HEADER CELL CYCLE 23-MAR-16 5IWZ
TITLE SYNAPTONEMAL COMPLEX PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPTONEMAL COMPLEX PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-390;
COMPND 5 SYNONYM: SCP-2,SYNAPTONEMAL COMPLEX LATERAL ELEMENT PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SYCP2, SCP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS COMPONENT OF SYNAPTONEMAL COMPLEXES, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.FENG,S.FU,X.CAO,H.WU,J.LU,M.ZENG,L.LIU,X.YANG,Y.SHEN
REVDAT 3 20-MAR-24 5IWZ 1 REMARK
REVDAT 2 18-OCT-17 5IWZ 1 JRNL
REVDAT 1 29-MAR-17 5IWZ 0
JRNL AUTH J.FENG,S.FU,X.CAO,H.WU,J.LU,M.ZENG,L.LIU,X.YANG,Y.SHEN
JRNL TITL STRUCTURE OF SYNAPTONEMAL COMPLEXES PROTEIN AT 2.6 ANGSTROMS
JRNL TITL 2 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 23596
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1206
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 32.4766 - 4.3609 0.95 2541 127 0.1869 0.2115
REMARK 3 2 4.3609 - 3.4627 0.99 2538 130 0.1681 0.2176
REMARK 3 3 3.4627 - 3.0253 1.00 2507 141 0.1858 0.2357
REMARK 3 4 3.0253 - 2.7489 1.00 2481 147 0.2115 0.2569
REMARK 3 5 2.7489 - 2.5519 1.00 2480 127 0.2021 0.2682
REMARK 3 6 2.5519 - 2.4015 0.99 2481 136 0.2068 0.2813
REMARK 3 7 2.4015 - 2.2813 1.00 2459 138 0.1989 0.2445
REMARK 3 8 2.2813 - 2.1820 0.99 2444 144 0.2078 0.2800
REMARK 3 9 2.1820 - 2.0980 0.99 2459 116 0.2145 0.2777
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.190
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) : 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 : 0.008 3001
REMARK 3 ANGLE : 1.475 4036
REMARK 3 CHIRALITY : 0.091 473
REMARK 3 PLANARITY : 0.005 508
REMARK 3 DIHEDRAL : 21.241 1134
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0497 -15.0477 19.1440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2429 T22: 0.2025
REMARK 3 T33: 0.2029 T12: -0.0454
REMARK 3 T13: -0.0218 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.2144 L22: 0.4589
REMARK 3 L33: 0.8056 L12: -0.4019
REMARK 3 L13: -0.3638 L23: -0.0527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: -0.4362 S13: -0.0683
REMARK 3 S21: 0.0785 S22: 0.0070 S23: -0.0235
REMARK 3 S31: -0.0841 S32: 0.1149 S33: -0.0347
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 5IWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219589.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23639
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 6.5, 25% PEG 3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 32.89050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.25550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.33950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.25550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.89050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.33950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 GLN A 115
REMARK 465 GLN A 116
REMARK 465 SER A 117
REMARK 465 LYS A 118
REMARK 465 PRO A 184
REMARK 465 GLN A 185
REMARK 465 ASP A 186
REMARK 465 ALA A 187
REMARK 465 ASN A 188
REMARK 465 LYS A 189
REMARK 465 ILE A 190
REMARK 465 LEU A 191
REMARK 465 SER A 192
REMARK 465 ALA A 320
REMARK 465 GLY A 321
REMARK 465 ASP A 322
REMARK 465 GLU A 323
REMARK 465 GLU A 324
REMARK 465 ASP A 325
REMARK 465 HIS A 326
REMARK 465 GLN A 327
REMARK 465 TRP A 328
REMARK 465 HIS A 395
REMARK 465 HIS A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
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 MET A 1 CG SD CE
REMARK 470 ARG A 4 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 36 CG CD OE1 OE2
REMARK 470 ASP A 37 CG OD1 OD2
REMARK 470 ASN A 113 CG OD1 ND2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 ASP A 119 CG OD1 OD2
REMARK 470 LYS A 290 CG CD CE NZ
REMARK 470 SER A 297 OG
REMARK 470 ASP A 298 CG OD1 OD2
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 LEU A 301 CG CD1 CD2
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 ARG A 346 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 347 CG CD OE1 OE2
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 NH2 ARG A 276 O HOH A 401 2.17
REMARK 500 O HOH A 443 O HOH A 500 2.18
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 ASP A 298 CB - CA - C ANGL. DEV. = 36.3 DEGREES
REMARK 500 ASP A 298 N - CA - C ANGL. DEV. = -33.1 DEGREES
REMARK 500 GLU A 299 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 GLU A 299 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 LYS A 300 CB - CA - C ANGL. DEV. = -25.5 DEGREES
REMARK 500 LYS A 300 N - CA - C ANGL. DEV. = 38.3 DEGREES
REMARK 500 LEU A 301 N - CA - C ANGL. DEV. = -25.7 DEGREES
REMARK 500 LEU A 315 CA - CB - CG ANGL. DEV. = 17.9 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 ASN A 113 13.85 -65.26
REMARK 500 ASP A 298 -147.01 -112.06
REMARK 500 LYS A 364 18.95 56.50
REMARK 500 PHE A 388 56.01 -113.27
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 A 508 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A 509 DISTANCE = 5.91 ANGSTROMS
DBREF 5IWZ A 1 390 UNP Q9CUU3 SYCP2_MOUSE 1 390
SEQADV 5IWZ PRO A -2 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ GLY A -1 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ SER A 0 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ LEU A 391 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ GLU A 392 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 393 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 394 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 395 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 396 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 397 UNP Q9CUU3 EXPRESSION TAG
SEQADV 5IWZ HIS A 398 UNP Q9CUU3 EXPRESSION TAG
SEQRES 1 A 401 PRO GLY SER MET PRO VAL ARG PRO ASP LEU GLN GLN LEU
SEQRES 2 A 401 GLU LYS CYS ILE ASP ASP ALA LEU ARG LYS ASN ASP PHE
SEQRES 3 A 401 LYS PRO LEU LEU ALA LEU LEU GLN ILE ASP ILE CYS GLU
SEQRES 4 A 401 ASP VAL LYS ILE LYS CYS SER LYS GLN PHE LEU ARG LYS
SEQRES 5 A 401 LEU ASP ASP LEU ILE CYS ARG GLU LEU ASN LYS LYS ASP
SEQRES 6 A 401 ILE GLN THR VAL SER SER ILE LEU ILE SER ILE GLY ARG
SEQRES 7 A 401 CYS SER LYS ASN ILE PHE ILE LEU GLY GLN ALA GLY LEU
SEQRES 8 A 401 GLN THR MET ILE LYS GLN GLY LEU VAL GLN LYS MET VAL
SEQRES 9 A 401 SER TRP PHE GLU ASN SER LYS GLU ILE ILE LEU ASN GLN
SEQRES 10 A 401 GLN GLN SER LYS ASP GLU ALA VAL MET ASN MET ILE GLU
SEQRES 11 A 401 ASP LEU PHE ASP LEU LEU MET VAL ILE TYR ASP ILE SER
SEQRES 12 A 401 ASP GLU GLY LYS ASN GLN VAL LEU GLU SER PHE ILE PRO
SEQRES 13 A 401 GLN ILE CYS ALA LEU VAL ILE ASP SER ARG VAL ASN PHE
SEQRES 14 A 401 CYS ILE GLN GLN GLU ALA LEU LYS LYS MET ASN LEU MET
SEQRES 15 A 401 LEU ASP ARG ILE PRO GLN ASP ALA ASN LYS ILE LEU SER
SEQRES 16 A 401 ASN GLN GLU MET LEU THR LEU MET SER ASN MET GLY GLU
SEQRES 17 A 401 ARG ILE LEU ASP VAL GLY ASP TYR GLU LEU GLN VAL GLY
SEQRES 18 A 401 ILE VAL GLU ALA LEU CYS ARG MET THR THR GLU LYS ARG
SEQRES 19 A 401 ARG GLN GLU LEU ALA TYR GLU TRP PHE SER MET ASP PHE
SEQRES 20 A 401 ILE ALA ASN ALA PHE LYS GLU ILE LYS ASP CYS GLU PHE
SEQRES 21 A 401 GLU THR ASP CYS ARG ILE PHE LEU ASN LEU VAL ASN GLY
SEQRES 22 A 401 ILE LEU GLY ASP LYS ARG ARG VAL TYR THR PHE PRO CYS
SEQRES 23 A 401 LEU SER ALA PHE LEU GLY LYS TYR GLU LEU GLN ILE PRO
SEQRES 24 A 401 SER ASP GLU LYS LEU GLU GLU PHE TRP ILE ASP PHE ASN
SEQRES 25 A 401 LEU GLY SER HIS THR LEU SER PHE TYR ILE ALA GLY ASP
SEQRES 26 A 401 GLU GLU ASP HIS GLN TRP GLU ALA VAL THR VAL PRO GLU
SEQRES 27 A 401 GLU LYS VAL GLN MET TYR ASN ILE GLU VAL ARG GLU SER
SEQRES 28 A 401 LYS LYS LEU LEU THR LEU THR LEU LYS ASN ILE VAL LYS
SEQRES 29 A 401 ILE SER LYS LYS GLU GLY LYS GLU LEU LEU PHE TYR PHE
SEQRES 30 A 401 ASP GLU SER LEU GLU ILE THR ASN VAL THR LYS LYS VAL
SEQRES 31 A 401 PHE GLY GLY LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *109(H2 O)
HELIX 1 AA1 ASP A 6 GLN A 8 5 3
HELIX 2 AA2 GLN A 9 ASN A 21 1 13
HELIX 3 AA3 PHE A 23 LEU A 30 1 8
HELIX 4 AA4 GLN A 45 LYS A 61 1 17
HELIX 5 AA5 ASP A 62 SER A 77 1 16
HELIX 6 AA6 GLY A 87 GLY A 95 1 9
HELIX 7 AA7 GLY A 95 ASN A 106 1 12
HELIX 8 AA8 SER A 107 ASN A 113 1 7
HELIX 9 AA9 GLU A 120 ILE A 139 1 20
HELIX 10 AB1 SER A 140 ASP A 161 1 22
HELIX 11 AB2 ASN A 165 ILE A 183 1 19
HELIX 12 AB3 GLN A 194 VAL A 210 1 17
HELIX 13 AB4 ASP A 212 THR A 227 1 16
HELIX 14 AB5 THR A 228 PHE A 240 1 13
HELIX 15 AB6 MET A 242 GLU A 251 1 10
HELIX 16 AB7 ILE A 252 CYS A 255 5 4
HELIX 17 AB8 GLU A 256 LEU A 272 1 17
HELIX 18 AB9 GLY A 273 ARG A 276 5 4
HELIX 19 AC1 GLU A 379 PHE A 388 1 10
SHEET 1 AA1 3 ILE A 40 CYS A 42 0
SHEET 2 AA1 3 ILE A 80 ILE A 82 1 O PHE A 81 N CYS A 42
SHEET 3 AA1 3 GLN A 85 ALA A 86 -1 O GLN A 85 N ILE A 82
SHEET 1 AA2 4 VAL A 278 PRO A 282 0
SHEET 2 AA2 4 TRP A 305 ASN A 309 -1 O PHE A 308 N TYR A 279
SHEET 3 AA2 4 THR A 314 PHE A 317 -1 O SER A 316 N ASP A 307
SHEET 4 AA2 4 VAL A 331 PRO A 334 -1 O VAL A 331 N PHE A 317
SHEET 1 AA3 5 TYR A 291 GLU A 292 0
SHEET 2 AA3 5 SER A 285 LEU A 288 -1 N LEU A 288 O TYR A 291
SHEET 3 AA3 5 LYS A 365 ASP A 375 -1 O LEU A 371 N PHE A 287
SHEET 4 AA3 5 LYS A 349 ILE A 362 -1 N LEU A 356 O LYS A 368
SHEET 5 AA3 5 VAL A 338 ARG A 346 -1 N GLU A 344 O LEU A 351
CRYST1 65.781 74.679 80.511 90.00 90.00 90.00 P 21 21 21 4
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 0.015202 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013391 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
