HEADER CELL ADHESION 16-MAY-12 4F7H
TITLE THE CRYSTAL STRUCTURE OF KINDLIN-2 PLECKSTRIN HOMOLOGY DOMAIN IN FREE
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERMITIN FAMILY HOMOLOG 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN, UNP RESIDUES 328-499;
COMPND 5 SYNONYM: KINDLIN-2, MITOGEN-INDUCIBLE GENE 2 PROTEIN, MIG-2,
COMPND 6 PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY C MEMBER 1, PH DOMAIN-
COMPND 7 CONTAINING FAMILY C MEMBER 1;
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 GENE: FERMT2, KIND2, MIG2, PLEKHC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-BARREL, MEMBRANE BINDING, INTEGRIN ACTIVATION, CYTOPLASMIC
KEYWDS 2 MEMBRANE, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,Y.ZHU,J.QIN,S.YE,R.ZHANG
REVDAT 3 13-SEP-23 4F7H 1 REMARK SEQADV
REVDAT 2 18-JUL-12 4F7H 1 JRNL
REVDAT 1 13-JUN-12 4F7H 0
JRNL AUTH Y.LIU,Y.ZHU,S.YE,R.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF KINDLIN-2 PH DOMAIN REVEALS A
JRNL TITL 2 CONFORMATIONAL TRANSITION FOR ITS MEMBRANE ANCHORING AND
JRNL TITL 3 REGULATION OF INTEGRIN ACTIVATION.
JRNL REF PROTEIN CELL V. 3 434 2012
JRNL REFN ISSN 1674-800X
JRNL PMID 22653426
JRNL DOI 10.1007/S13238-012-2046-1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13195
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 652
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 29.2404 - 3.2473 1.00 2680 118 0.1838 0.1978
REMARK 3 2 3.2473 - 2.5780 1.00 2506 136 0.1950 0.2255
REMARK 3 3 2.5780 - 2.2522 1.00 2465 125 0.2009 0.2593
REMARK 3 4 2.2522 - 2.0464 1.00 2475 135 0.2007 0.2258
REMARK 3 5 2.0464 - 1.8997 1.00 2417 138 0.2465 0.2886
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 45.96
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.28000
REMARK 3 B22 (A**2) : 2.28000
REMARK 3 B33 (A**2) : -4.55990
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 1116
REMARK 3 ANGLE : 1.486 1503
REMARK 3 CHIRALITY : 0.098 166
REMARK 3 PLANARITY : 0.006 189
REMARK 3 DIHEDRAL : 17.150 422
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 365:392)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1511 10.2129 24.5856
REMARK 3 T TENSOR
REMARK 3 T11: 0.3459 T22: 0.2083
REMARK 3 T33: 0.2169 T12: 0.0199
REMARK 3 T13: 0.0342 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.0361 L22: 4.7027
REMARK 3 L33: 0.4290 L12: 0.9275
REMARK 3 L13: 0.2142 L23: 0.9769
REMARK 3 S TENSOR
REMARK 3 S11: 0.2038 S12: 0.1268 S13: -0.0871
REMARK 3 S21: 0.2486 S22: -0.2024 S23: -0.3236
REMARK 3 S31: 0.1729 S32: 0.1529 S33: -0.0635
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 393:447)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3689 11.2320 27.9062
REMARK 3 T TENSOR
REMARK 3 T11: 0.2864 T22: 0.1846
REMARK 3 T33: 0.1868 T12: -0.0693
REMARK 3 T13: 0.0146 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.2204 L22: 3.0966
REMARK 3 L33: 4.4855 L12: -0.0261
REMARK 3 L13: -0.4947 L23: 0.3994
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: -0.0215 S13: 0.1808
REMARK 3 S21: -0.3507 S22: 0.0936 S23: -0.0046
REMARK 3 S31: -0.6666 S32: 0.4504 S33: -0.0559
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 448:499)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9554 6.1194 34.9868
REMARK 3 T TENSOR
REMARK 3 T11: 0.2302 T22: 0.1004
REMARK 3 T33: 0.1862 T12: -0.0192
REMARK 3 T13: 0.0199 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 3.1324 L22: 2.8244
REMARK 3 L33: 3.6402 L12: -0.3522
REMARK 3 L13: 0.4916 L23: 0.0578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: -0.0117 S13: 0.1637
REMARK 3 S21: 0.0238 S22: -0.0475 S23: 0.1163
REMARK 3 S31: -0.3238 S32: -0.0187 S33: 0.0517
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 4F7H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072551.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13245
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.237
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
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: PHASES
REMARK 200 STARTING MODEL: 2YS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM TARTRATE DIBASIC, 0.1 M
REMARK 280 TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.12450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 29.23700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 29.23700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.18675
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 29.23700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 29.23700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.06225
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 29.23700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 29.23700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.18675
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 29.23700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 29.23700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 23.06225
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 46.12450
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: MONOMERIC
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 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 A 739 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 A 327
REMARK 465 SER A 328
REMARK 465 ILE A 329
REMARK 465 MET A 330
REMARK 465 THR A 331
REMARK 465 SER A 332
REMARK 465 GLU A 333
REMARK 465 ASN A 334
REMARK 465 HIS A 335
REMARK 465 LEU A 336
REMARK 465 ASN A 337
REMARK 465 ASN A 338
REMARK 465 SER A 339
REMARK 465 ASP A 340
REMARK 465 LYS A 341
REMARK 465 GLU A 342
REMARK 465 VAL A 343
REMARK 465 ASP A 344
REMARK 465 GLU A 345
REMARK 465 VAL A 346
REMARK 465 ASP A 347
REMARK 465 ALA A 348
REMARK 465 ALA A 349
REMARK 465 LEU A 350
REMARK 465 SER A 351
REMARK 465 ASP A 352
REMARK 465 LEU A 353
REMARK 465 GLU A 354
REMARK 465 ILE A 355
REMARK 465 THR A 356
REMARK 465 LEU A 357
REMARK 465 GLU A 358
REMARK 465 GLY A 359
REMARK 465 GLY A 360
REMARK 465 LYS A 361
REMARK 465 THR A 362
REMARK 465 SER A 363
REMARK 465 THR A 364
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 HOH A 741 O HOH A 774 1.81
REMARK 500 OD2 ASP A 431 O HOH A 754 1.91
REMARK 500 O HOH A 736 O HOH A 782 2.09
REMARK 500 N ILE A 365 O HOH A 721 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 LEU A 366 19.28 56.93
REMARK 500 ASP A 368 -157.05 -103.77
REMARK 500 ASP A 401 -112.21 57.00
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 SRT A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2LKO RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF THE SAME DOMAIN IN COMPLEX WITH IP4
DBREF 4F7H A 328 499 UNP Q96AC1 FERM2_HUMAN 328 499
SEQADV 4F7H SER A 327 UNP Q96AC1 EXPRESSION TAG
SEQRES 1 A 173 SER SER ILE MET THR SER GLU ASN HIS LEU ASN ASN SER
SEQRES 2 A 173 ASP LYS GLU VAL ASP GLU VAL ASP ALA ALA LEU SER ASP
SEQRES 3 A 173 LEU GLU ILE THR LEU GLU GLY GLY LYS THR SER THR ILE
SEQRES 4 A 173 LEU GLY ASP ILE THR SER ILE PRO GLU LEU ALA ASP TYR
SEQRES 5 A 173 ILE LYS VAL PHE LYS PRO LYS LYS LEU THR LEU LYS GLY
SEQRES 6 A 173 TYR LYS GLN TYR TRP CYS THR PHE LYS ASP THR SER ILE
SEQRES 7 A 173 SER CYS TYR LYS SER LYS GLU GLU SER SER GLY THR PRO
SEQRES 8 A 173 ALA HIS GLN MET ASN LEU ARG GLY CYS GLU VAL THR PRO
SEQRES 9 A 173 ASP VAL ASN ILE SER GLY GLN LYS PHE ASN ILE LYS LEU
SEQRES 10 A 173 LEU ILE PRO VAL ALA GLU GLY MET ASN GLU ILE TRP LEU
SEQRES 11 A 173 ARG CYS ASP ASN GLU LYS GLN TYR ALA HIS TRP MET ALA
SEQRES 12 A 173 ALA CYS ARG LEU ALA SER LYS GLY LYS THR MET ALA ASP
SEQRES 13 A 173 SER SER TYR ASN LEU GLU VAL GLN ASN ILE LEU SER PHE
SEQRES 14 A 173 LEU LYS MET GLN
HET SRT A 601 10
HET SRT A 602 10
HETNAM SRT S,R MESO-TARTARIC ACID
FORMUL 2 SRT 2(C4 H6 O6)
FORMUL 4 HOH *86(H2 O)
HELIX 1 1 ASP A 368 ILE A 372 5 5
HELIX 2 2 SER A 409 SER A 413 5 5
HELIX 3 3 ASN A 460 LYS A 476 1 17
HELIX 4 4 SER A 483 LEU A 496 1 14
SHEET 1 A 7 HIS A 419 ASN A 422 0
SHEET 2 A 7 SER A 403 TYR A 407 -1 N CYS A 406 O HIS A 419
SHEET 3 A 7 LYS A 393 LYS A 400 -1 N TRP A 396 O TYR A 407
SHEET 4 A 7 LEU A 375 PHE A 382 -1 N ASP A 377 O CYS A 397
SHEET 5 A 7 GLY A 450 CYS A 458 -1 O ARG A 457 N LYS A 380
SHEET 6 A 7 LYS A 438 VAL A 447 -1 N ILE A 441 O LEU A 456
SHEET 7 A 7 GLU A 427 ASN A 433 -1 N ASN A 433 O LYS A 438
CISPEP 1 ILE A 372 PRO A 373 0 -6.91
SITE 1 AC1 11 ASP A 401 THR A 402 SER A 403 LYS A 410
SITE 2 AC1 11 GLU A 411 GLU A 412 SER A 413 SER A 414
SITE 3 AC1 11 ASN A 422 ARG A 424 HOH A 741
SITE 1 AC2 9 LYS A 400 LYS A 476 GLY A 477 LYS A 478
SITE 2 AC2 9 HOH A 724 HOH A 729 HOH A 775 HOH A 778
SITE 3 AC2 9 HOH A 781
CRYST1 58.474 58.474 92.249 90.00 90.00 90.00 P 43 21 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 0.017102 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017102 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010840 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
