HEADER TRANSFERASE 12-OCT-98 2JDX
TITLE CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE,
TITLE 2 DELETIONMUTANT ATDELTAM302
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (L-ARGININE:GLYCINE AMIDINOTRANSFERASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 64 - 423;
COMPND 5 SYNONYM: TRANSAMIDINASE, AT38;
COMPND 6 EC: 2.1.4.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL(21)DE3PLYSS;
SOURCE 6 ORGAN: KIDNEY;
SOURCE 7 ORGANELLE: MITOCHONDRIA;
SOURCE 8 CELLULAR_LOCATION: CYTOSOLIC;
SOURCE 9 GENE: AT38H;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR: PRSET;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PRSETAT38H;
SOURCE 15 EXPRESSION_SYSTEM_GENE: AT38H;
SOURCE 16 OTHER_DETAILS: WITHOUT SIGNAL SEQUENCE (1-37) BUT WITH 19 N-TERMINAL
SOURCE 17 ATTACHED 6-HISTIDINE-TAG (14 RESIDUES)
KEYWDS TRANSFERASE, CREATINE BIOSYNTHESIS, CATALYTIC TRIAD, REACTION
KEYWDS 2 MECHANISM, NOVEL FOLD, FIVEFOLD PSEUDOSYMMETRY
EXPDTA X-RAY DIFFRACTION
AUTHOR E.FRITSCHE,A.HUMM,R.HUBER
REVDAT 6 27-DEC-23 2JDX 1 SEQADV
REVDAT 5 04-OCT-17 2JDX 1 REMARK
REVDAT 4 24-FEB-09 2JDX 1 VERSN
REVDAT 3 01-APR-03 2JDX 1 JRNL
REVDAT 2 22-DEC-99 2JDX 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 09-FEB-99 2JDX 0
JRNL AUTH E.FRITSCHE,A.HUMM,R.HUBER
JRNL TITL THE LIGAND-INDUCED STRUCTURAL CHANGES OF HUMAN
JRNL TITL 2 L-ARGININE:GLYCINE AMIDINOTRANSFERASE. A MUTATIONAL AND
JRNL TITL 3 CRYSTALLOGRAPHIC STUDY.
JRNL REF J.BIOL.CHEM. V. 274 3026 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 9915841
JRNL DOI 10.1074/JBC.274.5.3026
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 15236
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 51
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.570
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JDX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73369
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
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) : 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: OTHER
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
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 100.20500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.85500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.85500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 150.30750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.85500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.85500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.10250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.85500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.85500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 150.30750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.85500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.85500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.10250
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 100.20500
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 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 BIOMT1 2 1.000000 0.000000 0.000000 -41.85500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 125.56500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 50.10250
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 38
REMARK 465 THR A 39
REMARK 465 GLN A 40
REMARK 465 ALA A 41
REMARK 465 ALA A 42
REMARK 465 THR A 43
REMARK 465 ALA A 44
REMARK 465 SER A 45
REMARK 465 SER A 46
REMARK 465 ARG A 47
REMARK 465 ASN A 48
REMARK 465 SER A 49
REMARK 465 CYS A 50
REMARK 465 ALA A 51
REMARK 465 ALA A 52
REMARK 465 ASP A 53
REMARK 465 ASP A 54
REMARK 465 LYS A 55
REMARK 465 ALA A 56
REMARK 465 THR A 57
REMARK 465 GLU A 58
REMARK 465 PRO A 59
REMARK 465 LEU A 60
REMARK 465 PRO A 61
REMARK 465 LYS A 62
REMARK 465 ASP A 63
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 HH22 ARG A 143 H1 HOH A 445 1.10
REMARK 500 HG SER A 68 HH12 ARG A 260 1.12
REMARK 500 HG1 THR A 246 HH12 ARG A 269 1.19
REMARK 500 H SER A 295 HE21 GLN A 326 1.34
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 SER A 67 102.61 -169.72
REMARK 500 PRO A 74 109.64 -43.95
REMARK 500 PRO A 116 109.64 -40.08
REMARK 500 LEU A 163 -90.70 -114.01
REMARK 500 MET A 184 175.70 84.42
REMARK 500 PRO A 228 21.49 -62.48
REMARK 500 PHE A 253 161.25 176.98
REMARK 500 HIS A 303 105.63 83.27
REMARK 500 ASP A 305 3.24 -67.24
REMARK 500 THR A 307 -32.78 -134.71
REMARK 500 PHE A 308 83.10 -150.50
REMARK 500 PRO A 313 94.21 -56.35
REMARK 500 SER A 354 -170.87 85.50
REMARK 500 TRP A 357 7.39 -68.28
REMARK 500 ASP A 366 -173.36 -177.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DELETION OF MET-302
DBREF 2JDX A 38 423 UNP P50440 GATM_HUMAN 38 423
SEQADV 2JDX A UNP P50440 MET 302 DELETION
SEQRES 1 A 385 SER THR GLN ALA ALA THR ALA SER SER ARG ASN SER CYS
SEQRES 2 A 385 ALA ALA ASP ASP LYS ALA THR GLU PRO LEU PRO LYS ASP
SEQRES 3 A 385 CYS PRO VAL SER SER TYR ASN GLU TRP ASP PRO LEU GLU
SEQRES 4 A 385 GLU VAL ILE VAL GLY ARG ALA GLU ASN ALA CYS VAL PRO
SEQRES 5 A 385 PRO PHE THR ILE GLU VAL LYS ALA ASN THR TYR GLU LYS
SEQRES 6 A 385 TYR TRP PRO PHE TYR GLN LYS GLN GLY GLY HIS TYR PHE
SEQRES 7 A 385 PRO LYS ASP HIS LEU LYS LYS ALA VAL ALA GLU ILE GLU
SEQRES 8 A 385 GLU MET CYS ASN ILE LEU LYS THR GLU GLY VAL THR VAL
SEQRES 9 A 385 ARG ARG PRO ASP PRO ILE ASP TRP SER LEU LYS TYR LYS
SEQRES 10 A 385 THR PRO ASP PHE GLU SER THR GLY LEU TYR SER ALA MET
SEQRES 11 A 385 PRO ARG ASP ILE LEU ILE VAL VAL GLY ASN GLU ILE ILE
SEQRES 12 A 385 GLU ALA PRO MET ALA TRP ARG SER ARG PHE PHE GLU TYR
SEQRES 13 A 385 ARG ALA TYR ARG SER ILE ILE LYS ASP TYR PHE HIS ARG
SEQRES 14 A 385 GLY ALA LYS TRP THR THR ALA PRO LYS PRO THR MET ALA
SEQRES 15 A 385 ASP GLU LEU TYR ASN GLN ASP TYR PRO ILE HIS SER VAL
SEQRES 16 A 385 GLU ASP ARG HIS LYS LEU ALA ALA GLN GLY LYS PHE VAL
SEQRES 17 A 385 THR THR GLU PHE GLU PRO CYS PHE ASP ALA ALA ASP PHE
SEQRES 18 A 385 ILE ARG ALA GLY ARG ASP ILE PHE ALA GLN ARG SER GLN
SEQRES 19 A 385 VAL THR ASN TYR LEU GLY ILE GLU TRP MET ARG ARG HIS
SEQRES 20 A 385 LEU ALA PRO ASP TYR ARG VAL HIS ILE ILE SER PHE LYS
SEQRES 21 A 385 ASP PRO ASN PRO HIS ILE ASP ALA THR PHE ASN ILE ILE
SEQRES 22 A 385 GLY PRO GLY ILE VAL LEU SER ASN PRO ASP ARG PRO CYS
SEQRES 23 A 385 HIS GLN ILE ASP LEU PHE LYS LYS ALA GLY TRP THR ILE
SEQRES 24 A 385 ILE THR PRO PRO THR PRO ILE ILE PRO ASP ASP HIS PRO
SEQRES 25 A 385 LEU TRP MET SER SER LYS TRP LEU SER MET ASN VAL LEU
SEQRES 26 A 385 MET LEU ASP GLU LYS ARG VAL MET VAL ASP ALA ASN GLU
SEQRES 27 A 385 VAL PRO ILE GLN LYS MET PHE GLU LYS LEU GLY ILE THR
SEQRES 28 A 385 THR ILE LYS VAL ASN ILE ARG ASN ALA ASN SER LEU GLY
SEQRES 29 A 385 GLY GLY PHE HIS CYS TRP THR CYS ASP VAL ARG ARG ARG
SEQRES 30 A 385 GLY THR LEU GLN SER TYR LEU ASP
FORMUL 2 HOH *51(H2 O)
HELIX 1 1 ILE A 93 ASN A 98 1 6
HELIX 2 2 GLU A 101 GLN A 110 5 10
HELIX 3 3 LYS A 117 THR A 136 1 20
HELIX 4 4 PRO A 168 ILE A 171 1 4
HELIX 5 5 ARG A 187 ARG A 189 5 3
HELIX 6 6 GLU A 192 HIS A 205 5 14
HELIX 7 7 ASP A 220 LEU A 222 5 3
HELIX 8 8 VAL A 232 GLN A 241 1 10
HELIX 9 9 ALA A 255 ASP A 257 5 3
HELIX 10 10 TYR A 275 LEU A 285 1 11
HELIX 11 11 ILE A 304 ALA A 306 5 3
HELIX 12 12 ILE A 327 LYS A 332 1 6
HELIX 13 13 LYS A 356 MET A 360 5 5
HELIX 14 14 VAL A 377 LEU A 386 1 10
HELIX 15 15 ARG A 396 LEU A 401 1 6
HELIX 16 16 PHE A 405 TRP A 408 1 4
SHEET 1 A 3 THR A 140 ARG A 143 0
SHEET 2 A 3 GLU A 77 VAL A 80 1 N VAL A 78 O THR A 140
SHEET 3 A 3 THR A 409 ASP A 411 -1 N CYS A 410 O ILE A 79
SHEET 1 B 3 LEU A 172 VAL A 175 0
SHEET 2 B 3 GLU A 178 GLU A 181 -1 N ILE A 180 O ILE A 173
SHEET 3 B 3 LYS A 209 THR A 212 1 N LYS A 209 O ILE A 179
SHEET 1 C 3 PHE A 258 ALA A 261 0
SHEET 2 C 3 ASP A 264 ALA A 267 -1 N PHE A 266 O ILE A 259
SHEET 3 C 3 ARG A 290 ILE A 293 1 N ARG A 290 O ILE A 265
SHEET 1 D 3 THR A 336 ILE A 338 0
SHEET 2 D 3 ILE A 315 SER A 318 1 N VAL A 316 O THR A 336
SHEET 3 D 3 PHE A 308 GLY A 312 -1 N GLY A 312 O ILE A 315
SHEET 1 E 3 THR A 389 VAL A 393 0
SHEET 2 E 3 ARG A 369 ASP A 373 1 N VAL A 370 O THR A 389
SHEET 3 E 3 LEU A 363 ASP A 366 -1 N ASP A 366 O ARG A 369
SHEET 1 F 2 PRO A 74 GLU A 77 0
SHEET 2 F 2 ARG A 413 ARG A 415 -1 N ARG A 415 O PRO A 74
CISPEP 1 ALA A 286 PRO A 287 0 0.19
CRYST1 83.710 83.710 200.410 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 0.011946 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004990 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
