HEADER TRANSFERASE 12-OCT-98 8JDW
TITLE CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN
TITLE 2 COMPLEX WITH L-ALANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (L-ARGININE:GLYCINE AMIDINOTRANSFERASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 38 - 423;
COMPND 5 SYNONYM: TRANSAMIDINASE, AT38;
COMPND 6 EC: 2.1.4.1;
COMPND 7 ENGINEERED: 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)
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 8JDW 1 REMARK
REVDAT 5 04-OCT-17 8JDW 1 REMARK
REVDAT 4 24-FEB-09 8JDW 1 VERSN
REVDAT 3 01-APR-03 8JDW 1 JRNL
REVDAT 2 22-DEC-99 8JDW 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 09-FEB-99 8JDW 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. 2.30 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) : 2.30
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) (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 28573
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) : 0.176
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 : 2938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 128
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) : 1.610
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 8JDW 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_1000008080.
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 : 29331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 91.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.84000
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 99.97500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.88000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 149.96250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.88000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.88000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.98750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.88000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.88000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 149.96250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.88000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.88000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.98750
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 99.97500
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 -41.88000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 125.64000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 49.98750
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 H2 HOH A 507 H2 HOH A 514 0.88
REMARK 500 HH TYR A 196 H2 HOH A 521 0.89
REMARK 500 HG1 THR A 307 H2 HOH A 580 0.94
REMARK 500 HH11 ARG A 142 H2 HOH A 607 0.97
REMARK 500 H SER A 295 HE22 GLN A 326 1.07
REMARK 500 HG SER A 354 H1 HOH A 618 1.09
REMARK 500 H GLY A 314 H1 HOH A 532 1.11
REMARK 500 H2 HOH A 506 H2 HOH A 621 1.12
REMARK 500 H TYR A 69 H1 HOH A 523 1.13
REMARK 500 H ASP A 373 H1 HOH A 522 1.21
REMARK 500 HG SER A 355 H TRP A 357 1.21
REMARK 500 H ASN A 394 H1 HOH A 540 1.23
REMARK 500 H ALA A 83 H2 HOH A 545 1.24
REMARK 500 H ILE A 147 H2 HOH A 615 1.25
REMARK 500 H1 HOH A 505 H1 HOH A 518 1.26
REMARK 500 HG1 THR A 246 HH12 ARG A 269 1.28
REMARK 500 H ASN A 85 H2 HOH A 579 1.29
REMARK 500 H1 HOH A 588 H2 HOH A 609 1.30
REMARK 500 H VAL A 174 H2 HOH A 513 1.32
REMARK 500 HG1 THR A 155 H ASP A 157 1.33
REMARK 500 H TRP A 186 H1 HOH A 520 1.35
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 67 100.31 -176.85
REMARK 500 LEU A 163 -81.22 -108.92
REMARK 500 TYR A 164 -172.27 -174.56
REMARK 500 MET A 184 171.29 78.92
REMARK 500 PRO A 228 46.95 -76.20
REMARK 500 HIS A 230 24.11 -53.51
REMARK 500 SER A 231 131.55 74.77
REMARK 500 VAL A 232 -27.25 178.79
REMARK 500 GLU A 233 -12.19 60.60
REMARK 500 ASP A 234 2.02 -67.29
REMARK 500 PHE A 244 -167.37 -125.44
REMARK 500 ASN A 300 57.37 -149.17
REMARK 500 MET A 302 100.15 -166.90
REMARK 500 HIS A 303 145.40 88.63
REMARK 500 THR A 307 -45.06 -136.71
REMARK 500 SER A 354 -154.89 -153.10
REMARK 500 TRP A 357 12.63 -66.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 COMPLEX WITH L-ALANINE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALA A 500
DBREF 8JDW A 38 423 UNP P50440 GATM_HUMAN 38 423
SEQRES 1 A 386 SER THR GLN ALA ALA THR ALA SER SER ARG ASN SER CYS
SEQRES 2 A 386 ALA ALA ASP ASP LYS ALA THR GLU PRO LEU PRO LYS ASP
SEQRES 3 A 386 CYS PRO VAL SER SER TYR ASN GLU TRP ASP PRO LEU GLU
SEQRES 4 A 386 GLU VAL ILE VAL GLY ARG ALA GLU ASN ALA CYS VAL PRO
SEQRES 5 A 386 PRO PHE THR ILE GLU VAL LYS ALA ASN THR TYR GLU LYS
SEQRES 6 A 386 TYR TRP PRO PHE TYR GLN LYS GLN GLY GLY HIS TYR PHE
SEQRES 7 A 386 PRO LYS ASP HIS LEU LYS LYS ALA VAL ALA GLU ILE GLU
SEQRES 8 A 386 GLU MET CYS ASN ILE LEU LYS THR GLU GLY VAL THR VAL
SEQRES 9 A 386 ARG ARG PRO ASP PRO ILE ASP TRP SER LEU LYS TYR LYS
SEQRES 10 A 386 THR PRO ASP PHE GLU SER THR GLY LEU TYR SER ALA MET
SEQRES 11 A 386 PRO ARG ASP ILE LEU ILE VAL VAL GLY ASN GLU ILE ILE
SEQRES 12 A 386 GLU ALA PRO MET ALA TRP ARG SER ARG PHE PHE GLU TYR
SEQRES 13 A 386 ARG ALA TYR ARG SER ILE ILE LYS ASP TYR PHE HIS ARG
SEQRES 14 A 386 GLY ALA LYS TRP THR THR ALA PRO LYS PRO THR MET ALA
SEQRES 15 A 386 ASP GLU LEU TYR ASN GLN ASP TYR PRO ILE HIS SER VAL
SEQRES 16 A 386 GLU ASP ARG HIS LYS LEU ALA ALA GLN GLY LYS PHE VAL
SEQRES 17 A 386 THR THR GLU PHE GLU PRO CYS PHE ASP ALA ALA ASP PHE
SEQRES 18 A 386 ILE ARG ALA GLY ARG ASP ILE PHE ALA GLN ARG SER GLN
SEQRES 19 A 386 VAL THR ASN TYR LEU GLY ILE GLU TRP MET ARG ARG HIS
SEQRES 20 A 386 LEU ALA PRO ASP TYR ARG VAL HIS ILE ILE SER PHE LYS
SEQRES 21 A 386 ASP PRO ASN PRO MET HIS ILE ASP ALA THR PHE ASN ILE
SEQRES 22 A 386 ILE GLY PRO GLY ILE VAL LEU SER ASN PRO ASP ARG PRO
SEQRES 23 A 386 CYS HIS GLN ILE ASP LEU PHE LYS LYS ALA GLY TRP THR
SEQRES 24 A 386 ILE ILE THR PRO PRO THR PRO ILE ILE PRO ASP ASP HIS
SEQRES 25 A 386 PRO LEU TRP MET SER SER LYS TRP LEU SER MET ASN VAL
SEQRES 26 A 386 LEU MET LEU ASP GLU LYS ARG VAL MET VAL ASP ALA ASN
SEQRES 27 A 386 GLU VAL PRO ILE GLN LYS MET PHE GLU LYS LEU GLY ILE
SEQRES 28 A 386 THR THR ILE LYS VAL ASN ILE ARG ASN ALA ASN SER LEU
SEQRES 29 A 386 GLY GLY GLY PHE HIS CYS TRP THR CYS ASP VAL ARG ARG
SEQRES 30 A 386 ARG GLY THR LEU GLN SER TYR LEU ASP
HET ALA A 500 9
HETNAM ALA ALANINE
FORMUL 2 ALA C3 H7 N O2
FORMUL 3 HOH *128(H2 O)
HELIX 1 1 ILE A 93 LYS A 96 1 4
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 ALA A 195 5 4
HELIX 7 7 ARG A 197 HIS A 205 1 9
HELIX 8 8 ASP A 220 LEU A 222 5 3
HELIX 9 9 ASP A 234 GLN A 241 5 8
HELIX 10 10 ALA A 255 ASP A 257 5 3
HELIX 11 11 TYR A 275 LEU A 285 1 11
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 LYS A 385 1 9
HELIX 15 15 ALA A 398 LEU A 401 5 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 2 LYS A 152 LYS A 154 0
SHEET 2 B 2 GLU A 159 THR A 161 -1 N SER A 160 O TYR A 153
SHEET 1 C 3 LEU A 172 VAL A 175 0
SHEET 2 C 3 GLU A 178 GLU A 181 -1 N ILE A 180 O ILE A 173
SHEET 3 C 3 LYS A 209 THR A 212 1 N LYS A 209 O ILE A 179
SHEET 1 D 3 PHE A 258 ALA A 261 0
SHEET 2 D 3 ASP A 264 ALA A 267 -1 N PHE A 266 O ILE A 259
SHEET 3 D 3 ARG A 290 ILE A 293 1 N ARG A 290 O ILE A 265
SHEET 1 E 3 THR A 336 ILE A 338 0
SHEET 2 E 3 ILE A 315 SER A 318 1 N VAL A 316 O THR A 336
SHEET 3 E 3 PHE A 308 GLY A 312 -1 N GLY A 312 O ILE A 315
SHEET 1 F 3 THR A 389 VAL A 393 0
SHEET 2 F 3 ARG A 369 ASP A 373 1 N VAL A 370 O THR A 389
SHEET 3 F 3 LEU A 363 ASP A 366 -1 N ASP A 366 O ARG A 369
SHEET 1 G 2 PRO A 74 GLU A 77 0
SHEET 2 G 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 0.41
SITE 1 AC1 5 MET A 302 ALA A 306 ARG A 322 SER A 354
SITE 2 AC1 5 SER A 355
CRYST1 83.760 83.760 199.950 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 0.011939 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
