 3 S31: 0.0021 S32: -0.1657 S33: 0.1011
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 93:103
REMARK 3 ORIGIN FOR THE GROUP (A): NULL NULL NULL
REMARK 3 T TENSOR
REMARK 3 T11: 0.2352 T22: 0.4105
REMARK 3 T33: 0.3090 T12: 0.0159
REMARK 3 T13: 0.0370 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.5328 L22: 0.8783
REMARK 3 L33: 0.2882 L12: -0.7373
REMARK 3 L13: -0.9719 L23: -0.8143
REMARK 3 S TENSOR
REMARK 3 S11: 0.2426 S12: 0.1837 S13: -0.4694
REMARK 3 S21: -0.1711 S22: -0.1755 S23: 0.1274
REMARK 3 S31: 0.4831 S32: -0.1321 S33: 0.2500
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND RESID 13:18
REMARK 3 ORIGIN FOR THE GROUP (A): NULL NULL NULL
REMARK 3 T TENSOR
REMARK 3 T11: 0.3626 T22: 0.3813
REMARK 3 T33: 0.4525 T12: -0.1422
REMARK 3 T13: 0.1072 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 5.6617 L22: 6.8894
REMARK 3 L33: 5.9527 L12: 2.5226
REMARK 3 L13: -5.2005 L23: -0.2847
REMARK 3 S TENSOR
REMARK 3 S11: -0.6037 S12: 0.2567 S13: -1.2859
REMARK 3 S21: -0.5836 S22: -0.6557 S23: -0.5422
REMARK 3 S31: 0.5917 S32: -0.7634 S33: 0.8121
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 24:92
REMARK 3 ORIGIN FOR THE GROUP (A): NULL NULL NULL
REMARK 3 T TENSOR
REMARK 3 T11: 0.1916 T22: 0.2837
REMARK 3 T33: 0.1950 T12: -0.0069
REMARK 3 T13: 0.0119 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 3.8097 L22: 2.1262
REMARK 3 L33: 0.6335 L12: -0.7301
REMARK 3 L13: -1.4574 L23: 1.0721
REMARK 3 S TENSOR
REMARK 3 S11: 0.0237 S12: 0.1451 S13: 0.2327
REMARK 3 S21: 0.1042 S22: 0.0473 S23: -0.1412
REMARK 3 S31: 0.0407 S32: 0.0539 S33: -0.0575
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESID 93:103
REMARK 3 ORIGIN FOR THE GROUP (A): NULL NULL NULL
REMARK 3 T TENSOR
REMARK 3 T11: 0.2586 T22: 0.5264
REMARK 3 T33: 0.3955 T12: -0.0104
REMARK 3 T13: -0.0769 T23: 0.1317
REMARK 3 L TENSOR
REMARK 3 L11: 8.4927 L22: 1.1906
REMARK 3 L33: 3.8485 L12: -1.1636
REMARK 3 L13: -2.8765 L23: 0.8970
REMARK 3 S TENSOR
REMARK 3 S11: -0.1405 S12: 1.0282 S13: 1.3635
REMARK 3 S21: -0.1417 S22: 0.4673 S23: -0.3490
REMARK 3 S31: 0.2605 S32: -0.2539 S33: -0.1373
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 3I84 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054083.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 27.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.45400
REMARK 200 R SYM FOR SHELL (I) : 0.45400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
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: PDB ENTRY 3B5H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.2 M SODIUM FORMATE, 3% MPD, 0.1 M
REMARK 280 SODIUM CITRATE, PH 3.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 34.62200
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 69.24400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.93300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 86.55500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.31100
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 34.62200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 69.24400
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 86.55500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 51.93300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 17.31100
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.500000 0.866025 0.000000 50.18550
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -86.92384
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 17.31100
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL B 1 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 115 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 LEU A 13
REMARK 465 LEU A 14
REMARK 465 GLY A 15
REMARK 465 THR A 16
REMARK 465 HIS A 17
REMARK 465 GLY A 18
REMARK 465 ASP A 19
REMARK 465 SER A 20
REMARK 465 GLY A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 47
REMARK 465 GLY A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
REMARK 465 HIS A 110
REMARK 465 ASP B 19
REMARK 465 SER B 20
REMARK 465 GLY B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 GLY B 103
REMARK 465 GLY B 104
REMARK 465 HIS B 105
REMARK 465 HIS B 106
REMARK 465 HIS B 107
REMARK 465 HIS B 108
REMARK 465 HIS B 109
REMARK 465 HIS B 110
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 ASP A 45 CG OD1 OD2
REMARK 470 SER A 46 OG
REMARK 470 THR A 48 OG1 CG2
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 ASP B 45 CG OD1 OD2
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 GLU A 49 84.85 -68.58
REMARK 500 ASP B 45 95.19 -50.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I85 RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF HUMAN EMMPRIN N-TERMINAL DOMAIN 1 IN P3(2)
REMARK 900 21 SPACE GROUP
DBREF 3I84 A 13 103 UNP Q54A51 Q54A51_HUMAN 13 103
DBREF 3I84 B 13 103 UNP Q54A51 Q54A51_HUMAN 13 103
SEQADV 3I84 ASP A 19 UNP Q54A51 ALA 19 ENGINEERED MUTATION
SEQADV 3I84 ASP A 44 UNP Q54A51 ASN 44 ENGINEERED MUTATION
SEQADV 3I84 GLY A 104 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 105 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 106 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 107 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 108 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 109 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS A 110 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 ASP B 19 UNP Q54A51 ALA 19 ENGINEERED MUTATION
SEQADV 3I84 ASP B 44 UNP Q54A51 ASN 44 ENGINEERED MUTATION
SEQADV 3I84 GLY B 104 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 105 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 106 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 107 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 108 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 109 UNP Q54A51 EXPRESSION TAG
SEQADV 3I84 HIS B 110 UNP Q54A51 EXPRESSION TAG
SEQRES 1 A 98 LEU LEU GLY THR HIS GLY ASP SER GLY ALA ALA GLY THR
SEQRES 2 A 98 VAL PHE THR THR VAL GLU ASP LEU GLY SER LYS ILE LEU
SEQRES 3 A 98 LEU THR CYS SER LEU ASP ASP SER ALA THR GLU VAL THR
SEQRES 4 A 98 GLY HIS ARG TRP LEU LYS GLY GLY VAL VAL LEU LYS GLU
SEQRES 5 A 98 ASP ALA LEU PRO GLY GLN LYS THR GLU PHE LYS VAL ASP
SEQRES 6 A 98 SER ASP ASP GLN TRP GLY GLU TYR SER CYS VAL PHE LEU
SEQRES 7 A 98 PRO GLU PRO MET GLY THR ALA ASN ILE GLN LEU HIS GLY
SEQRES 8 A 98 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 98 LEU LEU GLY THR HIS GLY ASP SER GLY ALA ALA GLY THR
SEQRES 2 B 98 VAL PHE THR THR VAL GLU ASP LEU GLY SER LYS ILE LEU
SEQRES 3 B 98 LEU THR CYS SER LEU ASP ASP SER ALA THR GLU VAL THR
SEQRES 4 B 98 GLY HIS ARG TRP LEU LYS GLY GLY VAL VAL LEU LYS GLU
SEQRES 5 B 98 ASP ALA LEU PRO GLY GLN LYS THR GLU PHE LYS VAL ASP
SEQRES 6 B 98 SER ASP ASP GLN TRP GLY GLU TYR SER CYS VAL PHE LEU
SEQRES 7 B 98 PRO GLU PRO MET GLY THR ALA ASN ILE GLN LEU HIS GLY
SEQRES 8 B 98 GLY HIS HIS HIS HIS HIS HIS
HET CL B 1 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL CL 1-
FORMUL 4 HOH *160(H2 O)
HELIX 1 1 ASP A 77 GLN A 81 5 5
SHEET 1 A 3 VAL A 26 LEU A 33 0
SHEET 2 A 3 LYS A 36 LEU A 43 -1 O LEU A 38 N GLU A 31
SHEET 3 A 3 LYS A 71 VAL A 76 -1 O VAL A 76 N ILE A 37
SHEET 1 B 4 VAL A 60 ASP A 65 0
SHEET 2 B 4 VAL A 50 LYS A 57 -1 N TRP A 55 O LEU A 62
SHEET 3 B 4 GLY A 83 PRO A 91 -1 O LEU A 90 N THR A 51
SHEET 4 B 4 GLY B 95 LEU B 101 -1 O ILE B 99 N TYR A 85
SHEET 1 C 4 GLY A 95 LEU A 101 0
SHEET 2 C 4 GLY B 83 LEU B 90 -1 O TYR B 85 N ILE A 99
SHEET 3 C 4 GLY B 52 LYS B 57 -1 N GLY B 52 O LEU B 90
SHEET 4 C 4 VAL B 60 ASP B 65 -1 O LEU B 62 N TRP B 55
SHEET 1 D 3 VAL B 26 ASP B 32 0
SHEET 2 D 3 LYS B 36 LEU B 43 -1 O LEU B 38 N GLU B 31
SHEET 3 D 3 LYS B 71 ASP B 77 -1 O PHE B 74 N LEU B 39
SSBOND 1 CYS A 41 CYS A 87 1555 1555 2.06
SSBOND 2 CYS B 41 CYS B 87 1555 1555 2.07
CRYST1 100.371 100.371 103.866 90.00 90.00 120.00 P 61 2 2 24
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 0.009963 0.005752 0.000000 0.00000
SCALE2 0.000000 0.011504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
