HEADER OXIDOREDUCTASE 27-DEC-11 3V9L
TITLE CRYSTAL STRUCTURE OF MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE
TITLE 2 COMPLEXED WITH NAD+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: UNP RESIDUES 21-562;
COMPND 6 SYNONYM: 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, P5C DEHYDROGENASE,
COMPND 7 ALDEHYDE DEHYDROGENASE FAMILY 4 MEMBER A1;
COMPND 8 EC: 1.5.1.12;
COMPND 9 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: ALDH4A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALDEHYDE DEHYDROGENASE, ROSSMANN FOLD, NUCLEOTIDE BINDING, ACTING ON
KEYWDS 2 ALDEHYDE OR OXO GROUP OF DONORS, NAD OR NADP AS ACCEPTOR,
KEYWDS 3 MITOCHONDRIA, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TANNER,D.SRIVASTAVA
REVDAT 3 13-SEP-23 3V9L 1 REMARK SEQADV
REVDAT 2 27-JUN-12 3V9L 1 JRNL
REVDAT 1 02-MAY-12 3V9L 0
JRNL AUTH D.SRIVASTAVA,R.K.SINGH,M.A.MOXLEY,M.T.HENZL,D.F.BECKER,
JRNL AUTH 2 J.J.TANNER
JRNL TITL THE THREE-DIMENSIONAL STRUCTURAL BASIS OF TYPE II
JRNL TITL 2 HYPERPROLINEMIA.
JRNL REF J.MOL.BIOL. V. 420 176 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22516612
JRNL DOI 10.1016/J.JMB.2012.04.010
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 168202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 8525
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 45.6686 - 3.2356 1.00 16578 898 0.1601 0.1665
REMARK 3 2 3.2356 - 2.5683 1.00 16152 895 0.1638 0.1764
REMARK 3 3 2.5683 - 2.2436 1.00 16022 854 0.1569 0.1728
REMARK 3 4 2.2436 - 2.0385 1.00 16036 817 0.1502 0.1740
REMARK 3 5 2.0385 - 1.8924 1.00 15964 837 0.1509 0.1714
REMARK 3 6 1.8924 - 1.7808 1.00 15979 818 0.1478 0.1794
REMARK 3 7 1.7808 - 1.6916 1.00 15915 811 0.1489 0.1758
REMARK 3 8 1.6916 - 1.6180 1.00 15861 919 0.1509 0.1820
REMARK 3 9 1.6180 - 1.5557 1.00 15900 844 0.1564 0.1917
REMARK 3 10 1.5557 - 1.5020 0.96 15270 832 0.1940 0.2122
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 34.04
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.79850
REMARK 3 B22 (A**2) : 2.19320
REMARK 3 B33 (A**2) : -0.09570
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 : 0.006 8653
REMARK 3 ANGLE : 1.111 11830
REMARK 3 CHIRALITY : 0.070 1306
REMARK 3 PLANARITY : 0.005 1545
REMARK 3 DIHEDRAL : 11.683 3080
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3V9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069767.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 168338
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.502
REMARK 200 RESOLUTION RANGE LOW (A) : 47.027
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
REMARK 200 R SYM FOR SHELL (I) : 0.39900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3V9J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 20-25% W/V PEG3350, 0.2 M
REMARK 280 LITHIUM SULFATE, 0.1 M BIS-TRIS, PH 6.5, CRYOPROTECTANT: 25%
REMARK 280 GLYCEROL, 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 42.44400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.21250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.02650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.21250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.44400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.02650
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 LEU A 22
REMARK 465 ARG A 23
REMARK 465 TRP A 24
REMARK 465 LYS A 25
REMARK 465 HIS A 26
REMARK 465 THR A 27
REMARK 465 SER A 28
REMARK 465 SER A 29
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
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 LEU A 30 CG CD1 CD2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 VAL A 32 CG1 CG2
REMARK 470 GLN A 42 CD OE1 NE2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 GLU A 71 CG CD OE1 OE2
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 GLU A 277 CD OE1 OE2
REMARK 470 LYS A 292 CE NZ
REMARK 470 GLN A 300 CG CD OE1 NE2
REMARK 470 ARG A 304 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 ARG A 367 NE CZ NH1 NH2
REMARK 470 LYS A 395 CG CD CE NZ
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 LYS A 462 CG CD CE NZ
REMARK 470 GLU A 465 CD OE1 OE2
REMARK 470 LYS A 468 CE NZ
REMARK 470 LYS A 487 CE NZ
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 GLN A 563 CG CD OE1 NE2
REMARK 470 SER B 19 OG
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 HIS B 26 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 27 OG1 CG2
REMARK 470 SER B 28 OG
REMARK 470 GLN B 42 CD OE1 NE2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 LYS B 90 NZ
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLU B 115 CD OE1 OE2
REMARK 470 GLN B 126 CG CD OE1 NE2
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 GLU B 183 CD OE1 OE2
REMARK 470 ARG B 247 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 277 CD OE1 OE2
REMARK 470 GLN B 300 CG CD OE1 NE2
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 ARG B 367 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 370 CG CD OE1 OE2
REMARK 470 LYS B 376 CE NZ
REMARK 470 LYS B 395 CG CD CE NZ
REMARK 470 LYS B 402 CG CD CE NZ
REMARK 470 ARG B 408 CD NE CZ NH1 NH2
REMARK 470 ARG B 464 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 LYS B 552 CE NZ
REMARK 470 GLN B 563 CG CD OE1 NE2
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 86 76.44 -157.19
REMARK 500 ASP A 161 -77.21 -96.14
REMARK 500 ALA A 163 -82.68 -93.74
REMARK 500 PRO A 190 36.66 -99.77
REMARK 500 CYS A 315 -153.99 -123.47
REMARK 500 SER A 389 -163.70 -119.45
REMARK 500 LEU A 478 -81.28 -89.23
REMARK 500 ALA A 523 -137.92 -106.56
REMARK 500 ARG A 524 -134.99 45.92
REMARK 500 ASN B 86 75.60 -154.81
REMARK 500 ASP B 161 -75.96 -96.00
REMARK 500 ALA B 163 -81.37 -95.10
REMARK 500 PRO B 190 35.82 -97.24
REMARK 500 CYS B 315 -153.23 -125.24
REMARK 500 SER B 389 -162.61 -118.90
REMARK 500 LEU B 478 -78.35 -88.21
REMARK 500 ALA B 523 -138.35 -107.26
REMARK 500 ARG B 524 -134.37 46.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NAD A 1518
REMARK 615 NAD B 1517
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 564
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 1518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 1517
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V9G RELATED DB: PDB
REMARK 900 HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE
REMARK 900 RELATED ID: 3V9H RELATED DB: PDB
REMARK 900 HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE MUTANT S352A
REMARK 900 RELATED ID: 3V9I RELATED DB: PDB
REMARK 900 HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE MUTANT S352L
REMARK 900 RELATED ID: 3V9J RELATED DB: PDB
REMARK 900 MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE COMPLEXED WITH
REMARK 900 SULFATE ION
REMARK 900 RELATED ID: 3V9K RELATED DB: PDB
REMARK 900 MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE COMPLEXED WITH THE
REMARK 900 PRODUCT GLUTAMATE
DBREF 3V9L A 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
DBREF 3V9L B 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
SEQADV 3V9L MET A 1 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY A 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER A 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER A 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER A 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER A 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY A 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L LEU A 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L VAL A 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L PRO A 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L ARG A 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY A 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER A 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS A 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L MET A 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L ALA A 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 3V9L THR A 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 3V9L LYS A 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQADV 3V9L MET B 1 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY B 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER B 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER B 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER B 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER B 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY B 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L LEU B 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L VAL B 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L PRO B 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L ARG B 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L GLY B 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L SER B 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L HIS B 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L MET B 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 3V9L ALA B 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 3V9L THR B 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 3V9L LYS B 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQRES 1 A 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 A 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 A 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 A 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 A 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 A 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 A 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 A 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 A 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 A 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 A 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 A 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 A 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 A 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 A 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 A 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 A 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 A 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 A 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 A 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 A 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 A 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 A 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 A 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 A 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 A 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 A 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 A 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 A 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 A 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 A 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 A 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 A 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 A 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 A 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 A 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 A 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 A 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 A 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 A 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 A 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 A 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 A 563 SER TYR MET GLN
SEQRES 1 B 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 B 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 B 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 B 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 B 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 B 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 B 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 B 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 B 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 B 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 B 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 B 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 B 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 B 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 B 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 B 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 B 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 B 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 B 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 B 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 B 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 B 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 B 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 B 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 B 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 B 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 B 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 B 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 B 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 B 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 B 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 B 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 B 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 B 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 B 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 B 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 B 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 B 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 B 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 B 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 B 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 B 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 B 563 SER TYR MET GLN
HET GOL A 564 6
HET GOL A 565 6
HET NAD A1518 44
HET NAD B1517 44
HETNAM GOL GLYCEROL
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 NAD 2(C21 H27 N7 O14 P2)
FORMUL 7 HOH *872(H2 O)
HELIX 1 1 SER A 44 LYS A 58 1 15
HELIX 2 2 ASP A 98 LYS A 119 1 22
HELIX 3 3 PRO A 120 GLY A 137 1 18
HELIX 4 4 ARG A 139 GLY A 152 1 14
HELIX 5 5 THR A 154 ALA A 163 1 10
HELIX 6 6 ALA A 163 GLU A 181 1 19
HELIX 7 7 PHE A 212 MET A 226 1 15
HELIX 8 8 SER A 235 THR A 237 5 3
HELIX 9 9 ALA A 238 ALA A 252 1 15
HELIX 10 10 ASP A 265 SER A 275 1 11
HELIX 11 11 SER A 287 ASN A 301 1 15
HELIX 12 12 LEU A 302 PHE A 305 5 4
HELIX 13 13 ASP A 328 GLU A 342 1 15
HELIX 14 14 TYR A 343 GLN A 346 5 4
HELIX 15 15 LEU A 360 ILE A 375 1 16
HELIX 16 16 ASP A 393 SER A 410 1 18
HELIX 17 17 GLU A 441 LYS A 445 5 5
HELIX 18 18 PRO A 459 ASP A 461 5 3
HELIX 19 19 LYS A 462 THR A 473 1 12
HELIX 20 20 ASP A 486 LEU A 497 1 12
HELIX 21 21 HIS A 536 ARG A 540 5 5
HELIX 22 22 TYR A 559 GLN A 563 5 5
HELIX 23 23 SER B 44 LYS B 58 1 15
HELIX 24 24 ASP B 98 LYS B 119 1 22
HELIX 25 25 PRO B 120 GLY B 137 1 18
HELIX 26 26 ARG B 139 GLY B 152 1 14
HELIX 27 27 THR B 154 ALA B 162 1 9
HELIX 28 28 ALA B 163 GLU B 181 1 19
HELIX 29 29 PHE B 212 MET B 226 1 15
HELIX 30 30 SER B 235 THR B 237 5 3
HELIX 31 31 ALA B 238 ALA B 252 1 15
HELIX 32 32 ASP B 265 SER B 275 1 11
HELIX 33 33 SER B 287 ASN B 301 1 15
HELIX 34 34 LEU B 302 PHE B 305 5 4
HELIX 35 35 ASP B 328 GLU B 342 1 15
HELIX 36 36 TYR B 343 GLN B 346 5 4
HELIX 37 37 LEU B 360 SER B 373 1 14
HELIX 38 38 ASP B 393 SER B 410 1 18
HELIX 39 39 GLU B 441 LYS B 445 5 5
HELIX 40 40 PRO B 459 ASP B 461 5 3
HELIX 41 41 LYS B 462 THR B 473 1 12
HELIX 42 42 ASP B 486 LEU B 497 1 12
HELIX 43 43 HIS B 536 THR B 542 5 7
HELIX 44 44 TYR B 559 GLN B 563 5 5
SHEET 1 A 3 GLU A 62 ALA A 63 0
SHEET 2 A 3 ASN A 86 CYS A 95 1 O LYS A 93 N GLU A 62
SHEET 3 A 3 ILE A 78 SER A 83 -1 N GLN A 79 O PHE A 94
SHEET 1 B 2 CYS A 66 VAL A 68 0
SHEET 2 B 2 GLU A 71 VAL A 73 -1 O VAL A 73 N CYS A 66
SHEET 1 C 9 SER A 191 GLY A 199 0
SHEET 2 C 9 THR A 542 THR A 550 -1 O GLN A 545 N VAL A 196
SHEET 3 C 9 ASN B 503 ILE B 506 1 O ILE B 506 N LYS A 548
SHEET 4 C 9 THR B 479 PHE B 483 1 N VAL B 482 O TYR B 505
SHEET 5 C 9 ASN B 319 VAL B 323 1 N PHE B 322 O ALA B 481
SHEET 6 C 9 CYS B 351 PRO B 357 1 O TYR B 355 N VAL B 323
SHEET 7 C 9 VAL B 452 TYR B 458 1 O TYR B 456 N LEU B 354
SHEET 8 C 9 CYS B 432 SER B 436 1 N ILE B 434 O VAL B 455
SHEET 9 C 9 LEU B 413 ALA B 417 -1 N SER B 414 O GLU B 435
SHEET 1 D 5 ILE A 259 PHE A 261 0
SHEET 2 D 5 VAL A 229 LYS A 233 1 N VAL A 230 O GLN A 260
SHEET 3 D 5 PHE A 203 ILE A 207 1 N ALA A 206 O LEU A 231
SHEET 4 D 5 LEU A 279 THR A 285 1 O ASN A 283 N ALA A 205
SHEET 5 D 5 ARG A 310 GLU A 314 1 O ALA A 312 N PHE A 284
SHEET 1 E 9 LEU A 413 ALA A 417 0
SHEET 2 E 9 CYS A 432 SER A 436 -1 O GLU A 435 N SER A 414
SHEET 3 E 9 VAL A 452 TYR A 458 1 O LEU A 453 N ILE A 434
SHEET 4 E 9 CYS A 351 PRO A 357 1 N LEU A 354 O TYR A 456
SHEET 5 E 9 ASN A 319 VAL A 323 1 N VAL A 323 O TYR A 355
SHEET 6 E 9 THR A 479 PHE A 483 1 O ALA A 481 N PHE A 322
SHEET 7 E 9 ASN A 503 ILE A 506 1 O TYR A 505 N VAL A 482
SHEET 8 E 9 GLN B 545 THR B 550 1 O LYS B 548 N ILE A 506
SHEET 9 E 9 SER B 191 VAL B 196 -1 N VAL B 196 O GLN B 545
SHEET 1 F 2 CYS A 421 ASN A 422 0
SHEET 2 F 2 TYR A 428 VAL A 429 -1 O TYR A 428 N ASN A 422
SHEET 1 G 2 TYR A 476 GLY A 477 0
SHEET 2 G 2 ALA A 523 ARG A 524 -1 N ALA A 523 O GLY A 477
SHEET 1 H 3 GLU B 62 ILE B 64 0
SHEET 2 H 3 ASN B 86 CYS B 95 1 O LYS B 93 N ILE B 64
SHEET 3 H 3 ILE B 78 SER B 83 -1 N GLN B 79 O PHE B 94
SHEET 1 I 2 CYS B 66 VAL B 68 0
SHEET 2 I 2 GLU B 71 VAL B 73 -1 O VAL B 73 N CYS B 66
SHEET 1 J 5 ILE B 259 PHE B 261 0
SHEET 2 J 5 VAL B 229 LYS B 233 1 N VAL B 230 O GLN B 260
SHEET 3 J 5 PHE B 203 ILE B 207 1 N ALA B 206 O LYS B 233
SHEET 4 J 5 LEU B 279 THR B 285 1 O ASN B 283 N ALA B 205
SHEET 5 J 5 ARG B 310 GLU B 314 1 O ALA B 312 N PHE B 284
SHEET 1 K 2 CYS B 421 ASN B 422 0
SHEET 2 K 2 TYR B 428 VAL B 429 -1 O TYR B 428 N ASN B 422
SHEET 1 L 2 TYR B 476 GLY B 477 0
SHEET 2 L 2 ALA B 523 ARG B 524 -1 O ALA B 523 N GLY B 477
CISPEP 1 PRO A 189 PRO A 190 0 6.13
CISPEP 2 PRO B 189 PRO B 190 0 5.54
SITE 1 AC1 7 CYS A 421 ASN A 422 TYR A 428 GLU A 430
SITE 2 AC1 7 PRO B 459 ASP B 461 LYS B 462
SITE 1 AC2 8 ARG A 408 SER A 409 PRO A 411 HOH A 918
SITE 2 AC2 8 ASP B 77 TYR B 96 ASP B 265 THR B 268
SITE 1 AC3 13 ILE A 207 SER A 208 LYS A 233 GLY A 266
SITE 2 AC3 13 PRO A 267 GLY A 270 PHE A 284 SER A 287
SITE 3 AC3 13 THR A 290 LEU A 294 HOH A 670 HOH A 973
SITE 4 AC3 13 HOH A1044
SITE 1 AC4 15 ILE B 207 SER B 208 LYS B 233 GLY B 266
SITE 2 AC4 15 PRO B 267 GLY B 270 PHE B 284 GLY B 286
SITE 3 AC4 15 SER B 287 THR B 290 HIS B 293 LEU B 294
SITE 4 AC4 15 HOH B 952 HOH B1045 HOH B1059
CRYST1 84.888 94.053 132.425 90.00 90.00 90.00 P 21 21 21 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 0.011780 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007551 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
